EzCatDB: S00334
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeS00334
CATH domainDomain 13.40.50.720 : Rossmann foldCatalytic domain
E.C.1.3.1.9
CSA1mfp,1qsg

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109

Enzyme Name
UniProtKBKEGG

P80030P0AEK4P0A5Y7P0A5Y6
Protein nameEnoyl-{acyl-carrier-protein} reductase {NADH}, chloroplasticEnoyl-{acyl-carrier-protein} reductase {NADH}Enoyl-{acyl-carrier-protein} reductase {NADH}Enoyl-{acyl-carrier-protein} reductase {NADH}enoyl-[acyl-carrier-protein] reductase (NADH)
enoyl-[acyl carrier protein] reductase
enoyl-ACP reductase
NADH-enoyl acyl carrier protein reductase
NADH-specific enoyl-ACP reductase
enoyl-[acyl-carrier-protein] reductase (NADH)
acyl-[acyl-carrier-protein]:NAD+ oxidoreductase
SynonymsEC 1.3.1.9
NADH-dependent enoyl-ACP reductase
EC 1.3.1.9
NADH-dependent enoyl-ACP reductase
EC 1.3.1.9
NADH-dependent enoyl-ACP reductase
EC 1.3.1.9
NADH-dependent enoyl-ACP reductase
RefSeq
NP_415804.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489556.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
NP_855172.1 (Protein)
NC_002945.3 (DNA/RNA sequence)
NP_216000.1 (Protein)
NC_000962.3 (DNA/RNA sequence)
NP_335982.1 (Protein)
NC_002755.2 (DNA/RNA sequence)
YP_006514868.1 (Protein)
NC_018143.1 (DNA/RNA sequence)

KEGG pathways
MAP codePathways
MAP00061Fatty acid biosynthesis

UniProtKB:Accession NumberP80030P0AEK4P0A5Y7P0A5Y6
Entry nameFABI_BRANAFABI_ECOLIINHA_MYCBOINHA_MYCTU
ActivityAcyl-[acyl-carrier-protein] + NAD(+) = trans- 2,3-dehydroacyl-[acyl-carrier-protein] + NADH.Acyl-[acyl-carrier-protein] + NAD(+) = trans- 2,3-dehydroacyl-[acyl-carrier-protein] + NADH.Acyl-[acyl-carrier-protein] + NAD(+) = trans- 2,3-dehydroacyl-[acyl-carrier-protein] + NADH.Acyl-[acyl-carrier-protein] + NAD(+) = trans- 2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
SubunitHomotetramer.Homotetramer.Homotetramer (By similarity).Homotetramer.
Subcellular locationPlastid, chloroplast.Cell inner membrane, Peripheral membrane protein.

Cofactor




Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00173C00003C00693C00004C00080
CompoundAcyl-[acyl-carrier protein]NAD+trans-2,3-Dehydroacyl-[acyl-carrier protein]NADHH+
Typecarbohydrate,peptide/protein,phosphate group/phosphate ion,sulfide groupamide group,amine group,nucleotidecarbohydrate,peptide/protein,phosphate group/phosphate ion,sulfide groupamide group,amine group,nucleotideothers
ChEBI
15846

