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Database: UniProt
Entry: Q9V0I8
LinkDB: Q9V0I8
Original site: Q9V0I8 
ID   PURP_PYRAB              Reviewed;         337 AA.
AC   Q9V0I8; G8ZH06;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JAN-2019, entry version 102.
DE   RecName: Full=5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase {ECO:0000255|HAMAP-Rule:MF_01163};
DE            EC=6.3.4.23 {ECO:0000255|HAMAP-Rule:MF_01163};
DE   AltName: Full=5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate--formate ligase {ECO:0000255|HAMAP-Rule:MF_01163};
GN   Name=purP {ECO:0000255|HAMAP-Rule:MF_01163};
GN   OrderedLocusNames=PYRAB08010; ORFNames=PAB0547;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C.,
RA   Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic
RT   archaeon Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5
RT   and Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- FUNCTION: Catalyzes the ATP- and formate-dependent formylation of
CC       5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-
CC       monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-
CC       beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of
CC       folates. {ECO:0000255|HAMAP-Rule:MF_01163}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
CC         carboxamide + ATP + formate = 5-formamido-1-(5-phospho-D-
CC         ribosyl)imidazole-4-carboxamide + ADP + phosphate;
CC         Xref=Rhea:RHEA:24836, ChEBI:CHEBI:15740, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58467, ChEBI:CHEBI:58475,
CC         ChEBI:CHEBI:456216; EC=6.3.4.23; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01163};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (formate
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01163}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01163}.
DR   EMBL; AJ248285; CAB49715.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70201.1; -; Genomic_DNA.
DR   PIR; B75125; B75125.
DR   ProteinModelPortal; Q9V0I8; -.
DR   SMR; Q9V0I8; -.
DR   STRING; 272844.PAB0547; -.
DR   EnsemblBacteria; CAB49715; CAB49715; PAB0547.
DR   KEGG; pab:PAB0547; -.
DR   PATRIC; fig|272844.11.peg.844; -.
DR   eggNOG; arCOG04346; Archaea.
DR   eggNOG; COG1759; LUCA.
DR   HOGENOM; HOG000228474; -.
DR   KO; K06863; -.
DR   OMA; VKPHGAK; -.
DR   UniPathway; UPA00074; UER00134.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01163; IMP_biosynth_PurP; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR023656; IMP_biosynth_PurP.
DR   InterPro; IPR009720; IMP_biosynth_PurP_C.
DR   InterPro; IPR010672; IMP_biosynth_PurP_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR38147; PTHR38147; 1.
DR   Pfam; PF06849; DUF1246; 1.
DR   Pfam; PF06973; DUF1297; 1.
DR   PIRSF; PIRSF004602; ATPgrasp_PurP; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN         1    337       5-formaminoimidazole-4-carboxamide-1-
FT                                (beta)-D-ribofuranosyl 5'-monophosphate
FT                                synthetase.
FT                                /FTId=PRO_0000348635.
FT   DOMAIN       81    328       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   NP_BIND     125    185       ATP. {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   METAL       273    273       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   METAL       286    286       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   BINDING      14     14       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   BINDING      74     74       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   BINDING     207    207       ATP. {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   BINDING     235    235       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
SQ   SEQUENCE   337 AA;  38529 MW;  0876B8E0D865C1C9 CRC64;
     MVKIVVRIAT YASHSALQIL KGAKDEGFET IAFGSERVKP LYTKYFPVAD YFLVGKYPED
     ELLELNAVVI PTGSFVAHLG VELVERMKVP YFGNKRVLKW ESDRNLERKW LEKAKLKLPR
     VYDDPDDIDR PVIVKPHGAK GGRGYFIAKD PQDFWTKVEK FLGIKDKEDL KNVQIQEYVI
     GVPVYPHYFY SKLTRELELM SIDRRYESNV DAIGRIPSKD QLELELDITY TVIGNIPLVL
     RESLLMDVIE AGERTVKAAE ELMGGLWGPF CLEGVFTPDL DFVVFEISAR IVAGTNPFIN
     GSPYTWLKYD EPMSTGRRIA REIRLAIEED KLDEVVS
//
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