ID A0A1D6MH98_MAIZE Unreviewed; 584 AA.
AC A0A1D6MH98;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=phosphoribosylaminoimidazole carboxylase {ECO:0000256|ARBA:ARBA00012329};
DE EC=4.1.1.21 {ECO:0000256|ARBA:ARBA00012329};
DE AltName: Full=AIR carboxylase {ECO:0000256|ARBA:ARBA00031607};
GN ORFNames=ZEAMMB73_Zm00001d039422 {ECO:0000313|EMBL:ONM28820.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM28820.1};
RN [1] {ECO:0000313|EMBL:ONM28820.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM28820.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-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}.
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DR EMBL; CM007649; ONM28820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6MH98; -.
DR UniPathway; UPA00074; UER00130.
DR ExpressionAtlas; A0A1D6MH98; baseline and differential.
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};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
SQ SEQUENCE 584 AA; 63445 MW; 36947233B08CEBB9 CRC64;
MHARFLSAPS PASAAPSPHG GPPVHGVSNT VIGVLGGGQL GKMLCHAASQ MGIRIVILDP
LPGCPASSVC DEHVIGSFND GDTVREFAKR CGVLTVEIEH VDAATLEKLE KQGVDCEPKA
STITIIQDKY RQKKHFSRYE IPLPDFMEVD TLRSIEEAGE KFGYPLMVKS KRLAYDGRGN
AVAKNKEELS SVVASLGGFE RGLYVERWTP FVKELSVIVA RSRDNSTVCY PVVETVHKEN
ICHVVEAPAD VSNKIKKLAT SVAEKAIKSL EGAGVFAVEL FLTEDDQILL NEVAPRPHNS
GHHTIESCYT SQYEQHIRAI LGLPLGDPSM KAPAAIMYNI LGEDEGEAGF FLAHQLISRA
LTIPGTSVHW YAKPEMRKQR KMGHITIVGP SKISVKSRLD NLLQRNSSDP KEVSPRVAII
MGSQSDLPVM KDAERVLKEF DIPCELTIVS AHRTPERMYD YAKSAKDRGF EVIIAGAGGA
AHLPGMVASL TPLPVIGVPI KTSTLSGFDS LLSIVQMPKG IPVATVAIGI AENAGLLAAR
ILAARDPELQ DRVTKYQDDL RDMVLETAER LEDQGPEEFL KGMD
//
