(data stored in SCRATCH zone)

SWISSPROT: D5E8Q5_METMS

ID   D5E8Q5_METMS            Unreviewed;       355 AA.
AC   D5E8Q5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 59.
DE   RecName: Full=5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase {ECO:0000256|HAMAP-Rule:MF_01163};
DE            EC=6.3.4.23 {ECO:0000256|HAMAP-Rule:MF_01163};
DE   AltName: Full=5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate--formate ligase {ECO:0000256|HAMAP-Rule:MF_01163};
GN   Name=purP {ECO:0000256|HAMAP-Rule:MF_01163};
GN   OrderedLocusNames=Mmah_0026 {ECO:0000313|EMBL:ADE35564.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35564.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35564.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP- and formate-dependent formylation of 5-
CC       aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate
CC       (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl
CC       5'-monophosphate (FAICAR) in the absence of folates.
CC       {ECO:0000256|HAMAP-Rule:MF_01163}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide +
CC         ATP + formate = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC         carboxamide + ADP + phosphate; Xref=Rhea:RHEA:24836,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58467, ChEBI:CHEBI:58475, ChEBI:CHEBI:456216;
CC         EC=6.3.4.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01163};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC       1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (formate route): step
CC       1/1. {ECO:0000256|HAMAP-Rule:MF_01163}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01163}.
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DR   EMBL; CP001994; ADE35564.1; -; Genomic_DNA.
DR   RefSeq; WP_013036507.1; NC_014002.1.
DR   EnsemblBacteria; ADE35564; ADE35564; Mmah_0026.
DR   GeneID; 8982157; -.
DR   KEGG; mmh:Mmah_0026; -.
DR   eggNOG; arCOG04346; Archaea.
DR   eggNOG; COG1759; LUCA.
DR   HOGENOM; HOG000228474; -.
DR   KO; K06863; -.
DR   OMA; CIHYFYS; -.
DR   OrthoDB; 21169at2157; -.
DR   BioCyc; MMAH547558:G1GHT-26-MONOMER; -.
DR   UniPathway; UPA00074; UER00134.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; D5E8Q5.
DR   SWISS-2DPAGE; D5E8Q5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01163, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Ligase {ECO:0000256|HAMAP-Rule:MF_01163};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01163, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01163};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN          101..332
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   BINDING         27
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01163"
FT   BINDING         94
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01163"
FT   BINDING         225
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01163"
FT   BINDING         254
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01163"
SQ   SEQUENCE   355 AA;  40105 MW;  B63683535DF41A97 CRC64;
     MITKKQISDI LKDYNADDLA IATVCSHSSL QIFHGARKEG LKTIGICIGE PPRFYNAYPL
     AKPDEFISVD SYKDIPNIAP LLRQKNAIII PHGSFVEYMG ADKFLDLEVP TFGNRAVLNW
     ESDRTKEREW LEGAGIHMPR LVEPEDIHGP VMVKYHGAKG GRGFFIAKNY EEFLENIDES
     EKYTVQEFIV GTRYYLHYFY SPLKQEGYRL SNGTLEMLSM DRRVESNADE IFRLGSPKEL
     EESNVQPTYV VTGNIPLVAR ESLMPKIFSL GEQVVEESLK LFGGMIGSFC LETVFTDQLE
     IKVFEISARI VAGTNIYTNG SPYSDFIEEG LSTGKRISQE VKLAAEQEKL EVILS
//

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