EzCatDB: M00133
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DB codeM00133
RLCP classification1.13.30000.10 : Hydrolysis
CATH domainDomain 14.10.740.10 : Coagulation Factor IX
Domain 22.10.25.10 : Laminin
Domain 32.10.25.10 : Laminin
Domain 42.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 52.40.10.10 : Thrombin, subunit HCatalytic domain
E.C.3.4.21.22

CATH domainRelated DB codes (homologues)
2.10.25.10 : LamininM00139,M00212,M00152,M00155,M00315,M00316
2.40.10.10 : Thrombin, subunit HM00139,D00214,M00167,D00426,D00428,D00429,D00430,D00431,D00432,D00433,D00434,D00435,M00227,M00209,D00194,D00197,D00211,D00212,D00216,M00212,D00224,D00497,M00217,M00216,D00528,D00848,D00850,D00851,D00852,D00855,M00152,M00155,M00157,M00181,M00315,M00316,M00317,M00348,M00349,T00074,T00410,T00411

Enzyme Name
UniProtKBKEGG

P16293P00741P00740
Protein nameCoagulation factor IXCoagulation factor IXCoagulation factor IXcoagulation factor IXa
activated Christmas factor
blood-coagulation factor IXa
activated blood-coagulation factor IX
autoprothrombin II
blood platelet cofactor II
activated blood coagulation factor XI
SynonymsEC 3.4.21.22
Christmas factor
EC 3.4.21.22
Christmas factor
EC 3.4.21.22
Christmas factor
Plasma thromboplastin component
PTC
ContainsCoagulation factor IXa light chain
Coagulation factor IXa heavy chain
Coagulation factor IXa light chain
Coagulation factor IXa heavy chain
Coagulation factor IXa light chain
Coagulation factor IXa heavy chain
RefSeq

NP_000124.1 (Protein)
NM_000133.3 (DNA/RNA sequence)
MEROPSS01.214 (Serine)
S01.214 (Serine)
S01.214 (Serine)
PfamPF00008 (EGF)
PF00594 (Gla)
PF00089 (Trypsin)
[Graphical view]
PF00008 (EGF)
PF00594 (Gla)
PF00089 (Trypsin)
[Graphical view]
PF00008 (EGF)
PF00594 (Gla)
PF00089 (Trypsin)
[Graphical view]


UniProtKB:Accession NumberP16293P00741P00740
Entry nameFA9_PIGFA9_BOVINFA9_HUMAN
ActivitySelective cleavage of Arg-|-Ile bond in factor X to form factor Xa.Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.
SubunitHeterodimer of a light chain and a heavy chain, disulfide-linked.Heterodimer of a light chain and a heavy chain, disulfide-linked.Heterodimer of a light chain and a heavy chain, disulfide-linked.
Subcellular locationSecreted.Secreted.Secreted.
Cofactor



Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC01038C00001C01065I00087I00085I00086
CompoundCoagulation Factor XH2OCoagulation Factor XaPeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinH2Opeptide/protein


ChEBI
15377




PubChem
962
22247451




              
1pfxC01Unbound UnboundUnboundIntermediate-analogue:PHE-PRO-ARG(chain I)Unbound
1rfnA01Unbound UnboundUnboundUnboundUnbound
1pfxC02Unbound UnboundUnboundUnboundUnbound
1rfnA02Unbound UnboundUnboundUnboundUnbound
1pfxL01Unbound UnboundUnboundUnboundUnbound
1pfxL02Unbound UnboundUnboundUnboundUnbound
1rfnBUnbound UnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P00741,P16293
pdbCatalytic residuesMain-chain involved in catalysis
          
1pfxC01SER 195
GLY 193;SER 195
1rfnA01SER 195
GLY 193;SER 195
1pfxC02HIS  57;ASP 102
 
1rfnA02HIS  57;ASP 102
 
1pfxL01 
 
1pfxL02 
 
1rfnB 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.9797

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID96003866
PubMed ID7568220
JournalProc Natl Acad Sci U S A
Year1995
Volume92
Pages9796-800
AuthorsBrandstetter H, Bauer M, Huber R, Lollar P, Bode W
TitleX-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B.
Related PDB1pfx
Related UniProtKBP16293
[2]
PubMed ID9235979
JournalBiochemistry
Year1997
Volume36
Pages9365-73
AuthorsParker ET, Pohl J, Blackburn MN, Lollar P
TitleSubunit structure and function of porcine factor Xa-activated factor VIII.
[3]
PubMed ID9668086
JournalJ Biol Chem
Year1998
Volume273
Pages19049-54
AuthorsFay PJ, Koshibu K
TitleThe A2 subunit of factor VIIIa modulates the active site of factor IXa.
[4]
PubMed ID9925787
JournalJ Mol Biol
Year1999
Volume285
Pages2089-104
AuthorsZhang E, St Charles R, Tulinsky A
TitleStructure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant.
[5]
PubMed ID10605707
JournalThromb Haemost
Year1999
Volume82
Pages218-25
AuthorsBajaj SP
TitleRegion of factor IXa protease domain that interacts with factor VIIIa: analysis of select hemophilia B mutants.
[6]
PubMed ID10595635
JournalThromb Haemost
Year1999
Volume82
Pages1443-5
AuthorsFeuerstein GZ, Toomey JR, Valocik R, Koster P, Patel A, Blackburn MN
TitleAn inhibitory anti-factor IX antibody effectively reduces thrombus formation in a rat model of venous thrombosis.
[7]
PubMed ID10467148
JournalStructure Fold Des
Year1999
Volume7
Pages989-96
AuthorsHopfner KP, Lang A, Karcher A, Sichler K, Kopetzki E, Brandstetter H, Huber R, Bode W, Engh RA
TitleCoagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding.
Related PDBP00740,1rfn

comments
This protein is composed of a heavy chain, with a trypsin-like serine protease domain (peptidase family-S1), and a light chain with two EGF-like domains. According to the literature [1], the catalytic heavy chain has a catalytic triad, composed of Ser/His/Asp, which is characteristic for trypsin-like serine proteases.

createdupdated
2004-03-172011-02-17


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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