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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//