(data stored in SCRATCH zone)

SWISSPROT: D6ZBQ9_SEGRD

ID   D6ZBQ9_SEGRD            Unreviewed;       201 AA.
AC   D6ZBQ9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 44.
DE   RecName: Full=Hypoxanthine phosphoribosyltransferase {ECO:0000256|RuleBase:RU364099};
DE            EC=2.4.2.8 {ECO:0000256|RuleBase:RU364099};
GN   OrderedLocusNames=Srot_0399 {ECO:0000313|EMBL:ADG96886.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96886.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96886.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-
CC         diphosphate + hypoxanthine; Xref=Rhea:RHEA:17973,
CC         ChEBI:CHEBI:17368, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017,
CC         ChEBI:CHEBI:58053; EC=2.4.2.8;
CC         Evidence={ECO:0000256|RuleBase:RU364099};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364099};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway;
CC       IMP from hypoxanthine: step 1/1. {ECO:0000256|RuleBase:RU364099}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364099}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000256|RuleBase:RU364099}.
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DR   EMBL; CP001958; ADG96886.1; -; Genomic_DNA.
DR   RefSeq; WP_013137342.1; NC_014168.1.
DR   STRING; 640132.Srot_0399; -.
DR   EnsemblBacteria; ADG96886; ADG96886; Srot_0399.
DR   KEGG; srt:Srot_0399; -.
DR   eggNOG; ENOG4108UGV; Bacteria.
DR   eggNOG; COG0634; LUCA.
DR   HOGENOM; HOG000236520; -.
DR   KO; K00760; -.
DR   OMA; TMDWMAV; -.
DR   OrthoDB; 1819460at2; -.
DR   BioCyc; SROT640132:G1GLH-402-MONOMER; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   InterPro; IPR005904; Hxn_phspho_trans.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01203; HGPRTase; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZBQ9.
DR   SWISS-2DPAGE; D6ZBQ9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Cytoplasm {ECO:0000256|RuleBase:RU364099};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU364099,
KW   ECO:0000313|EMBL:ADG96886.1};
KW   Magnesium {ECO:0000256|RuleBase:RU364099};
KW   Metal-binding {ECO:0000256|RuleBase:RU364099};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364099};
KW   Purine salvage {ECO:0000256|RuleBase:RU364099};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Transferase {ECO:0000256|RuleBase:RU364099,
KW   ECO:0000313|EMBL:ADG96886.1}.
FT   DOMAIN       27    181       Pribosyltran. {ECO:0000259|Pfam:PF00156}.
SQ   SEQUENCE   201 AA;  22113 MW;  E995B822270D7AAC CRC64;
     MNESAVAAAP QANWYDADVL SVVLTEEQIA ARTTQLAHQI AQNHPYRPGQ PRSEDLLLVT
     VLKGAVMFTA DLARSLPIPS QLEFMVVSSY GAATKSSGVV RIVKDLDRDI RGRDVLVVED
     VVDSGLTLSW LLRHLAAREP KSLEVCALLR KPEAQEAPVA LDYVGFDIPN VFVVGYGLDF
     DERYRDLPYL GELDPAAVER P
//

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