(data stored in SCRATCH zone)

SWISSPROT: A4AVQ1_MARSH

ID   A4AVQ1_MARSH            Unreviewed;       170 AA.
AC   A4AVQ1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   RecName: Full=Adenine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00004, ECO:0000256|SAAS:SAAS01090472};
DE            Short=APRT {ECO:0000256|HAMAP-Rule:MF_00004};
DE            EC=2.4.2.7 {ECO:0000256|HAMAP-Rule:MF_00004, ECO:0000256|SAAS:SAAS01090463};
GN   Name=apt {ECO:0000256|HAMAP-Rule:MF_00004};
GN   OrderedLocusNames=FB2170_01367 {ECO:0000313|EMBL:EAQ99981.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAQ99981.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAQ99981.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation
CC       of AMP, that is energically less costly than de novo synthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00004, ECO:0000256|SAAS:SAAS01090470}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + diphosphate = 5-phospho-alpha-D-ribose 1-
CC         diphosphate + adenine; Xref=Rhea:RHEA:16609, ChEBI:CHEBI:16708,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:456215;
CC         EC=2.4.2.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00004,
CC         ECO:0000256|SAAS:SAAS01124295};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway;
CC       AMP from adenine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00004,
CC       ECO:0000256|SAAS:SAAS01090473}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00004,
CC       ECO:0000256|SAAS:SAAS01090458}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00004,
CC       ECO:0000256|SAAS:SAAS01090474}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00004, ECO:0000256|SAAS:SAAS01090468}.
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DR   EMBL; CP002157; EAQ99981.1; -; Genomic_DNA.
DR   RefSeq; WP_013304967.1; NC_014472.1.
DR   STRING; 313603.FB2170_01367; -.
DR   EnsemblBacteria; EAQ99981; EAQ99981; FB2170_01367.
DR   KEGG; fbc:FB2170_01367; -.
DR   eggNOG; ENOG4109003; Bacteria.
DR   eggNOG; COG0503; LUCA.
DR   HOGENOM; HOG000036776; -.
DR   KO; K00759; -.
DR   OMA; CAPIRKK; -.
DR   OrthoDB; 1532478at2; -.
DR   BioCyc; MSP313603:G1GNS-535-MONOMER; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-UniRule.
DR   GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 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   3: Inferred from homology;
DR   PRODOM; A4AVQ1.
DR   SWISS-2DPAGE; A4AVQ1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00004,
KW   ECO:0000256|SAAS:SAAS01090459};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00004,
KW   ECO:0000256|SAAS:SAAS01090465, ECO:0000313|EMBL:EAQ99981.1};
KW   Purine salvage {ECO:0000256|HAMAP-Rule:MF_00004,
KW   ECO:0000256|SAAS:SAAS01090461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00004,
KW   ECO:0000256|SAAS:SAAS01090460, ECO:0000313|EMBL:EAQ99981.1}.
FT   DOMAIN       31    148       Pribosyltran. {ECO:0000259|Pfam:PF00156}.
SQ   SEQUENCE   170 AA;  18927 MW;  75ECCE51695B283C CRC64;
     MNLKSFVRDI PDFPSKGVIF RDITPLLKDP KAIEYAKKAL LELLGNVKID KVVGMESRGF
     FFAPMLATEL NAGFVPVRKP GKLPYDTIRQ DYSLEYGTDA LEMHSDAILR GDKVLVHDDV
     LATGGTAKAT CELIEKMGGE IVQCNFLLEL DFLNGRGKLP DYDVKSLLLY
//

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