(data stored in SCRATCH zone)

SWISSPROT: D4YYU1_SPHJU

ID   D4YYU1_SPHJU            Unreviewed;       407 AA.
AC   D4YYU1;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 45.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:BAI95523.1};
DE            EC=4.4.1.8 {ECO:0000313|EMBL:BAI95523.1};
GN   Name=metC {ECO:0000313|EMBL:BAI95523.1};
GN   OrderedLocusNames=SJA_C1-06890 {ECO:0000313|EMBL:BAI95523.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95523.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95523.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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; AP010803; BAI95523.1; -; Genomic_DNA.
DR   RefSeq; WP_013039212.1; NC_014006.1.
DR   ProteinModelPortal; D4YYU1; -.
DR   STRING; 452662.SJA_C1-06890; -.
DR   EnsemblBacteria; BAI95523; BAI95523; SJA_C1-06890.
DR   GeneID; 29272361; -.
DR   KEGG; sjp:SJA_C1-06890; -.
DR   eggNOG; ENOG4105C28; Bacteria.
DR   eggNOG; COG0626; LUCA.
DR   HOGENOM; HOG000246416; -.
DR   KO; K01760; -.
DR   OMA; PTHFAFQ; -.
DR   OrthoDB; POG091H053G; -.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
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; IPR006233; Cys_b_lyase_bac.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR43500:SF1; PTHR43500:SF1; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01324; cysta_beta_ly_B; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YYU1.
DR   SWISS-2DPAGE; D4YYU1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Lyase {ECO:0000313|EMBL:BAI95523.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2,
KW   ECO:0000256|RuleBase:RU362118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   MOD_RES     222    222       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR001434-2}.
SQ   SEQUENCE   407 AA;  44011 MW;  4579C3910BF9E1F6 CRC64;
     MSRDSDKRRD RKPLTQIAQA GRKPEWTGMP GQPGGIVNPP VWRASTILYD DVAHLRSAAG
     RSTHERLFYG RKGTPTAWSL ADALTEMEPG AEGTMLYPSG VAAIACALMA VLKPGDQLLM
     VDSAYDPTRN FCEQMLRPLG IETVYYDPMA GAGIADLITD ATRAIFLESP GSLTFEVQDV
     PAITAIARDR GIATLIDNTW ATPWFFPALS HGVDISILAC TKYIVGHSDV MIGSVTATPA
     FFAKIRQAAY LFGQMTSPDD AWLAARGLRT LGVRLNQHQA SALRIAQWLA QQPDVARVLH
     PALPSCPGHA LWQRDFTGSS GLFSFVLKGG DEKARAALID GLAHFGIGYS WGGFESLALP
     VDPARYRTAT AWQAEGPVVR LQIGLEDSDD LMADLDASLA RFRAARG
//

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