16908
15378
PubChem
5893

439153
1038
             
1bvrAAnalogue:THTBound:NADUnboundUnbound 
1bvrBAnalogue:THTBound:NADUnboundUnbound 
1bvrCAnalogue:THTBound:NADUnboundUnbound 
1bvrDUnboundBound:NADUnboundUnbound 
1bvrEUnboundBound:NADUnboundUnbound 
1bvrFAnalogue:THTBound:NADUnboundUnbound 
1c14AUnboundBound:NADUnboundUnbound 
1c14BUnboundBound:NADUnboundUnbound 
1cwuAUnboundAnalogue:NAD-TDBUnboundUnbound 
1cwuBUnboundAnalogue:NAD-TDBUnboundUnbound 
1d7oAUnboundBound:NADUnboundUnbound 
1d8aAUnboundBound:NADUnboundUnbound 
1d8aBUnboundBound:NADUnboundUnbound 
1dfgAUnboundAnalogue:NAD-NDTUnboundUnbound 
1dfgBUnboundAnalogue:NAD-NDTUnboundUnbound 
1dfhAUnboundAnalogue:NAD-TDBUnboundUnbound 
1dfhBUnboundAnalogue:NAD-TDBUnboundUnbound 
1dfiAUnboundBound:NADUnboundUnbound 
1dfiBUnboundBound:NADUnboundUnbound 
1dfiCUnboundBound:NADUnboundUnbound 
1dfiDUnboundBound:NADUnboundUnbound 
1enoAUnboundBound:NADUnboundUnbound 
1enpAUnboundUnboundUnboundBound:NAD 
1enyAUnboundBound:NADUnboundUnbound 
1enzAUnboundBound:NADUnboundUnbound 
1i2zAUnboundBound:NADUnboundUnbound 
1i2zBUnboundBound:NADUnboundUnbound 
1i30AUnboundBound:NADUnboundUnbound 
1i30BUnboundBound:NADUnboundUnbound 
1lx6AAnalogue:ZAMBound:NADUnboundUnbound 
1lx6BAnalogue:ZAMBound:NADUnboundUnbound 
1lxcAAnalogue:AYMBound:NADUnboundUnbound 
1lxcBAnalogue:AYMBound:NADUnboundUnbound 
1mfpAAnalogue:IDNBound:NADUnboundUnbound 
1mfpBAnalogue:IDNBound:NADUnboundUnbound 
1p44AUnboundBound:NADUnboundUnbound 
1p44BUnboundBound:NADUnboundUnbound 
1p44CUnboundBound:NADUnboundUnbound 
1p44DUnboundBound:NADUnboundUnbound 
1p44EUnboundBound:NADUnboundUnbound 
1p44FUnboundBound:NADUnboundUnbound 
1p45AUnboundBound:NADUnboundUnbound 
1p45BUnboundBound:NADUnboundUnbound 
1qg6AUnboundBound:NADUnboundUnbound 
1qg6BUnboundBound:NADUnboundUnbound 
1qg6CUnboundBound:NADUnboundUnbound 
1qg6DUnboundBound:NADUnboundUnbound 
1qsgAUnboundBound:NADUnboundUnbound 
1qsgBUnboundBound:NADUnboundUnbound 
1qsgCUnboundBound:NADUnboundUnbound 
1qsgDUnboundBound:NADUnboundUnbound 
1qsgEUnboundBound:NADUnboundUnbound 
1qsgFUnboundBound:NADUnboundUnbound 
1qsgGUnboundBound:NADUnboundUnbound 
1qsgHUnboundBound:NADUnboundUnbound 
1zidAUnboundAnalogue:ZIDUnboundUnbound 

Active-site residues
resource
literature [6], [9], [11]
pdbCatalytic residuescomment
          
1bvrATYR  158
 
1bvrBTYR  158
 
1bvrCTYR  158
 
1bvrDTYR  158
 
1bvrETYR  158
 
1bvrFTYR  158
 
1c14ATYR  156
 
1c14BTYR 1156
 
1cwuATYR  198
mutant A138G
1cwuBTYR  198
mutant A138G
1d7oATYR  198
 
1d8aATYR  156
 
1d8aBTYR  156
 
1dfgATYR  156
 
1dfgBTYR  156
 
1dfhATYR  156
 
1dfhBTYR  156
 
1dfiATYR  156
 
1dfiBTYR  156
 
1dfiCTYR  156
 
1dfiDTYR  156
 
1enoATYR  198
mutant S1A
1enpATYR  198
mutant S1A
1enyATYR  158
 
1enzATYR  158
mutant S94A
1i2zATYR  156
 
1i2zBTYR 1156
 
1i30ATYR  156
 
1i30BTYR 1156
 
1lx6ATYR  156
 
1lx6BTYR  156
 
1lxcATYR  156
 
1lxcBTYR  156
 
1mfpATYR  156
 
1mfpBTYR 1156
 
1p44ATYR  158
 
1p44BTYR  158
 
1p44CTYR  158
 
1p44DTYR  158
 
1p44ETYR  158
 
1p44FTYR  158
 
1p45ATYR  158
 
1p45BTYR  158
 
1qg6ATYR  156
 
1qg6BTYR  156
 
1qg6CTYR  156
 
1qg6DTYR  156
 
1qsgATYR  156
 
1qsgBTYR  156
 
1qsgCTYR  156
 
1qsgDTYR  156
 
1qsgETYR  156
 
1qsgFTYR  156
 
1qsgGTYR  156
 
1qsgHTYR  156
 
1zidATYR  158
mutant T2A

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]Fig.8, p.932-933
[8]Fig.8, p.1539-1541
[10]p.13628-13629
[11]

