(data stored in SCRATCH zone)

SWISSPROT: D4YWX0_SPHJU

ID   D4YWX0_SPHJU            Unreviewed;       445 AA.
AC   D4YWX0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 39.
DE   SubName: Full=Cystathionine beta-lyase/cystathionine gamma-synthase {ECO:0000313|EMBL:BAI94852.1};
DE            EC=4.4.1.11 {ECO:0000313|EMBL:BAI94852.1};
GN   OrderedLocusNames=SJA_C1-00180 {ECO:0000313|EMBL:BAI94852.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI94852.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI94852.1, 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; BAI94852.1; -; Genomic_DNA.
DR   RefSeq; WP_013038700.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-00180; -.
DR   EnsemblBacteria; BAI94852; BAI94852; SJA_C1-00180.
DR   GeneID; 29271728; -.
DR   KEGG; sjp:SJA_C1-00180; -.
DR   eggNOG; ENOG4105C28; Bacteria.
DR   eggNOG; COG0626; LUCA.
DR   HOGENOM; HOG000246415; -.
DR   KO; K01761; -.
DR   OMA; FNAWVLS; -.
DR   OrthoDB; POG091H053G; -.
DR   BioCyc; SJAP452662:GHEL-18-MONOMER; -.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0018826; F:methionine gamma-lyase activity; IEA:UniProtKB-EC.
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.
PE   3: Inferred from homology;
DR   PRODOM; D4YWX0.
DR   SWISS-2DPAGE; D4YWX0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Lyase {ECO:0000313|EMBL:BAI94852.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2,
KW   ECO:0000256|RuleBase:RU362118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   MOD_RES     255    255       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR001434-2}.
SQ   SEQUENCE   445 AA;  47727 MW;  EE2F79DB299C59F6 CRC64;
     MTGETEADLT GAEPTRNRRR PKQPIMEIEG RKLKPATLMM GHGYDPTLSE GSLKPPIFLT
     STFAFESAAA GKRHFEGVTG IRPGGAEGLV YSRFNGPNQE IAEDRLSVWE EAEDALLFSS
     GMSAIATTLL ALVQPGDVIV HSAPLYAATE SLIGRILGKF GVQWLDFPAG ATEEEIGAVI
     EKAKGLGRVA LIYLESPANP TNVLVDLEAV VARRDFSFAG EEHRPPVAID NTFLGPLWLH
     PLSHGADLVI YSLTKYAGGH SDLVAGGVLG SNALINTIRL MRNTIGTILD PHSAWMLLRS
     LETLELRMSR AGENAARVCS WLKDQPQVEK VVYLGFPETE RQADIYRRHC TGAGSTFSLY
     LKGGEAEAFA FLDALKIAKL AVSLGGTETL ASHPAAMTHL SVPAERKKAL AIGDNMVRIS
     IGCEDAEDLI ADFAQALRAV EGAGG
//

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