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Database: UniProt
Entry: Q8PWT3
LinkDB: Q8PWT3
Original site: Q8PWT3 
ID   PURP1_METMA             Reviewed;         356 AA.
AC   Q8PWT3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JAN-2019, entry version 98.
DE   RecName: Full=5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01163};
GN   Name=purP1 {ECO:0000255|HAMAP-Rule:MF_01163};
GN   OrderedLocusNames=MM_1493;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 /
OS   JCM 11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene
RT   transfer between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(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; AE008384; AAM31189.1; -; Genomic_DNA.
DR   RefSeq; WP_011033439.1; NC_003901.1.
DR   ProteinModelPortal; Q8PWT3; -.
DR   SMR; Q8PWT3; -.
DR   STRING; 192952.MM_1493; -.
DR   EnsemblBacteria; AAM31189; AAM31189; MM_1493.
DR   GeneID; 24883220; -.
DR   KEGG; mma:MM_1493; -.
DR   PATRIC; fig|192952.21.peg.1725; -.
DR   eggNOG; arCOG04346; Archaea.
DR   eggNOG; COG1759; LUCA.
DR   HOGENOM; HOG000228474; -.
DR   KO; K06863; -.
DR   OMA; KFPGARG; -.
DR   OrthoDB; 21169at2157; -.
DR   BioCyc; MMAZ192952:G1FZI-1549-MONOMER; -.
DR   UniPathway; UPA00074; UER00134.
DR   Proteomes; UP000000595; 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    356       5-formaminoimidazole-4-carboxamide-1-
FT                                (beta)-D-ribofuranosyl 5'-monophosphate
FT                                synthetase 1.
FT                                /FTId=PRO_0000348627.
FT   DOMAIN      101    333       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   NP_BIND     145    196       ATP. {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   METAL       293    293       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   METAL       306    306       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     226    226       ATP. {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   BINDING     255    255       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
SQ   SEQUENCE   356 AA;  40282 MW;  9E0182EB1DAA3932 CRC64;
     MITKQQVLEF LKNYDLDNIT IATVCSHSSL QIFDGARKEG FRTMGICVGK PPKFYEAFPR
     AKPDEYLIVE SYEDIMNKVE ELRKKNVIII PHGSFVAYLG TENFAEMAVP TFGNRAVLEW
     ESDRSKEREW LLGAGIHMPG KIDDPRDING PVMVKYDGAK GGKGFFVAKT YEEFDELVDR
     TQKYTIQEFI TGTRYYLHYF YSPIRNEGYT LSEGSLELLS MDRRVESNAD EIFRLGSPRE
     LIEAGIRPTY VVTGNVPLVA RESLLPLIFS LGERVVEESL GLFGGMIGAF CLETVFTDEL
     EIKVFEISAR IVAGTNLYIS GSPYADLIQE DLSTGRRIAQ EIKEAVRKNQ LDKIIS
//
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