(data stored in SCRATCH zone)

SWISSPROT: D6XY10_BACIE

ID   D6XY10_BACIE            Unreviewed;       377 AA.
AC   D6XY10;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 57.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:ADH98083.1};
DE            EC=2.5.1.48 {ECO:0000313|EMBL:ADH98083.1};
GN   OrderedLocusNames=Bsel_0547 {ECO:0000313|EMBL:ADH98083.1};
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:ADH98083.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98083.1, 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; ADH98083.1; -; Genomic_DNA.
DR   RefSeq; WP_013171512.1; NC_014219.1.
DR   STRING; 439292.Bsel_0547; -.
DR   EnsemblBacteria; ADH98083; ADH98083; Bsel_0547.
DR   KEGG; bse:Bsel_0547; -.
DR   eggNOG; ENOG4105C28; Bacteria.
DR   eggNOG; COG0626; LUCA.
DR   HOGENOM; HOG000246415; -.
DR   OMA; NPTVARF; -.
DR   OrthoDB; 637281at2; -.
DR   BioCyc; BSEL439292:G1GLR-587-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0003962; F:cystathionine gamma-synthase 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; 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; D6XY10.
DR   SWISS-2DPAGE; D6XY10.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2,
KW   ECO:0000256|RuleBase:RU362118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Transferase {ECO:0000313|EMBL:ADH98083.1}.
FT   MOD_RES     203    203       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR001434-2}.
SQ   SEQUENCE   377 AA;  40620 MW;  90BA52AFEAE3BCE4 CRC64;
     MKFRTDNVHL KKAQTSGEYS KTTPIYQTSA FAFKDIDDME QYFNGDKSYL YTRMGNPNTD
     ELGQAVAALE GAEAGVASSS GLSAILAGFL SVAKPGDHVI VAEDLYGGTF QLINDEIQGL
     GIRVTFMDMT NVKDVEAAIT ADTVMIYTES ITNPLLRVED LEGISALAKA HDLKLMVDNT
     FATPYLIRPL ENGADLVVHS ATKYIGGHSD VTAGVIVGGE ALISEARKKI VTLGSNLGPF
     DSWLAVRGLK TLSLRMRAQC ENAQKLSDAL RQTQGIKKVY YPEHASDSGN GAVVTIDLED
     GLDVNAFTRA LDWVKVVPTL AGVETTVSYP EGTSHRALTP EMRTRLGVTP QMIRISVGIE
     DPDDIVGVFV NAVAAIR
//

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