EzCatDB: S00841
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DB codeS00841
RLCP classification4.1514.818600.1130 : Addition
8.113.919760.1180 : Isomerization
CATH domainDomain 13.20.20.70 : TIM BarrelCatalytic domain
E.C.4.4.1.19

CATH domainRelated DB codes (homologues)
3.20.20.70 : TIM BarrelS00215,S00217,S00218,S00219,S00532,S00198,S00220,S00745,S00537,S00538,S00539,S00826,S00235,S00239,S00240,S00243,S00244,S00199,S00200,S00201,S00221,S00222,S00847,S00224,S00225,S00226,D00014,D00029,M00141,T00015,T00239,D00664,D00665,D00804,D00863,T00089

Enzyme Name
UniProtKBKEGG

Q57703O06739
Protein namePhosphosulfolactate synthasePhosphosulfolactate synthasePhosphosulfolactate synthase
(2R)-phospho-3-sulfolactate synthase
(2R)-O-phospho-3-sulfolactate sulfo-lyase
SynonymsEC 4.4.1.19
EC 4.4.1.19) ((2R)-phospho-3-sulfolactate synthase
PSL synthase
EC 4.4.1.19
EC 4.4.1.19) ((2R)-phospho-3-sulfolactate synthase
PSL synthase
RefSeqNP_247226.1 (Protein)
NC_000909.1 (DNA/RNA sequence)
NP_388976.1 (Protein)
NC_000964.3 (DNA/RNA sequence)
PfamPF02679 (ComA)
[Graphical view]
PF02679 (ComA)
[Graphical view]


UniProtKB:Accession NumberQ57703O06739
Entry nameCOMA_METJACOMA_BACSU
Activity(2R)-2-O-phospho-3-sulfolactate = phosphoenolpyruvate + hydrogen sulfite.(2R)-2-O-phospho-3-sulfolactate = phosphoenolpyruvate + hydrogen sulfite.
SubunitHomotrimer (Probable).
Subcellular location

CofactorMagnesium.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00305C00074C11481C11536
CompoundMagnesiumphosphoenolpyruvatehydrogen sulfite(2R)-2-O-phospho-3-sulfolactateEnolate intermediate
Typedivalent metal (Ca2+, Mg2+)carboxyl group,phosphate group/phosphate ionsulfitecarboxyl group,phosphate group/phosphate ion,sulfonate group
ChEBI18420
44897
17137
32896

PubChem888
59658623
58114173
1005
104748
443249

             
1qwgA00UnboundUnboundAnalogue:SO4 300UnboundUnbound
1u83A00UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [4]
pdbCatalytic residuesCofactor-binding residuescomment
           
1qwgA00LYS 137;ARG 170;ARG 244
GLU 103;GLU 133(Magnesium-1);GLU 168;GLU 205(Magnesium-2)
 
1u83A00LYS 139;       ;ARG 246
GLU 106;GLU 135(Magnesium-1);GLU 170;GLU 207(Magnesium-2)
invisible 141-146, 171-188

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]

[4]FIG.4, p.45862

references
[1]
PubMed ID10978150
JournalBiochemistry
Year2000
Volume39
Pages10662-76
AuthorsThompson TB, Garrett JB, Taylor EA, Meganathan R, Gerlt JA, Rayment I
TitleEvolution of enzymatic activity in the enolase superfamily: structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg2+ and o-succinylbenzoate.
Related PDB1fhv
[2]
CommentsCHARACTERIZATION, MUTAGENESIS OF LYS-137.
PubMed ID11830598
JournalJ Biol Chem
Year2002
Volume277
Pages13421-9
AuthorsGraham DE, Xu H, White RH
TitleIdentification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of sulfonate-biosynthesizing enzymes.
[3]
PubMed ID12013276
JournalNat Prod Rep
Year2002
Volume19
Pages133-47
AuthorsGraham DE, White RH
TitleElucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
PubMed ID12952952
JournalJ Biol Chem
Year2003
Volume278
Pages45858-63
AuthorsWise EL, Graham DE, White RH, Rayment I
TitleThe structural determination of phosphosulfolactate synthase from Methanococcus jannaschii at 1.7-A resolution: an enolase that is not an enolase.
Related PDB1qwg
Related UniProtKBQ57703

comments
According to the literature [4], although this enzyme does not belong to enolase superfamily(CATH 3.20.20.120), it catalyzes a similar reaction to those by the enolase homologues, which involves an enolate intermediate along with magnesium ion.
Although the literature [4] suggested that it is not a member of the enolase superfamily (CATH 3.20.20.120), some metal-binding residues can be superimposed with the corresponding residues of the enolase homologues, mandelate racemase (D00273 in EzCatDB), glucarate dehydratase (D00261) and chloromuconate cycloisomerase (D00283), using Matras program (by T. Kawabata).
According to the literature [2] and [4], this enzyme catalyzes two succsessive reactions, as follows
(A) Addition of sulfite to phosphoenolpyruvate(PEP), forming an enolate intermediate:
(B) Isomerization of the enolate intermediate, producing phosphosulfolactate:
More detailed mechanism might be as follows:
(A) Addition of sulfite to PEP, forming an enolate intermediate:
(A0) PEP must be stablized by two magnesium ions, through carboxylate oxygens of the intermediate.
(A1) Sulfite molecule, whose negative charge must be stabilized by Arg170 and Arg244' (from the adjacent subunit)(of 1qwg), makes a nucleophilic attack at the C3 atom of an unsaturated carboxylic acid, to form an enolate anion intermediate.
(B) Isomerization of the enolate intermediate, producing phosphosulfolactate:
(B0) The carboxyl group of the enolate intermediate must be stablized by two magnesium ions.
(B1) Lys137 (of 1qwg) may act as a general acid to protonate the C2 atom of the enolate intermediate.

createdupdated
2009-12-152010-02-08


Copyright: Nozomi Nagano, JST & CBRC-AIST
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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 - )
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