(data stored in SCRATCH zone)

SWISSPROT: A0A0E1P079_YERPA

ID   A0A0E1P079_YERPA        Unreviewed;       329 AA.
AC   A0A0E1P079;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   05-DEC-2018, entry version 19.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABG12232.1};
GN   OrderedLocusNames=YPA_0263 {ECO:0000313|EMBL:ABG12232.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12232.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12232.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12232.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; CP000308; ABG12232.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABG12232; ABG12232; YPA_0263.
DR   EnsemblBacteria; AJJ80948; AJJ80948; CH58_3109.
DR   KEGG; ypa:YPA_0263; -.
DR   PATRIC; fig|360102.15.peg.3260; -.
DR   KO; K01739; -.
DR   OMA; HPGRMTH; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR011821; O_succ_thio_ly.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR11808; PTHR11808; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR02080; O_succ_thio_ly; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1P079.
DR   SWISS-2DPAGE; A0A0E1P079.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU362118}.
SQ   SEQUENCE   329 AA;  35780 MW;  265C3407F1EA5573 CRC64;
     MTRKQATIAV RSGLNDDEQY GCVVPPIHLS STYNFIDFNQ PRTHDYSRRG NPTRDVVQRA
     LAELEGGAGA VMTSSGMSAL HLVCTTFLQP GDLLVAPHDC YGGSYRLFDS LSKRGAYRVL
     FVDQGDEAAL NCALAEKPKL VLIETPSNPL LRVVDIAAIC QAARAAGALT VCDNTFLSPA
     LQQPLSLGAD LVVHSCTKYL NGHSDVVAGA VIAKDPELVV ELAWWANNIG VTGAAFDSYL
     LLRGLRTLSP RMAQQQRNAD DIVRYLQQQP LVKKLYHPSL PQHPGHEIAC RQQSGFGAML
     SFELDGDEQV MRRFLSALEL FTLAESLGG
//

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