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Database: UniProt
Entry: P14027
LinkDB: P14027
Original site: P14027 
ID   PURP_METVS              Reviewed;         361 AA.
AC   P14027; A6UQ17; P14028;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 3.
DT   16-JAN-2019, entry version 111.
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=Mevan_0683;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 /
OS   OCM 148 / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci;
OC   Methanococcales; Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2475640; DOI=10.1007/BF02106178;
RA   Lechner K., Heller G., Boeck A.;
RT   "Organization and nucleotide sequence of a transcriptional unit of
RT   Methanococcus vannielii comprising genes for protein synthesis
RT   elongation factors and ribosomal proteins.";
RL   J. Mol. Evol. 29:20-27(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA34094.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
CC       Sequence=CAA34095.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
DR   EMBL; X15972; CAA34094.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X15972; CAA34095.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP000742; ABR54589.1; -; Genomic_DNA.
DR   PIR; S06626; QQMX3.
DR   PIR; S06627; QQMX4.
DR   RefSeq; WP_011972491.1; NC_009634.1.
DR   ProteinModelPortal; P14027; -.
DR   SMR; P14027; -.
DR   STRING; 406327.Mevan_0683; -.
DR   PRIDE; P14027; -.
DR   EnsemblBacteria; ABR54589; ABR54589; Mevan_0683.
DR   GeneID; 5324980; -.
DR   KEGG; mvn:Mevan_0683; -.
DR   eggNOG; arCOG04346; Archaea.
DR   eggNOG; COG1759; LUCA.
DR   HOGENOM; HOG000228474; -.
DR   KO; K06863; -.
DR   OMA; KFPGARG; -.
DR   OrthoDB; 21169at2157; -.
DR   BioCyc; MVAN406327:G1G99-704-MONOMER; -.
DR   UniPathway; UPA00074; UER00134.
DR   Proteomes; UP000001107; 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    361       5-formaminoimidazole-4-carboxamide-1-
FT                                (beta)-D-ribofuranosyl 5'-monophosphate
FT                                synthetase.
FT                                /FTId=PRO_0000148028.
FT   DOMAIN      116    348       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   NP_BIND     146    208       ATP. {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   METAL       297    297       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   METAL       310    310       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   BINDING      27     27       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   BINDING      94     94       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   BINDING     230    230       ATP. {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   BINDING     258    258       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
SQ   SEQUENCE   361 AA;  40683 MW;  DEAB7434509EF849 CRC64;
     MIPKEEIMGI FEKYNKDEIT IATVGSHTSL HILKGAKLEG FSTAVITTKD RDVPYKRFGV
     ADKFIYVDKF SDISSEEIQE QLREMNAIVV PHGSFIAYCG LDNVESTFKV PMFGNRAILR
     WEAERDLEGQ LLGGSGLRLP KKYNSPDEID GPVMVKFPGA RGGRGYFPCS STEEFWRKIN
     DFKAKGVLSE EDVKKAHIEE YVVGANYCIH YFYSPLKDRV ELMGIDRRYE SSIDGLVRVP
     SKDQLELDID PSYVITGNFP VVIRESLLPQ VFDMGDKLCK KAEELVKPGM LGPFCLQSLC
     TENLELVVFE MSARSDGGNN TFMNGSPYSY LYNAEPLSMG QRIAKEIKLA LELKMIEKVI
     S
//
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