PUR6_PONAB
ID PUR6_PONAB Reviewed; 425 AA.
AC Q5RB59;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase {ECO:0000250|UniProtKB:P22234};
DE Short=PAICS {ECO:0000250|UniProtKB:P22234};
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazole carboxylase {ECO:0000250|UniProtKB:P22234};
DE EC=4.1.1.21 {ECO:0000250|UniProtKB:P22234};
DE AltName: Full=AIR carboxylase {ECO:0000250|UniProtKB:P22234};
DE Short=AIRC {ECO:0000250|UniProtKB:P22234};
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazole succinocarboxamide synthetase {ECO:0000250|UniProtKB:P22234};
DE EC=6.3.2.6 {ECO:0000250|UniProtKB:P22234};
DE AltName: Full=SAICAR synthetase {ECO:0000250|UniProtKB:P22234};
GN Name=PAICS {ECO:0000250|UniProtKB:P22234};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional phosphoribosylaminoimidazole carboxylase and
CC phosphoribosylaminoimidazole succinocarboxamide synthetase catalyzing
CC two reactions of the de novo purine biosynthetic pathway.
CC {ECO:0000250|UniProtKB:P22234}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP +
CC L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-
CC 4-carboxamido]succinate + ADP + 2 H(+) + phosphate;
CC Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58443,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:456216; EC=6.3.2.6;
CC Evidence={ECO:0000250|UniProtKB:P22234};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22629;
CC Evidence={ECO:0000250|UniProtKB:P22234};
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:0000250|UniProtKB:P22234};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10794;
CC Evidence={ECO:0000250|UniProtKB:P22234};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC {ECO:0000250|UniProtKB:P22234}.
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:0000250|UniProtKB:P22234}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000250|UniProtKB:P22234}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the SAICAR synthetase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase
CC family. Class II subfamily. {ECO:0000305}.
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DR EMBL; CR858796; CAH91001.1; -; mRNA.
DR RefSeq; NP_001128995.1; NM_001135523.1.
DR AlphaFoldDB; Q5RB59; -.
DR SMR; Q5RB59; -.
DR STRING; 9601.ENSPPYP00000016477; -.
DR GeneID; 100190835; -.
DR KEGG; pon:100190835; -.
DR CTD; 10606; -.
DR eggNOG; KOG2835; Eukaryota.
DR InParanoid; Q5RB59; -.
DR UniPathway; UPA00074; UER00130.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000001595; 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-KW.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; ISS:UniProtKB.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; ISS:UniProtKB.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; ISS:UniProtKB.
DR HAMAP; MF_02045; PurE_classII; 1.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR033626; PurE_classII.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR Pfam; PF00731; AIRC; 1.
DR Pfam; PF01259; SAICAR_synt; 1.
DR SMART; SM01001; AIRC; 1.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Decarboxylase; Ligase; Lyase;
KW Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW Purine biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT CHAIN 2..425
FT /note="Bifunctional phosphoribosylaminoimidazole
FT carboxylase/phosphoribosylaminoimidazole succinocarboxamide
FT synthetase"
FT /id="PRO_0000075032"
FT REGION 2..260
FT /note="SAICAR synthetase domain"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT REGION 261..266
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT REGION 267..425
FT /note="AIR carboxylase domain"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT BINDING 332
FT /ligand="CO2"
FT /ligand_id="ChEBI:CHEBI:16526"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT MOD_RES 22
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCL9"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT MOD_RES 36
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCL9"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT MOD_RES 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT MOD_RES 247
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P22234"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22234"
SQ SEQUENCE 425 AA; 46937 MW; 8EF27845011A5C9D CRC64;
MATAEVLNIG KKLYEGKTKE VYELLDSPGK VLLQSKDQIT AGNAARKNHL EGKAAISNKI
TSCIFQLLQE AGIKTAFTRK CGETAFIAPQ CEMIPIEWVC GRIATGSFLK RNPGVKEGYK
FYPPKVELFF KDDANNDPQW SAEQLIAAKF CFAGLVIGQT EVDIMSHATQ AIFEILEKSW
LPQNCTLVDM KIEFGVDVTT KEIVLADVID NDSWRLWPSG DRSQQKDKQS YRDLKEVTPE
GLQMVKKNFE WVAERVELLL KSESQCRVVV LMGSTSDLGH CEKIKKACGN FGIPCELRVT
SAHKGPDETL RIKAEYEGDG IPTVFVAVAG RSNGLGPVMC GNTAYPVISC PPLTPDWGAQ
DVWSSLRLPS GLGCSTILSP EGSAQFAAQI FGLNNHLVWS KLRASILNTW ISLKQADKKI
RECNL
