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Database: UniProt
Entry: B8D426_DESA1
LinkDB: B8D426_DESA1
Original site: B8D426_DESA1 
ID   B8D426_DESA1            Unreviewed;       355 AA.
AC   B8D426;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 74.
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   OrderedLocusNames=DKAM_0531 {ECO:0000313|EMBL:ACL10857.1};
OS   Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 /
OS   1221n) (Desulfurococcus kamchatkensis).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Desulfurococcus.
OX   NCBI_TaxID=490899 {ECO:0000313|EMBL:ACL10857.1, ECO:0000313|Proteomes:UP000006903};
RN   [1] {ECO:0000313|EMBL:ACL10857.1, ECO:0000313|Proteomes:UP000006903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18924 / JCM 16383 / VKM B-2413 / 1221n
RC   {ECO:0000313|Proteomes:UP000006903};
RX   PubMed=19114480; DOI=10.1128/JB.01525-08;
RA   Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V.,
RA   Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Complete genome sequence of the anaerobic, protein-degrading
RT   hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.";
RL   J. Bacteriol. 191:2371-2379(2009).
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}.
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DR   EMBL; CP001140; ACL10857.1; -; Genomic_DNA.
DR   RefSeq; WP_012608199.1; NC_011766.1.
DR   AlphaFoldDB; B8D426; -.
DR   STRING; 490899.DKAM_0531; -.
DR   GeneID; 7171747; -.
DR   KEGG; dka:DKAM_0531; -.
DR   eggNOG; arCOG04346; Archaea.
DR   HOGENOM; CLU_065084_0_0_2; -.
DR   OMA; CIHYFYS; -.
DR   UniPathway; UPA00074; UER00134.
DR   Proteomes; UP000006903; Chromosome.
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}; Ligase {ECO:0000256|HAMAP-Rule:MF_01163};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01163, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01163}.
FT   DOMAIN          125..331
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   BINDING         23
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         91
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         224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01163"
FT   BINDING         252
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   355 AA;  39857 MW;  4E588EB54F1E77DB CRC64;
     MNIDELLRGY DTGNLAIGTL ASHSALQIMH GAKKEGFTTI LVALRDRAWF YRDFDHLIDL
     IIEVNSWRDI CKPEIVEELR GYNTILVPHG SFVEYVGLEC GESINVPLFG TRSLLRVEAD
     QKLKMLLLMK AGIPTPRVYE LSDDVRGPVI VKLPGAKGGK GYFIASSNSE IEAKLRKYIE
     DGLLRSPREA IIQEYIVGVT AYFHYFYSPV LNRLELLGAD IRYESDVDGL RRLPVGILEE
     LGIDPTFTVV GNLPLVLRES LLPKIIEYGR RFVDASRGMV SPGVIGPFCL ESVIDRELNV
     KVFEFSGRIV AGTNLYIDGS PYSYLYWDQP VSMGRRIAIE VRLALEKGLL EKIVT
//
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