[13]p.30817
[14]p.15587-15588
[16]


references
[1]
PubMed ID3535882
JournalBiochemistry
Year1986
Volume25
Pages5617-24
AuthorsLeanz GF, Hammes GG
TitleKinetic and nuclear magnetic resonance study of the interaction of NADP+ and NADPH with chicken liver fatty acid synthase.
[2]
PubMed ID8126737
JournalJ Mol Biol
Year1994
Volume237
Pages240-2
AuthorsRafferty JB, Simon JW, Stuitje AR, Slabas AR, Fawcett T, Rice DW
TitleCrystallization of the NADH-specific enoyl acyl carrier protein reductase from Brassica napus.
[3]
PubMed ID7932735
JournalJ Mol Biol
Year1994
Volume243
Pages126-7
AuthorsWagner UG, Bergler H, Fuchsbichler S, Turnowsky F, Hogenauer G, Kratky C
TitleCrystallization and preliminary X-ray diffraction studies of the enoyl-ACP reductase from Escherichia coli.
[4]
CommentsX-ray crystallography
PubMed ID7886450
JournalScience
Year1995
Volume267
Pages1638-41
AuthorsDessen A, Quemard A, Blanchard JS, Jacobs WR Jr, Sacchettini JC
TitleCrystal structure and function of the isoniazid target of Mycobacterium tuberculosis.
Related PDB1eny,1enz
[5]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 74-382.
Medline ID96097399
PubMed ID8535786
JournalStructure
Year1995
Volume3
Pages927-38
AuthorsRafferty JB, Simon JW, Baldock C, Artymiuk PJ, Baker PJ, Stuitje AR, Slabas AR, Rice DW
TitleCommon themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase.
Related PDB1eno,1enp
Related UniProtKBP80030
[6]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID97113207
PubMed ID8953047
JournalScience
Year1996
Volume274
Pages2107-10
AuthorsBaldock C, Rafferty JB, Sedelnikova SE, Baker PJ, Stuitje AR, Slabas AR, Hawkes TR, Rice DW
TitleA mechanism of drug action revealed by structural studies of enoyl reductase.
Related PDB1dfg,1dfh,1dfi
Related UniProtKBP0AEK4
[7]
PubMed ID9204389
JournalJ Enzyme Inhib
Year1997
Volume11
Pages209-16
AuthorsMukherjee S, Katiyar SS
TitleEvidence for the essential histidine at the NADPH binding site of enoyl-CoA reductase domain of pigeon liver fatty acid synthetase.
[8]
PubMed ID9878369
JournalJ Mol Biol
Year1998
Volume284
Pages1529-46
AuthorsBaldock C, Rafferty JB, Stuitje AR, Slabas AR, Rice DW
TitleThe X-ray structure of Escherichia coli enoyl reductase with bound NAD+ at 2.1 A resolution.
[9]
CommentsX-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
Medline ID98079172
PubMed ID9417034
JournalScience
Year1998
Volume279
Pages98-102
AuthorsRozwarski DA, Grant GA, Barton DH, Jacobs WR Jr, Sacchettini JC
TitleModification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis.
Related PDB1zid
Related UniProtKBP46533
[10]
PubMed ID10521269
JournalBiochemistry
Year1999
Volume38
Pages13623-34
AuthorsParikh S, Moynihan DP, Xiao G, Tonge PJ
TitleRoles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis.
[11]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID99425142
PubMed ID10493822
JournalBiochemistry
Year1999
Volume38
Pages12514-25
AuthorsWard WH, Holdgate GA, Rowsell S, McLean EG, Pauptit RA, Clayton E, Nichols WW, Colls JG, Minshull CA, Jude DA, Mistry A, Timms D, Camble R, Hales NJ, Britton CJ, Taylor IW
TitleKinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan.
Related PDB1qg6
Related UniProtKBP0AEK4
[12]
