(data stored in SCRATCH zone)

SWISSPROT: D6XXG5_BACIE

ID   D6XXG5_BACIE            Unreviewed;       386 AA.
AC   D6XXG5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 56.
DE   SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:ADH98022.1};
DE            EC=4.4.1.1 {ECO:0000313|EMBL:ADH98022.1};
GN   OrderedLocusNames=Bsel_0484 {ECO:0000313|EMBL:ADH98022.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98022.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98022.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001791; ADH98022.1; -; Genomic_DNA.
DR   RefSeq; WP_013171451.1; NC_014219.1.
DR   STRING; 439292.Bsel_0484; -.
DR   EnsemblBacteria; ADH98022; ADH98022; Bsel_0484.
DR   KEGG; bse:Bsel_0484; -.
DR   eggNOG; COG0626; LUCA.
DR   HOGENOM; HOG000246415; -.
DR   KO; K01760; -.
DR   OMA; AVDNCFC; -.
DR   OrthoDB; 637281at2; -.
DR   BioCyc; BSEL439292:G1GLR-514-MONOMER; -.
DR   Proteomes; UP000000271; 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; D6XXG5.
DR   SWISS-2DPAGE; D6XXG5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Lyase {ECO:0000313|EMBL:ADH98022.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2,
KW   ECO:0000256|RuleBase:RU362118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   MOD_RES     199    199       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR001434-2}.
SQ   SEQUENCE   386 AA;  42209 MW;  04019E67D340AE49 CRC64;
     MTESLDIQTR LLHHRHKTDP HNGAVSVGVQ HASTFHQNSL EQFGAYDYAR SGNPTREALE
     EIFAGLENGT DAFAFASGMA AISTTFMLLS SGDHLVITED VYGGTFRMTT EVLTRLGIEH
     TFVDMTRVDE VKATLQDNTK MIFMETPSNP TMKITPIRDI VALAEAHDCL TVLDNTFMTP
     VLQRPLDLGV DIVVHSATKF IGGHSDVVSG LAVVKRPDLA GRLGFLQNSF GAIPGPDDCW
     LIMRGLKTLH TRMMVSQEVA SNLAHWLDVQ PEVKRVYYPG FSDQLGNAIH AGQSDGPGAV
     LSFELADREA VSRFSQAVEI PVFAVSLGAV ESILSYPAKM SHAAMPDHER VARGITDGLL
     RLSVGLESEA DLKRDFRQAF DSLARM
//

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