(data stored in ACNUC7421 zone)

SWISSPROT: Q47ST9_THEFY

ID   Q47ST9_THEFY            Unreviewed;       381 AA.
AC   Q47ST9;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:AAZ54478.1};
DE            EC=4.4.1.1 {ECO:0000313|EMBL:AAZ54478.1};
GN   OrderedLocusNames=Tfu_0440 {ECO:0000313|EMBL:AAZ54478.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54478.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ54478.1; -; Genomic_DNA.
DR   RefSeq; WP_011290887.1; NC_007333.1.
DR   STRING; 269800.Tfu_0440; -.
DR   EnsemblBacteria; AAZ54478; AAZ54478; Tfu_0440.
DR   KEGG; tfu:Tfu_0440; -.
DR   eggNOG; ENOG4105C28; Bacteria.
DR   eggNOG; COG0626; LUCA.
DR   HOGENOM; HOG000246415; -.
DR   KO; K01739; -.
DR   OMA; HPGRMTH; -.
DR   OrthoDB; 637281at2; -.
DR   BioCyc; TFUS269800:G1G4Q-447-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); 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; 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   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47ST9.
DR   SWISS-2DPAGE; Q47ST9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Lyase {ECO:0000313|EMBL:AAZ54478.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2,
KW   ECO:0000256|RuleBase:RU362118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   MOD_RES     200    200       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR001434-2}.
SQ   SEQUENCE   381 AA;  40430 MW;  BC6858FC31F11575 CRC64;
     MSYEGFETLA IHAGQEADAE TGAVVVPIYQ TSTYRQDGVG GLRGGYEYSR TANPTRTALE
     ECLAALEGGV RGLAFASGMA AEDTLLRTIA RPGDHLIIPN DAYGGTFRLV SKVFERWGVS
     WDAVDLSNPE AVRTAIRPET VAIWVETPTN PLLNIADIAA LADIAHAADA LLVVDNTFAS
     PYLQRPLSLG ADVVVHSTTK YLGGHSDVVG GALVVADAEL GERLAFHQNS MGAVAGPFDA
     WLTLRGIKTL GVRMDRHCAN AERVVEALVG HPEVAEVLYP GLSDHPGHKV AVDQMRAFGG
     MVSFRMRGGE EAALRVCAKT KVFTLAESLG GVESLIEHPG KMTHASTAGS LLEVPSDLVR
     LSVGIETVDD LVNDLLQALE P
//

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