PUR6_CHICK
ID PUR6_CHICK Reviewed; 426 AA.
AC P38024; P87465;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Multifunctional protein ADE2;
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase;
DE EC=6.3.2.6;
DE AltName: Full=SAICAR synthetase;
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazole carboxylase;
DE EC=4.1.1.21;
DE AltName: Full=AIR carboxylase;
DE Short=AIRC;
GN Name=AIRC;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1691501; DOI=10.1073/pnas.87.8.3097;
RA Chen Z.D., Dixon J.E., Zalkin H.;
RT "Cloning of a chicken liver cDNA encoding 5-aminoimidazole ribonucleotide
RT carboxylase and 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide
RT synthetase by functional complementation of Escherichia coli pur mutants.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3097-3101(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RX PubMed=8336716; DOI=10.1128/mcb.13.8.4784-4792.1993;
RA Gavalas A., Dixon J.E., Brayton K.A., Zalkin H.;
RT "Coexpression of two closely linked avian genes for purine nucleotide
RT synthesis from a bidirectional promoter.";
RL Mol. Cell. Biol. 13:4784-4792(1993).
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 -!- 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 -!- 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 -!- 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 -!- SUBUNIT: Homooctamer. {ECO:0000250}.
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; M31764; AAA48601.1; -; mRNA.
DR EMBL; L12533; AAA17894.1; -; Genomic_DNA.
DR PIR; A35641; A35641.
DR RefSeq; NP_990855.1; NM_205524.2.
DR RefSeq; XP_015140912.1; XM_015285426.1.
DR AlphaFoldDB; P38024; -.
DR SMR; P38024; -.
DR BioGRID; 676778; 1.
DR STRING; 9031.ENSGALP00000022269; -.
DR BindingDB; P38024; -.
DR ChEMBL; CHEMBL5312; -.
DR PaxDb; P38024; -.
DR GeneID; 396534; -.
DR KEGG; gga:396534; -.
DR CTD; 10606; -.
DR VEuPathDB; HostDB:geneid_396534; -.
DR eggNOG; KOG2835; Eukaryota.
DR HOGENOM; CLU_061495_1_0_1; -.
DR InParanoid; P38024; -.
DR PhylomeDB; P38024; -.
DR TreeFam; TF106384; -.
DR Reactome; R-GGA-419140; De novo synthesis of IMP.
DR UniPathway; UPA00074; UER00130.
DR UniPathway; UPA00074; UER00131.
DR PRO; PR:P38024; -.
DR Proteomes; UP000000539; Unplaced.
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:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Decarboxylase; Ligase; Lyase; Multifunctional enzyme;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..426
FT /note="Multifunctional protein ADE2"
FT /id="PRO_0000075029"
FT REGION 1..261
FT /note="SAICAR synthetase"
FT REGION 262..426
FT /note="AIR carboxylase"
SQ SEQUENCE 426 AA; 47240 MW; B4A990AEB2AD360C CRC64;
MAPAASELKL GKKVNEGKTK EVYELPDIPG CVLMQSKDQI TAGNAARKDR MEGKAAISNT
TTSCVFQLLQ EAGIKTAFVR KQSDTAFIAA HCEMIPIEWV CRRIATGSFL KRNPGVKEGY
KFYPPKIEMF YKDDANNDPQ WSEEQLIEAK FSFAGLTIGK TEVDIMARST QAIFEILEKS
WQPQNCTLVD LKIEFGVNIL TKEIVLADVI DNDSWRLWPS GDRSQQKDKQ SYRDLKEVTP
EALQMVKRNF EWVAERVELL LKTKSQGRVV VLMGSTSDLG HCEKIKKACA TFGIPCELRV
TSAHKGPDET LRIKAEYEGD GIPTVFVAVA GRSNGLGPVM SGNTAYPVVN CPPLSSDWGA
QDVWSSLRLP SGLGCPTTLS PEGAAQFAAQ IFGLNNHLVW AKLRSNMLNT WISLKQADKK
LRECTL
