ID A0A087S7T9_9ARCH Unreviewed; 341 AA.
AC A0A087S7T9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=AAA799B03_00610 {ECO:0000313|EMBL:KFM21793.1};
OS Marine Group I thaumarchaeote SCGC AAA799-B03.
OC Archaea; Nitrososphaerota; Marine Group I.
OX NCBI_TaxID=1502289 {ECO:0000313|EMBL:KFM21793.1, ECO:0000313|Proteomes:UP000029384};
RN [1] {ECO:0000313|EMBL:KFM21793.1, ECO:0000313|Proteomes:UP000029384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC AAA799-B03 {ECO:0000313|EMBL:KFM21793.1};
RA Ngugi D.K., Blom J., Alam I., Rashid M., Baalawi W., Zhang G., Hikmawan T.,
RA Guan Y., Antunes A., Siam R., El-Dorry H., Bajic V., Stingl U.;
RL Submitted (JUN-2014) 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 -!- 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:KFM21793.1}.
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DR EMBL; JOTA01000010; KFM21793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087S7T9; -.
DR PATRIC; fig|1502289.3.peg.569; -.
DR UniPathway; UPA00074; UER00134.
DR Proteomes; UP000029384; Unassembled WGS sequence.
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; 3.40.50.20; -; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01163};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01163, ECO:0000313|EMBL:KFM21793.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01163};
KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01163};
KW Reference proteome {ECO:0000313|Proteomes:UP000029384}.
FT DOMAIN 4..124
FT /note="IMP biosynthesis enzyme PurP N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06849"
FT DOMAIN 156..341
FT /note="IMP biosynthesis enzyme PurP C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06973"
FT BINDING 10
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 77
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 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01163"
FT BINDING 238
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 341 AA; 38594 MW; B03920D11120E53C CRC64;
MTSIATLGSH CSLQVLKGAK DEGLKTILVC EKKREKLYRR FPFIDELIIV DKFREVLDEK
CQATLEQNDA VLIPHGTLIA QMSSEEIESI KTPIFGNKWI LRWESDREMK EKLMREANLP
MPKPVTNPSE IEKLSIVKRQ GAAGGKGYFM VANEEDYNTK RNQLISEGVI SKDETLYIQE
YAAGVLAYLT FFYSPLKEEL EFYGVDQRHE SDIEGLGRIP SEQQLKTNKV PSFNVIGNSP
LVLRESLLDE VYTMGENFVE AAKRIVAPGM NGPFCIEGVY DENAKFTSFE FSARIVAGSN
IYMDGSPYYS LLFNETMSMG KRIAREVKTA TESNQLDKIT T
//
