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Database: UniProt
Entry: Q8PT10
LinkDB: Q8PT10
Original site: Q8PT10 
ID   PURP2_METMA             Reviewed;         356 AA.
AC   Q8PT10;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   13-FEB-2019, entry version 98.
DE   RecName: Full=5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01163};
GN   Name=purP2 {ECO:0000255|HAMAP-Rule:MF_01163};
GN   OrderedLocusNames=MM_2913;
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; AAM32609.1; -; Genomic_DNA.
DR   RefSeq; WP_011034815.1; NC_003901.1.
DR   ProteinModelPortal; Q8PT10; -.
DR   SMR; Q8PT10; -.
DR   STRING; 192952.MM_2913; -.
DR   EnsemblBacteria; AAM32609; AAM32609; MM_2913.
DR   GeneID; 24881232; -.
DR   KEGG; mma:MM_2913; -.
DR   PATRIC; fig|192952.21.peg.3366; -.
DR   eggNOG; arCOG04346; Archaea.
DR   eggNOG; COG1759; LUCA.
DR   HOGENOM; HOG000228474; -.
DR   KO; K06863; -.
DR   OMA; VKPHGAK; -.
DR   OrthoDB; 21169at2157; -.
DR   BioCyc; MMAZ192952:G1FZI-3040-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;
KW   Reference proteome.
FT   CHAIN         1    356       5-formaminoimidazole-4-carboxamide-1-
FT                                (beta)-D-ribofuranosyl 5'-monophosphate
FT                                synthetase 2.
FT                                /FTId=PRO_0000348628.
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;  CA0A265212A1EC2E CRC64;
     MITKQQVLEF LKDYDLDNIT IATICSHSSL QIFDGARKEG FRTLGICVGK PPKFYDAFPR
     AKPDEYLVLE DYEDLINRAE ELRKKNTIII PHSSLIYYLG RENFTGMAVP TFGNRTSIEW
     ESDRDKESRW FLGAGIQMPK KIDDPHDIKG PVMVEYEGAK GGKGFFVAKN YKEFSELVDH
     TQKYTIHEYI NGTRYDLHYF YSPIRNDGYT LSKGSLELLS MDRRVESNAD EIFRLGSPRE
     LIESGICPTY VLTGNVPLVA RESILSRIFS LGEQVVEESL ALFGGITGAF CIEAVITDSL
     DIKVFELSSR IVSGTNLYIS GSPYSDLMQK RLSTGRRIAL EIKEAAKSNQ LDKILS
//
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