ID A0A062V349_9EURY Unreviewed; 357 AA.
AC A0A062V349;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 ORFNames=ANME2D_00554 {ECO:0000313|EMBL:KCZ73486.1};
OS Candidatus Methanoperedens nitroreducens.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Candidatus Methanoperedenaceae; Methanoperedens.
OX NCBI_TaxID=1392998 {ECO:0000313|EMBL:KCZ73486.1, ECO:0000313|Proteomes:UP000027153};
RN [1] {ECO:0000313|EMBL:KCZ73486.1, ECO:0000313|Proteomes:UP000027153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANME-2d {ECO:0000313|EMBL:KCZ73486.1,
RC ECO:0000313|Proteomes:UP000027153};
RX PubMed=23892779; DOI=10.1038/nature12375;
RA Haroon M.F., Hu S., Shi Y., Imelfort M., Keller J., Hugenholtz P., Yuan Z.,
RA Tyson G.W.;
RT "Anaerobic oxidation of methane coupled to nitrate reduction in a novel
RT archaeal lineage.";
RL Nature 500:567-570(2013).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KCZ73486.1}.
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DR EMBL; JMIY01000001; KCZ73486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A062V349; -.
DR PATRIC; fig|1392998.3.peg.156; -.
DR UniPathway; UPA00074; UER00134.
DR Proteomes; UP000027153; Unassembled WGS sequence.
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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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:SF2; 5-FORMAMINOIMIDAZOLE-4-CARBOXAMIDE-1-(BETA)-D-RIBOFURANOSYL 5'-MONOPHOSPHATE SYNTHETASE; 1.
DR PANTHER; PTHR38147; 5-FORMAMINOIMIDAZOLE-4-CARBOXAMIDE-1-(BETA)-D-RIBOFURANOSYL 5'-MONOPHOSPHATE SYNTHETASE-RELATED; 1.
DR Pfam; PF06849; DUF1246; 1.
DR Pfam; PF06973; DUF1297; 1.
DR PIRSF; PIRSF004602; ATPgrasp_PurP; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01163, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01163, ECO:0000313|EMBL:KCZ73486.1};
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:UP000027153}.
FT DOMAIN 102..334
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT BINDING 28
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01163"
FT BINDING 95
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01163"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01163"
FT BINDING 256
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01163"
SQ SEQUENCE 357 AA; 40472 MW; 0B18732F94690019 CRC64;
MMVTKQEILE ILENYDKDKL AIATVCSHSS LQIFDGARKE GFRTIGICIN APPKFYDAFP
KAKPDEFFTV KDYKEIISKT DELARKNAII IPHGSFVEYL GAANFNKLHL PTFGNRRVLE
WESDRDMSRM WLEAAGIKMP RQIKNPEDID SPMMVKYYGA KGGMGFFVVK NYSDFQKRIN
PAEKYTIQEF VLGTRYYMHY FYSPIKHEGY ALSKGTLELL GIDRRVESNA DEIFRIGSPT
ELAEAEIYPT FVVTGNLPLI VRESLLPRVF EMGEQVVEKS LELFGGMVGP FCLETVVTDT
LELKVFEISA RIVAGTNLFI SGSPYADLVD EGLSTGRRIA REIKTARDMD LLSEVIS
//
