ID A0A2G5HVD5_CERBT Unreviewed; 660 AA.
AC A0A2G5HVD5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Phosphoribosylaminoimidazole carboxylase {ECO:0000256|ARBA:ARBA00021059};
DE EC=4.1.1.21 {ECO:0000256|ARBA:ARBA00012329};
DE AltName: Full=AIR carboxylase {ECO:0000256|ARBA:ARBA00031607};
GN ORFNames=CB0940_10644 {ECO:0000313|EMBL:PIA96202.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA96202.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIA96202.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIA96202.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) 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:PIA96202.1}.
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DR EMBL; LKMD01000103; PIA96202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5HVD5; -.
DR OrthoDB; 7491at2759; -.
DR UniPathway; UPA00074; UER00130.
DR Proteomes; UP000230605; Chromosome 8.
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_01929; PurE_classI; 1.
DR HAMAP; MF_01928; PurK; 1.
DR InterPro; IPR016301; Ade2_fungi/plant.
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; IPR033747; PurE_ClassI.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR005875; PurK.
DR InterPro; IPR040686; PurK_C.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR01162; purE; 1.
DR NCBIfam; TIGR01161; purK; 1.
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; 1.
DR Pfam; PF17769; PurK_C; 1.
DR PIRSF; PIRSF001340; AIR_carboxylase; 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}.
FT DOMAIN 192..381
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 660 AA; 72464 MW; F420E09A0F506493 CRC64;
MRPCLINDRL DVEKTWSSCR TCNFVPIATA SLVVPMRQES NFLSLTKISR VTSTRRKLFR
HSRAETTSSR PTSEQITLTS DLVDMASDKV VGVLGGGQLG RMLAEAANLL EIKVNFLDAA
GSSAKQVSGH DGHVEGSFKD KDAIQKLAEK SDVITVEIEH VDTEMLKEVA DTVDVQPSWQ
TIRTIQDKYV QKLHLEKNGV AAAQFQALSA PTLQEMDRVG TELGLPFMLK CRRDAYDGRG
NFAVKTKTDF REALDVLSKN KDLYAEKWCN FKMELAVMVV KTKDNVLSFP TVETIHEDSI
CKLTYCPARG VSPEIDKKAQ ALARQAVGCF WGKGVFGVEM FLTRNNDLLI NEIAPRPHNS
GHYTIEGCPV SQYEAHLRAI LDLPLQQEDL QLREPSIMLN ILGGESPDSH LLIARAALRH
RRTKIHLYGK GQARKGRKMG HITVCAPTMQ EAEQIIQPMI DLVDEGKPQI NRRGSVMYST
PQEKPTEKPL VAIVMGSDSD LPVLQPGLAI LNKFSIPYTT RITSAHRTPS WMAEFASGAA
ASGLKVIIAA AGGAAHLPGM TAAYTSLPVI GVPVKPTIGD GMDSLLSICN MPRGVPVATV
SINNSVNAAL LAARIIGSAD LKVRDVVEKY MKDSEKEVRE KDLKLVEIGA EKYATEILKK
//
