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APT_CAEEL
ID   APT_CAEEL               Reviewed;         185 AA.
AC   P91455;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Adenine phosphoribosyltransferase;
DE            Short=APRT;
DE            EC=2.4.2.7;
GN   ORFNames=T19B4.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Bristol N2;
RA   Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA   Thierry-Mieg D., Thierry-Mieg J.;
RT   "The Caenorhabditis elegans transcriptome project, a complementary view of
RT   the genome.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC       AMP, that is energically less costly than de novo synthesis.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate +
CC         adenine; Xref=Rhea:RHEA:16609, ChEBI:CHEBI:16708, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58017, ChEBI:CHEBI:456215; EC=2.4.2.7;
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from adenine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; FO080338; CCD62975.1; -; Genomic_DNA.
DR   EMBL; AF303266; AAG50224.1; -; mRNA.
DR   PIR; T25891; T25891.
DR   RefSeq; NP_491663.1; NM_059262.7.
DR   AlphaFoldDB; P91455; -.
DR   SMR; P91455; -.
DR   BioGRID; 37689; 23.
DR   STRING; 6239.T19B4.3; -.
DR   EPD; P91455; -.
DR   PaxDb; P91455; -.
DR   PeptideAtlas; P91455; -.
DR   EnsemblMetazoa; T19B4.3.1; T19B4.3.1; WBGene00020557.
DR   GeneID; 172232; -.
DR   KEGG; cel:CELE_T19B4.3; -.
DR   UCSC; T19B4.3.1; c. elegans.
DR   CTD; 172232; -.
DR   WormBase; T19B4.3; CE13740; WBGene00020557; -.
DR   eggNOG; KOG1712; Eukaryota.
DR   GeneTree; ENSGT00390000017259; -.
DR   HOGENOM; CLU_063339_3_2_1; -.
DR   InParanoid; P91455; -.
DR   OMA; KPGIVFR; -.
DR   OrthoDB; 1291050at2759; -.
DR   PhylomeDB; P91455; -.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   Reactome; R-CEL-74217; Purine salvage.
DR   UniPathway; UPA00588; UER00646.
DR   PRO; PR:P91455; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00020557; Expressed in larva and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0002055; F:adenine binding; IBA:GO_Central.
DR   GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR   GO; GO:0006168; P:adenine salvage; IBA:GO_Central.
DR   GO; GO:0044209; P:AMP salvage; IBA:GO_Central.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   HAMAP; MF_00004; Aden_phosphoribosyltr; 1.
DR   InterPro; IPR005764; Ade_phspho_trans.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01090; apt; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Glycosyltransferase; Purine salvage; Reference proteome;
KW   Transferase.
FT   CHAIN           1..185
FT                   /note="Adenine phosphoribosyltransferase"
FT                   /id="PRO_0000149511"
SQ   SEQUENCE   185 AA;  20210 MW;  91A984C4F770F268 CRC64;
     MTLPRFDQIR PKIEQHIREV KDFPKKGINF RDIMPLFTNP QLVNELCVVI ADHVRHTVGH
     VDSVAGLEAR GFLFGPQVAI QLGVPFVPIR KKGKLPGATI EASYVKEYGE DRVEIQEGAI
     KNGDIVFLID DLLATGGTLR AATDLVVKAG GKVGEAFVLI ELAPLNGRSK LPDVNLTTLI
     SYDSA
 
 
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