ID A0A133VK48_9EURY Unreviewed; 367 AA.
AC A0A133VK48;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=AKJ51_02835 {ECO:0000313|EMBL:KXB06811.1};
OS candidate division MSBL1 archaeon SCGC-AAA382A20.
OC Archaea; Euryarchaeota; candidate division MSBL1.
OX NCBI_TaxID=1698280 {ECO:0000313|EMBL:KXB06811.1, ECO:0000313|Proteomes:UP000070263};
RN [1] {ECO:0000313|EMBL:KXB06811.1, ECO:0000313|Proteomes:UP000070263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC-AAA382A20 {ECO:0000313|EMBL:KXB06811.1};
RX PubMed=26758088; DOI=10.1038/srep19181;
RA Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT pools of the Red Sea.";
RL Sci. Rep. 6:19181-19181(2016).
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:KXB06811.1}.
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DR EMBL; LHYE01000029; KXB06811.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133VK48; -.
DR PATRIC; fig|1698280.3.peg.495; -.
DR UniPathway; UPA00074; UER00134.
DR Proteomes; UP000070263; 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};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01163};
KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01163};
KW Reference proteome {ECO:0000313|Proteomes:UP000070263}.
FT DOMAIN 22..145
FT /note="IMP biosynthesis enzyme PurP N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06849"
FT DOMAIN 176..366
FT /note="IMP biosynthesis enzyme PurP C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06973"
FT BINDING 27
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 96
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 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01163"
FT BINDING 264
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 367 AA; 41933 MW; FCDE8B5E45C0CBEB CRC64;
MIEKETIRET LSEYDKENIT LGILCSHSAL QLIHGAKLEG FNTIGICPEE REKAYKAFPK
ARADEYMIVD QFDEILEDDR QEELLEKNTI IIPHGSFVEY VGAEKLLEQF RVPIFGNRNS
LRWEGKRIKQ REWLKKSGVN VPKRYNDPSK IDGKVFVKFS GAKGGRGFFI ANSEEDFEEK
VKKKIEKGYI TEEEAENATI QEFVLGIRYY PHYFHSTFDR RGAETEDGAI EILGMDRRIE
PIDESYRGLP NVPEEFFDYT VTGNEPLTIR EKLLVNLIDM GINVVETSKD LFSGGINGPF
CLETVFHPDE GFTVFEISGR IVAGTNLYPL GSPYSAYLFE EPMSTGRRMA REIKDGAEAG
ELEKVVY
//
