ID A0A1R1XG23_9FUNG Unreviewed; 553 AA.
AC A0A1R1XG23;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE RecName: Full=Phosphoribosylaminoimidazole carboxylase {ECO:0000256|ARBA:ARBA00021059};
DE EC=4.1.1.21 {ECO:0000256|ARBA:ARBA00012329};
DE Flags: Fragment;
GN ORFNames=AYI70_g8415 {ECO:0000313|EMBL:OMJ13568.1};
OS Smittium culicis.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ13568.1, ECO:0000313|Proteomes:UP000187283};
RN [1] {ECO:0000313|EMBL:OMJ13568.1, ECO:0000313|Proteomes:UP000187283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSMNP {ECO:0000313|EMBL:OMJ13568.1,
RC ECO:0000313|Proteomes:UP000187283};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + H(+)
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + CO2;
CC Xref=Rhea:RHEA:10792, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:137981; EC=4.1.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001244};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004747}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase
CC family. Class I subfamily. {ECO:0000256|ARBA:ARBA00006114}.
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:OMJ13568.1}.
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DR EMBL; LSSN01003438; OMJ13568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1XG23; -.
DR STRING; 133412.A0A1R1XG23; -.
DR UniPathway; UPA00074; UER00130.
DR Proteomes; UP000187283; Unassembled WGS sequence.
DR GO; GO:0043727; F:5-amino-4-imidazole carboxylate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1970; -; 1.
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_01928; PurK; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR005875; PurK.
DR InterPro; IPR040686; PurK_C.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR11609:SF5; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE; 1.
DR PANTHER; PTHR11609; PURINE BIOSYNTHESIS PROTEIN 6/7, PUR6/7; 1.
DR Pfam; PF00731; AIRC; 1.
DR Pfam; PF02222; ATP-grasp; 2.
DR Pfam; PF17769; PurK_C; 1.
DR SMART; SM01001; AIRC; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE); 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000187283}.
FT DOMAIN 137..359
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 553
FT /evidence="ECO:0000313|EMBL:OMJ13568.1"
SQ SEQUENCE 553 AA; 60349 MW; 0B145634A5BD2C30 CRC64;
MNPLDKKVGI LGGGQLGRML IEAAHRLNVD VTIVDPQSDS PAKQISNKSH IDKDFKRSDA
IVELSNKVDV ITAEIEHVDT KTLSEIVAIQ ISQSEILRAG SSLELPVTQD ASVNSIHTYV
LPSPKTIEVI QDKYLQHKVL FENEIPVAEF EACNNYEHAV SIGTRFSYPL ILKARRGAYD
GRGNVFVNSE LELKEAWDKL SSNLVSSTGE EIKDSGIYAE KLISFTKELA VMVVKGIDNE
IVCYPVVETV QSNNICNLVI APAPINGLIR EKAEKMACTA VKAITSVPTS INLKVKSGEA
PISIEKISKS AGVFGVELFL LDNGEVIVNE IAPRPHNSGH YTIEACETSQ YENHLRSVLG
LPLGSTKLKV NFAAMVNILG LPNIFNVPTP CYNSTEVMKS IVADTLSVPG STVHMYGKKE
AKVDRKMGHV TIVANSPVEL SQRLRAILYI VSGKNYNNVH PTQFKQILDL NTQNIENTYD
YKPTPLVGII MGSDSDLPVM KLAADQLKSF GVPFELTIVS AHRTPERMVE YAQSAKKRGL
KVIIAGAGGA AHL
//
