(data stored in ACNUC9543 zone)

SWISSPROT: A0A0H2Y5I8_YERPA

ID   A0A0H2Y5I8_YERPA        Unreviewed;       434 AA.
AC   A0A0H2Y5I8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 18.
DE   SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:ABG12467.1};
DE            EC=2.8.1.7 {ECO:0000313|EMBL:ABG12467.1};
GN   OrderedLocusNames=YPA_0499 {ECO:0000313|EMBL:ABG12467.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12467.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12467.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12467.1,
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:RU004504,
CC         ECO:0000256|SAAS:SAAS00608357};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU004075,
CC       ECO:0000256|SAAS:SAAS00544146}.
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DR   EMBL; CP000308; ABG12467.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABG12467; ABG12467; YPA_0499.
DR   KEGG; ypa:YPA_0499; -.
DR   KO; K01766; -.
DR   OMA; QGVVHGR; -.
DR   BioCyc; YPES360102:GHZU-522-MONOMER; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR022471; Cys_desulphurase_CdsA.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03392; FeS_syn_CsdA; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2Y5I8.
DR   SWISS-2DPAGE; A0A0H2Y5I8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Pyridoxal phosphate {ECO:0000256|SAAS:SAAS00427524};
KW   Transferase {ECO:0000313|EMBL:ABG12467.1}.
FT   DOMAIN       55    421       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
SQ   SEQUENCE   434 AA;  47604 MW;  179A1D0576659F14 CRC64;
     MCITSICITS LLKHATMIKA KKFRGHSQDA NNSMKVFNPM DFRREFPALS DKLTYLDSAA
     TALKPRAMID ATQQFYQQDS ATVHRSQHQS ALSLTVRFEN TRQQVADFIN SSTAENIIWT
     RGTTEAINLI AQSYARPRLQ PEDEIIVSEA EHHANLIPWL MVAEQTGAKI VKLPLGLDHL
     PDLQQLPQLL NEKTRILALG QMSNVTGGSP DLAQAIRLAH QYDCVVVVDG AQGIVHYPAD
     VQALDIDFYA FSSHKLYGPT GIGVLYGKTE LLEEMPAWQG GGKMLTHASF GGFTPHEVPY
     RFEAGTPNIA GVIGLSAVLK WLEHIDLEEA EVYSQGLATM AENKLAQLPG FHSYRCQQSS
     LLAFTFDGVH HSDLVALLAE QGIALRAGQH CAQPLMAALG VNGSLRASFA PYNTPQDVEM
     LCSALGKALE LLRD
//

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