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Database: UniProt
Entry: Q06203
LinkDB: Q06203
Original site: Q06203 
ID   PUR1_HUMAN              Reviewed;         517 AA.
AC   Q06203;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   01-OCT-2014, entry version 147.
DE   RecName: Full=Amidophosphoribosyltransferase;
DE            Short=ATase;
DE            EC=2.4.2.14;
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase;
DE            Short=GPAT;
DE   Flags: Precursor;
GN   Name=PPAT; Synonyms=GPAT;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hepatoma;
RX   PubMed=8380692; DOI=10.1006/bbrc.1993.1030;
RA   Iwahana H., Oka J., Mizusawa N., Kudo E., Ii S., Yoshimoto K.,
RA   Holmes E.W., Itakura M.;
RT   "Molecular cloning of human amidophosphoribosyltransferase.";
RL   Biochem. Biophys. Res. Commun. 190:192-200(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=8106516;
RA   Brayton K.A., Chen Z., Zhou G., Nagy P.L., Gavalas A., Trent J.M.,
RA   Deaven L.L., Dixon J.E., Zalkin H.;
RT   "Two genes for de novo purine nucleotide synthesis on human chromosome
RT   4 are closely linked and divergently transcribed.";
RL   J. Biol. Chem. 269:5313-5321(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Muscle;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- CATALYTIC ACTIVITY: 5-phospho-beta-D-ribosylamine + diphosphate +
CC       L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate
CC       + H(2)O.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit. {ECO:0000250}.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. {ECO:0000250}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-diphosphate: step 1/2.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       purine/pyrimidine phosphoribosyltransferase family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00609}.
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DR   EMBL; D13757; BAA02903.1; -; mRNA.
DR   EMBL; U00238; AAC27345.1; -; mRNA.
DR   EMBL; U00239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004200; AAH04200.1; -; mRNA.
DR   CCDS; CCDS3505.1; -.
DR   PIR; A53342; A53342.
DR   RefSeq; NP_002694.3; NM_002703.4.
DR   UniGene; Hs.331420; -.
DR   ProteinModelPortal; Q06203; -.
DR   SMR; Q06203; 12-515.
DR   BioGrid; 111467; 19.
DR   IntAct; Q06203; 2.
DR   STRING; 9606.ENSP00000264220; -.
DR   ChEMBL; CHEMBL2362992; -.
DR   DrugBank; DB00130; L-Glutamine.
DR   DrugBank; DB00352; Thioguanine.
DR   GuidetoPHARMACOLOGY; 2761; -.
DR   MEROPS; C44.001; -.
DR   PhosphoSite; Q06203; -.
DR   DMDM; 548638; -.
DR   MaxQB; Q06203; -.
DR   PaxDb; Q06203; -.
DR   PeptideAtlas; Q06203; -.
DR   PRIDE; Q06203; -.
DR   DNASU; 5471; -.
DR   Ensembl; ENST00000264220; ENSP00000264220; ENSG00000128059.
DR   GeneID; 5471; -.
DR   KEGG; hsa:5471; -.
DR   UCSC; uc003hbr.3; human.
DR   CTD; 5471; -.
DR   GeneCards; GC04M057259; -.
DR   HGNC; HGNC:9238; PPAT.
DR   HPA; HPA036091; -.
DR   HPA; HPA036092; -.
DR   MIM; 172450; gene.
DR   neXtProt; NX_Q06203; -.
DR   PharmGKB; PA33559; -.
DR   eggNOG; COG0034; -.
DR   HOGENOM; HOG000033688; -.
DR   HOVERGEN; HBG002589; -.
DR   InParanoid; Q06203; -.
DR   KO; K00764; -.
DR   OMA; IPVGDMN; -.
DR   OrthoDB; EOG789C9W; -.
DR   PhylomeDB; Q06203; -.
DR   TreeFam; TF106370; -.
DR   BioCyc; MetaCyc:HS05157-MONOMER; -.
DR   Reactome; REACT_1776; Purine ribonucleoside monophosphate biosynthesis.
DR   UniPathway; UPA00074; UER00124.
DR   GeneWiki; Amidophosphoribosyltransferase; -.
DR   GenomeRNAi; 5471; -.
DR   NextBio; 21182; -.
DR   PRO; PR:Q06203; -.
DR   ArrayExpress; Q06203; -.
DR   Bgee; Q06203; -.
DR   CleanEx; HS_PPAT; -.
DR   Genevestigator; Q06203; -.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; TAS:ProtInc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0006543; P:glutamine catabolic process; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0007595; P:lactation; IEA:Ensembl.
DR   GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR   GO; GO:0055086; P:nucleobase-containing small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   GO; GO:0031100; P:organ regeneration; IEA:Ensembl.
DR   GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; TAS:ProtInc.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; TAS:Reactome.
DR   GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR005854; Amd_phspho_trans.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR000583; GATase_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF00310; GATase_2; 2.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR01134; purF; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Acetylation; Allosteric enzyme; Complete proteome;
KW   Glutamine amidotransferase; Glycosyltransferase; Iron; Iron-sulfur;
KW   Magnesium; Metal-binding; Purine biosynthesis; Reference proteome;
KW   Transferase.
FT   PROPEP        1     11       {ECO:0000305}.
FT                                /FTId=PRO_0000029283.
FT   CHAIN        12    517       Amidophosphoribosyltransferase.
FT                                /FTId=PRO_0000029284.
FT   DOMAIN       12    261       Glutamine amidotransferase type-2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00609}.
FT   ACT_SITE     12     12       For GATase activity. {ECO:0000250}.
FT   METAL       280    280       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL       327    327       Magnesium. {ECO:0000250}.
FT   METAL       389    389       Magnesium. {ECO:0000250}.
FT   METAL       390    390       Magnesium. {ECO:0000250}.
FT   METAL       426    426       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL       503    503       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL       506    506       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000269|PubMed:22814378}.
FT   CONFLICT    369    369       V -> I (in Ref. 2; AAC27345).
FT                                {ECO:0000305}.
SQ   SEQUENCE   517 AA;  57399 MW;  D3F2A354C36B29D9 CRC64;
     MELEELGIRE ECGVFGCIAS GEWPTQLDVP HVITLGLVGL QHRGQESAGI VTSDGSSVPT
     FKSHKGMGLV NHVFTEDNLK KLYVSNLGIG HTRYATTGKC ELENCQPFVV ETLHGKIAVA
     HNGELVNAAR LRKKLLRHGI GLSTSSDSEM ITQLLAYTPP QEQDDTPDWV ARIKNLMKEA
     PTAYSLLIMH RDVIYAVRDP YGNRPLCIGR LIPVSDINDK EKKTSETEGW VVSSESCSFL
     SIGARYYREV LPGEIVEISR HNVQTLDIIS RSEGNPVAFC IFEYVYFARP DSMFEDQMVY
     TVRYRCGQQL AIEAPVDADL VSTVPESATP AALAYAGKCG LPYVEVLCKN RYVGRTFIQP
     NMRLRQLGVA KKFGVLSDNF KGKRIVLVDD SIVRGNTISP IIKLLKESGA KEVHIRVASP
     PIKYPCFMGI NIPTKEELIA NKPEFDHLAE YLGANSVVYL SVEGLVSSVQ EGIKFKKQKE
     KKHDIMIQEN GNGLECFEKS GHCTACLTGK YPVELEW
//
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