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Database: UniProt
Entry: G7P5S1_MACFA
LinkDB: G7P5S1_MACFA
Original site: G7P5S1_MACFA 
ID   G7P5S1_MACFA            Unreviewed;       428 AA.
AC   G7P5S1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=PurE domain-containing protein {ECO:0000259|SMART:SM01001};
DE   Flags: Fragment;
GN   ORFNames=EGM_14490 {ECO:0000313|EMBL:EHH53789.1};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1] {ECO:0000313|EMBL:EHH53789.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CE-4 {ECO:0000313|EMBL:EHH53789.1};
RX   PubMed=22002653; DOI=10.1038/nbt.1992;
RA   Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA   Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA   Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA   Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA   Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA   Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT   "Genome sequencing and comparison of two nonhuman primate animal models,
RT   the cynomolgus and Chinese rhesus macaques.";
RL   Nat. Biotechnol. 29:1019-1023(2011).
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:0000256|ARBA:ARBA00004672}.
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   -!- SUBUNIT: Homooctamer. {ECO:0000256|ARBA:ARBA00011823}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase
CC       family. Class II subfamily. {ECO:0000256|ARBA:ARBA00010478}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the SAICAR synthetase
CC       family. {ECO:0000256|ARBA:ARBA00011020}.
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DR   EMBL; CM001280; EHH53789.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7P5S1; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; KOG2835; Eukaryota.
DR   UniPathway; UPA00074; UER00130.
DR   Proteomes; UP000009130; Chromosome 5.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01416; SAICAR_synt_Ade5; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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   PANTHER; PTHR43599:SF3; BIFUNCTIONAL PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE_PHOSPHORIBOSYLAMINOIMIDAZOLE SUCCINOCARBOXAMIDE SYNTHETASE; 1.
DR   PANTHER; PTHR43599; MULTIFUNCTIONAL PROTEIN ADE2; 1.
DR   Pfam; PF00731; AIRC; 1.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   SMART; SM01001; AIRC; 1.
DR   SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE); 1.
DR   SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR   PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lyase {ECO:0000256|ARBA:ARBA00022793};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT   DOMAIN          270..417
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EHH53789.1"
FT   NON_TER         428
FT                   /evidence="ECO:0000313|EMBL:EHH53789.1"
SQ   SEQUENCE   428 AA;  47628 MW;  721F4964B105DF38 CRC64;
     STVLNIGKKL YEGKTKEVYE LLDSPGKVLL QSKEQITAGN AARKNHLEGK AAISNKITSC
     IFQLLQEADF GYQYVGIKTA FTRKCGETAF IAPQCEMIPI EWVCRRIATD SFLKRNPDDK
     EGYKFYPPKV ELFFKDDANN DPQWSEEQLI AAKLCFAGLV IGQTEVDIMS HATQAIFEIL
     EKSWLPQNCT LVDMKIEFGV DVTTKEIVLA DVIDNDSWRL WPSGDRSQQK DKQSYRDLKE
     VTPEGLQMVK KNFEWVAERV ELLLKSESQC RVVVLMGSTS DLGHCEKIKK ACGNFGIPCE
     LRVTSAHKGP DETLRIKAEY EGDGIPTVFV AVAGRSNGLG PVMSGNTAYP VISCPPLTPD
     WGAQDVWSSL RLPSGLGCST ILSPEGSAQF AAQIFGLNNH LVWGKLQADI LNTWISLKQA
     DKKIRECH
//
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