PubMed ID10196195
JournalJ Biol Chem
Year1999
Volume274
Pages11110-4
AuthorsHeath RJ, Rubin JR, Holland DR, Zhang E, Snow ME, Rock CO
TitleMechanism of triclosan inhibition of bacterial fatty acid synthesis.
[13]
CommentsX-ray crystallography
PubMed ID10521472
JournalJ Biol Chem
Year1999
Volume274
Pages30811-7
AuthorsRoujeinikova A, Sedelnikova S, de Boer GJ, Stuitje AR, Slabas AR, Rafferty JB, Rice DW
TitleInhibitor binding studies on enoyl reductase reveal conformational changes related to substrate recognition.
Related PDB1cwu
[14]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID99269096
PubMed ID10336454
JournalJ Biol Chem
Year1999
Volume274
Pages15582-9
AuthorsRozwarski DA, Vilcheze C, Sugantino M, Bittman R, Sacchettini JC
TitleCrystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate.
Related PDB1bvr
Related UniProtKBP46533
[15]
CommentsX-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 84-380.
Medline ID20079515
PubMed ID10610777
JournalJ Mol Biol
Year1999
Volume294
Pages527-35
AuthorsRoujeinikova A, Levy CW, Rowsell S, Sedelnikova S, Baker PJ, Minshull CA, Mistry A, Colls JG, Camble R, Stuitje AR, Slabas AR, Rafferty JB, Pauptit RA, Viner R, Rice DW
TitleCrystallographic analysis of triclosan bound to enoyl reductase.
Related PDB1d7o
Related UniProtKBP80030
[16]
CommentsX-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
Medline ID99329134
PubMed ID10398587
JournalJ Mol Biol
Year1999
Volume290
Pages859-65
AuthorsStewart MJ, Parikh S, Xiao G, Tonge PJ, Kisker C
TitleStructural basis and mechanism of enoyl reductase inhibition by triclosan.
Related PDB1qsg
Related UniProtKBP0AEK4
[17]
PubMed ID10027962
JournalMol Microbiol
Year1999
Volume31
Pages443-50
Authorsde Boer GJ, Pielage GJ, Nijkamp HJ, Slabas AR, Rafferty JB, Baldock C, Rice DW, Stuitje AR
TitleMolecular genetic analysis of enoyl-acyl carrier protein reductase inhibition by diazaborine.
[18]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Medline ID99215552
PubMed ID10201369
JournalNature
Year1999
Volume398
Pages383-4
AuthorsLevy CW, Roujeinikova A, Sedelnikova S, Baker PJ, Stuitje AR, Slabas AR, Rice DW, Rafferty JB
TitleMolecular basis of triclosan activity.
Related PDB1d8a
Related UniProtKBP0AEK4
[19]
CommentsX-ray crystallography
PubMed ID10595560
JournalProtein Sci
Year1999
Volume8
Pages2529-32
AuthorsQiu X, Janson CA, Court RI, Smyth MG, Payne DJ, Abdel-Meguid SS
TitleMolecular basis for triclosan activity involves a flipping loop in the active site.
Related PDB1c14
[20]
PubMed ID11068033
JournalFEBS Lett
Year2000
Volume484
Pages65-8
AuthorsFawcett T, Copse CL, Simon JW, Slabas AR
TitleKinetic mechanism of NADH-enoyl-ACP reductase from Brassica napus.
[21]
CommentsX-ray crystallography
PubMed ID11514139
JournalBioorg Med Chem Lett
Year2001
Volume11
Pages2061-5
AuthorsHeerding DA, Chan G, DeWolf WE, Fosberry AP, Janson CA, Jaworski DD, McManus E, Miller WH, Moore TD, Payne DJ, Qiu X, Rittenhouse SF, Slater-Radosti C, Smith W, Takata DT, Vaidya KS, Yuan CC, Huffman WF
Title1,4-Disubstituted imidazoles are potential antibacterial agents functioning as inhibitors of enoyl acyl carrier protein reductase (FabI).
Related PDB1i2z,1i30
[22]
PubMed ID11491286
JournalJ Mol Biol
