PUR6_RAT
ID PUR6_RAT Reviewed; 425 AA.
AC P51583;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 150.
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:0000303|PubMed:7742366};
DE EC=4.1.1.21 {ECO:0000250|UniProtKB:P22234};
DE AltName: Full=AIR carboxylase {ECO:0000303|PubMed:7742366};
DE Short=AIRC {ECO:0000303|PubMed:7742366};
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazole succinocarboxamide synthetase {ECO:0000303|PubMed:7742366};
DE EC=6.3.2.6 {ECO:0000250|UniProtKB:P22234};
DE AltName: Full=SAICAR synthetase {ECO:0000303|PubMed:7742366};
GN Name=Paics {ECO:0000312|RGD:620066}; Synonyms=Ade2, Airc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer;
RX PubMed=7742366; DOI=10.1016/0167-4781(95)00036-g;
RA Iwahana H., Honda S., Tsujisawa T., Takahashi Y., Adzuma K., Katashima R.,
RA Yamaoka T., Moritani M., Yoshimoto K., Itakura M.;
RT "Rat genomic structure of amidophosphoribosyltransferase, cDNA sequence of
RT aminoimidazole ribonucleotide carboxylase, and cell cycle-dependent
RT expression of these two physically linked genes.";
RL Biochim. Biophys. Acta 1261:369-380(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; D37979; BAA07197.1; -; mRNA.
DR EMBL; BC072508; AAH72508.1; -; mRNA.
DR EMBL; BC085711; AAH85711.1; -; mRNA.
DR PIR; S55684; S55684.
DR RefSeq; NP_543186.1; NM_080910.3.
DR RefSeq; XP_006250914.1; XM_006250852.3.
DR RefSeq; XP_006250915.1; XM_006250853.3.
DR RefSeq; XP_006250916.1; XM_006250854.2.
DR AlphaFoldDB; P51583; -.
DR SMR; P51583; -.
DR IntAct; P51583; 2.
DR STRING; 10116.ENSRNOP00000061495; -.
DR iPTMnet; P51583; -.
DR PhosphoSitePlus; P51583; -.
DR jPOST; P51583; -.
DR PaxDb; P51583; -.
DR PRIDE; P51583; -.
DR Ensembl; ENSRNOT00000063942; ENSRNOP00000061495; ENSRNOG00000002101.
DR GeneID; 140946; -.
DR KEGG; rno:140946; -.
DR UCSC; RGD:620066; rat.
DR CTD; 10606; -.
DR RGD; 620066; Paics.
DR eggNOG; KOG2835; Eukaryota.
DR GeneTree; ENSGT00390000010172; -.
DR HOGENOM; CLU_061495_1_0_1; -.
DR InParanoid; P51583; -.
DR OMA; WSDEQII; -.
DR OrthoDB; 566769at2759; -.
DR PhylomeDB; P51583; -.
DR TreeFam; TF106384; -.
DR Reactome; R-RNO-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00130.
DR UniPathway; UPA00074; UER00131.
DR PRO; PR:P51583; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002101; Expressed in ovary and 19 other tissues.
DR Genevisible; P51583; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; ISS:UniProtKB.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; ISS:UniProtKB.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; ISO:RGD.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; ISO:RGD.
DR GO; GO:0097294; P:'de novo' XMP biosynthetic process; ISO:RGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEP:RGD.
DR GO; GO:0006177; P:GMP biosynthetic process; ISO:RGD.
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 TIGRFAMs; TIGR01162; purE; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE 1: Evidence at protein 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_0000075033"
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:0007744|PubMed:22673903"
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; 47096 MW; 8E097CFD114E9DAB CRC64;
MATAEVLNIG RKLYEGKTKE VYELLDSPGR VLLQSKDQIT AGNAARKNHL EGKAAISNKI
TSCIFQLLQE AGIKTAFTKK CGETAFIAPQ CEMIPIEWVC RRIATGSFLK RNPGVKEGYR
FYPPKVEMFF KDDANNDPQW SEEQLIAAKF CFAGLVIGQT EVDIMSHATQ AIFEILEKSW
LPQNCTLVDM KIEFGVDVTT KEIVLADVID NDSWRLWPSG DRSQQKDKQS YRDLKEVTPE
GLQMVKKNFE WVADRVELLL KSNSQCRVVV LMGSTSDLGH CEKIKKACGN FGIPCELRVT
SAHKGPDETL RIKAEYEGDG IPTVFVAVAG RSNGLGPVMS GNTAYPVISC PPITADWGAQ
DVWSSLRLPS GIGCSTILSP EGSAQFAAQI FGLNNHLVWA KLRASKLNTW ISLKQADKKI
RECNL
