(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZKV7_PSEAB

ID   A0A0H2ZKV7_PSEAB        Unreviewed;       394 AA.
AC   A0A0H2ZKV7;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 9.
DE   SubName: Full=Probable cystathionine gamma-lyase {ECO:0000313|EMBL:ABJ15367.1};
GN   OrderedLocusNames=PA14_05230 {ECO:0000313|EMBL:ABJ15367.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15367.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15367.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15367.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(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; CP000438; ABJ15367.1; -; Genomic_DNA.
DR   RefSeq; WP_003110017.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZKV7; -.
DR   EnsemblBacteria; ABJ15367; ABJ15367; PA14_05230.
DR   KEGG; pau:PA14_05230; -.
DR   KO; K01758; -.
DR   OMA; MQTKLIH; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR11808; PTHR11808; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZKV7.
DR   SWISS-2DPAGE; A0A0H2ZKV7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Lyase {ECO:0000313|EMBL:ABJ15367.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2,
KW   ECO:0000256|RuleBase:RU362118}.
FT   MOD_RES     208    208       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR001434-2}.
SQ   SEQUENCE   394 AA;  42757 MW;  E2487BCA8CCE617A CRC64;
     MSQHDQHPDA PAQAFATRVI HAGQAPDPST GAIMPPIYAN STYIQESPGV HKGLDYGRSH
     NPTRWALERC VADLEGGAQA FAFASGLAAI SSVLELLDAG SHIVSGNDLY GGTFRLFERV
     RRRSAGHRFS FVDPTDLQAF EAALTPETRM VWVETPSNPL LRLTDLRAIA QLCRARGIIS
     VADNTFASPY IQRPLELGFD VVVHSTTKYL NGHSDVIGGI AIVGDNPDLR ERLGFLQNSV
     GAISGPFDAF LTLRGVKTLA LRMERHCSNA LALAQWLERQ PQVARVYYPG LASHPQHELA
     KRQMRGFGGM ISLDLRCDLA GARRFLENVR IFSLAESLGG VESLIEHPAI MTHASIPAET
     RADLGIGDSL IRLSVGVEAL EDLQADLAQA LAKI
//

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