Year2001
Volume309
Pages171-80
AuthorsLevy CW, Baldock C, Wallace AJ, Sedelnikova S, Viner RC, Clough JM, Stuitje AR, Slabas AR, Rice DW, Rafferty JB
TitleA study of the structure-activity relationship for diazaborine inhibition of Escherichia coli enoyl-ACP reductase.
[23]
PubMed ID11552685
JournalJ Mol Graph Model
Year2001
Volume19
Pages560-70
AuthorsChen YZ, Gu XL, Cao ZW
TitleCan an optimization/scoring procedure in ligand-protein docking be employed to probe drug-resistant mutations in proteins?
[24]
PubMed ID12459184
JournalBiochem Biophys Res Commun
Year2002
Volume299
Pages621-7
AuthorsLee IH, Kim EJ, Cho YH, Lee JK
TitleCharacterization of a novel enoyl-acyl carrier protein reductase of diazaborine-resistant Rhodobacter sphaeroides mutant.
[25]
PubMed ID11792710
JournalJ Biol Chem
Year2002
Volume277
Pages13106-14
AuthorsPerozzo R, Kuo M, Sidhu AS, Valiyaveettil JT, Bittman R, Jacobs WR Jr, Fidock DA, Sacchettini JC
TitleStructural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase.
[26]
PubMed ID12109908
JournalJ Med Chem
Year2002
Volume45
Pages3246-56
AuthorsMiller WH, Seefeld MA, Newlander KA, Uzinskas IN, Burgess WJ, Heerding DA, Yuan CC, Head MS, Payne DJ, Rittenhouse SF, Moore TD, Pearson SC, Berry V, DeWolf WE Jr, Keller PM, Polizzi BJ, Qiu X, Janson CA, Huffman WF
TitleDiscovery of aminopyridine-based inhibitors of bacterial enoyl-ACP reductase (FabI).
[27]
CommentsX-ray crystallography
PubMed ID12606558
JournalJ Biol Chem
Year2003
Volume278
Pages20851-9
AuthorsKuo MR, Morbidoni HR, Alland D, Sneddon SF, Gourlie BB, Staveski MM, Leonard M, Gregory JS, Janjigian AD, Yee C, Musser JM, Kreiswirth B, Iwamoto H, Perozzo R, Jacobs WR Jr, Sacchettini JC, Fidock DA
TitleTargeting tuberculosis and malaria through inhibition of Enoyl reductase: compound activity and structural data.
Related PDB1p44,1p45
[28]
PubMed ID12529157
JournalJ Biomol Struct Dyn
Year2003
Volume20
Pages589-94
AuthorsMuralidharan J, Suguna K, Surolia A, Surolia N
TitleExploring the interaction energies for the binding of hydroxydiphenyl ethers to enoyl-acyl carrier protein reductases.
[29]
CommentsX-ray crystallography
PubMed ID12699381
JournalJ Med Chem
Year2003
Volume46
Pages1627-35
AuthorsSeefeld MA, Miller WH, Newlander KA, Burgess WJ, DeWolf WE Jr, Elkins PA, Head MS, Jakas DR, Janson CA, Keller PM, Manley PJ, Moore TD, Payne DJ, Pearson S, Polizzi BJ, Qiu X, Rittenhouse SF, Uzinskas IN, Wallis NG, Huffman WF
TitleIndole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases FabI and FabK.
Related PDB1mfp
[30]
PubMed ID15491144
JournalBiochemistry
Year2004
Volume43
Pages13380-9
AuthorsProtasevich II, Brouillette CG, Snow ME, Dunham S, Rubin JR, Gogliotti R, Siegel K
TitleRole of inhibitor aliphatic chain in the thermodynamics of inhibitor binding to Escherichia coli enoyl-ACP reductase and the Phe203Leu mutant: a proposed mechanism for drug resistance.
[31]
PubMed ID15381426
JournalJ Mol Biol
Year2004
Volume343
Pages147-55
AuthorsPidugu LS, Kapoor M, Surolia N, Surolia A, Suguna K
TitleStructural basis for the variation in triclosan affinity to enoyl reductases.


createdupdated
2005-04-112012-06-01


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.