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Database: UniProt
Entry: A7GSV4_BACCN
LinkDB: A7GSV4_BACCN
Original site: A7GSV4_BACCN 
ID   A7GSV4_BACCN            Unreviewed;       370 AA.
AC   A7GSV4;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:ABS23212.1};
DE            EC=2.5.1.48 {ECO:0000313|EMBL:ABS23212.1};
GN   OrderedLocusNames=Bcer98_2985 {ECO:0000313|EMBL:ABS23212.1};
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS23212.1, ECO:0000313|Proteomes:UP000002300};
RN   [1] {ECO:0000313|EMBL:ABS23212.1, ECO:0000313|Proteomes:UP000002300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC   {ECO:0000313|Proteomes:UP000002300};
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; CP000764; ABS23212.1; -; Genomic_DNA.
DR   RefSeq; WP_012095449.1; NC_009674.1.
DR   AlphaFoldDB; A7GSV4; -.
DR   STRING; 315749.Bcer98_2985; -.
DR   GeneID; 56418529; -.
DR   KEGG; bcy:Bcer98_2985; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_1_9; -.
DR   OMA; YKQDGVG; -.
DR   OrthoDB; 9803887at2; -.
DR   Proteomes; UP000002300; Chromosome.
DR   GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11808:SF50; CYSTATHIONINE BETA-LYASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Transferase {ECO:0000313|EMBL:ABS23212.1}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         196
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   370 AA;  40869 MW;  0B01B5FDDB698BFE CRC64;
     MSTIETTLAQ IGNRSETGTG TVNPPVYFST AYRHEGIGKS TGFDYSRTGN PTRGLVERAI
     ADLEKGDQGY ACSSGMAAVL LVLSLFRSDD ELIVSEDLYG GTYRLFSEHE KKWNIRCRYV
     DTQSIEQIEH AITSKTKAIF IETPTNPLMQ VTDIQAVATI AKRHGLLLIV DNTFYTPYIQ
     QPLTDGADIV LHSATKYLGG HNDVLSGLVV AKGSGLCAEL AHYHNASGAV LSPFDSWLLI
     RGMKTLALRM KQHEENANKI VTYLKEEDGV TDVFYPGRGG MISFRLRDEK WINPFLQSLS
     IITFAESLGG VESLMTYPAT QTHADIPTDV RIARGVCNRL LRFSVGIEHS DDLIQDLQQA
     IQYAKEGVKI
//
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