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-MAY-2013, entry version 134.
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).
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 (By similarity).
CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
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.
CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain.
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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 IPI; IPI00029534; -.
DR PIR; A53342; A53342.
DR RefSeq; NP_002694.3; NM_002703.4.
DR UniGene; Hs.331420; -.
DR ProteinModelPortal; Q06203; -.
DR IntAct; Q06203; 2.
DR STRING; 9606.ENSP00000264220; -.
DR MEROPS; C44.001; -.
DR PhosphoSite; Q06203; -.
DR DMDM; 548638; -.
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; 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; GIPFELG; -.
DR OrthoDB; EOG47M1XN; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00074; UER00124.
DR DrugBank; DB00130; L-Glutamine.
DR DrugBank; DB00352; Thioguanine.
DR GenomeRNAi; 5471; -.
DR NextBio; 21182; -.
DR ArrayExpress; Q06203; -.
DR Bgee; Q06203; -.
DR CleanEx; HS_PPAT; -.
DR Genevestigator; Q06203; -.
DR GermOnline; ENSG00000128059; Homo sapiens.
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:Compara.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Compara.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Compara.
DR GO; GO:0006543; P:glutamine catabolic process; IEA:Compara.
DR GO; GO:0001822; P:kidney development; IEA:Compara.
DR GO; GO:0007595; P:lactation; IEA:Compara.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Compara.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR GO; GO:0031100; P:organ regeneration; IEA:Compara.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Compara.
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 InterPro; IPR005854; Amd_phspho_trans.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR000583; GATase_dom.
DR InterPro; IPR000836; PRibTrfase_dom.
DR Pfam; PF00310; GATase_2; 2.
DR Pfam; PF00156; Pribosyltran; 1.
DR PIRSF; PIRSF000485; Amd_phspho_trans; 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; 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 Probable.
FT /FTId=PRO_0000029283.
FT CHAIN 12 517 Amidophosphoribosyltransferase.
FT /FTId=PRO_0000029284.
FT DOMAIN 12 261 Glutamine amidotransferase type-2.
FT ACT_SITE 12 12 For GATase activity (By similarity).
FT METAL 280 280 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 327 327 Magnesium (By similarity).
FT METAL 389 389 Magnesium (By similarity).
FT METAL 390 390 Magnesium (By similarity).
FT METAL 426 426 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 503 503 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 506 506 Iron-sulfur (4Fe-4S) (By similarity).
FT CONFLICT 369 369 V -> I (in Ref. 2; AAC27345).
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
//
