ID A0A1U7ZFK3_NELNU Unreviewed; 638 AA.
AC A0A1U7ZFK3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 Name=LOC104589619 {ECO:0000313|RefSeq:XP_010246294.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010246294.1};
RN [1] {ECO:0000313|RefSeq:XP_010246294.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_010246294.1; XM_010247992.2.
DR AlphaFoldDB; A0A1U7ZFK3; -.
DR GeneID; 104589619; -.
DR OrthoDB; 7491at2759; -.
DR UniPathway; UPA00074; UER00130.
DR Proteomes; UP000189703; Unplaced.
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}; 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:UP000189703}.
FT DOMAIN 190..378
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 638 AA; 69141 MW; 1F65A747FBBA9B9B CRC64;
MLLRSTSAVF CGQLNDSLFG SEFRSQPTYK LKKELGFPMG HVNRGKVESG SSSMQHKNWI
SCCQAYTEDH ASSTRKDDLS VHGLSDTIVG VLGGGQLGRM LCQAASKMAI KVAVLDPLEN
CPASALSHYH MVGSFDDSAT VQEFAKRCGV LTVEIEHVDV ATLEKLEQQG VDCQPKASTI
RIIQDKYLQK VHFSQHAIPL PDFMQIDDLE SAKRAGNLFG YPLMIKSKRL AYDGRGNAVA
QGEEELSSAV AALGGYGRGL YVEKWAPFVK ELAVIVARGR DNSISCYPVV ETIHRDNICH
IVKAPADVPW KIRNLATEVA QEAVSSLEGA GVFAVELFLT SDSQILLNEV APRPHNSGHH
TIESCFTSQF EQHLRAVVGL PLGDPSMKMP AAIMYNLLGE EEGEQGFYLA NQLIGRALSI
PGATVHWYDK PEMRKQRKMG HITIVGPSLG MVEARLNSML NQESLEAQTA GLASPRVGII
MGSDSDLPIM KDAARILSNF GVPHEVRIVS AHRTPEMMFS YAISARERGI QIIIAGAGGA
AHLPALTPLP VIGVPVRASS LDGLDSLLSI VQMPRGVPVA TVAINNATNA GLLAVRMLGV
GDADLQARTL QYQQDTKDDV LTKAEKLGKD GWEAYLNR
//
