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Database: UniProt
Entry: Q8ZYV1
LinkDB: Q8ZYV1
Original site: Q8ZYV1 
ID   PURP_PYRAE              Reviewed;         341 AA.
AC   Q8ZYV1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   16-JAN-2019, entry version 94.
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=PAE0608;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630
OS   / NBRC 100827).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL62892.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q8ZYV1; -.
DR   SMR; Q8ZYV1; -.
DR   STRING; 178306.PAE0608; -.
DR   EnsemblBacteria; AAL62892; AAL62892; PAE0608.
DR   KEGG; pai:PAE0608; -.
DR   PATRIC; fig|178306.9.peg.436; -.
DR   eggNOG; arCOG04346; Archaea.
DR   eggNOG; COG1759; LUCA.
DR   HOGENOM; HOG000228474; -.
DR   InParanoid; Q8ZYV1; -.
DR   KO; K06863; -.
DR   OMA; KFPGARG; -.
DR   UniPathway; UPA00074; UER00134.
DR   Proteomes; UP000002439; 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;
KW   Reference proteome.
FT   CHAIN         1    341       5-formaminoimidazole-4-carboxamide-1-
FT                                (beta)-D-ribofuranosyl 5'-monophosphate
FT                                synthetase.
FT                                /FTId=PRO_0000348631.
FT   DOMAIN      113    328       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   NP_BIND     143    195       ATP. {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   METAL       276    276       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   METAL       289    289       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   BINDING      27     27       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   BINDING      92     92       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   BINDING     217    217       ATP. {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   BINDING     237    237       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
SQ   SEQUENCE   341 AA;  38690 MW;  A982F7163170625B CRC64;
     MALKPTMSQL LKNYDLERLA ISTVASHTAL QILRGAKKYG FRTIAVARGE AVAQFYRQFP
     FIDEVWVGDF ANFRKTAEKL AANNAVFIPH GSYVEYVGWR QALEAPVPTL GCRELLRWEA
     DQFKKMSLLE KAGIPIPRIY KTAEEVEGPV IVKLFGAKGG RGYFVARDRR ELAERLKRVT
     EDYIIQEYLF GVPAYYHYFS SPVYSRLEIF GADIRYESNV DGRTFGWAEP TFVVVGNLPM
     VLRESLLPTI YTYGVQFLKA VEEAVGCKLA GPFCLESIIK DDMSIVVFEF SGRIVAGTNI
     YMGYGSPYSV LYFDKPMDMG ERIAHEIKEA VKRGKIEHLF T
//
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