ID C3G867_BACTU Unreviewed; 409 AA.
AC C3G867;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Cystathionine gamma-synthase / cysteine synthase {ECO:0000313|EMBL:EEM69931.1};
GN ORFNames=bthur0009_40230 {ECO:0000313|EMBL:EEM69931.1};
OS Bacillus thuringiensis serovar andalousiensis BGSC 4AW1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=527032 {ECO:0000313|EMBL:EEM69931.1};
RN [1] {ECO:0000313|EMBL:EEM69931.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 4AW1 {ECO:0000313|EMBL:EEM69931.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEM69931.1}.
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DR EMBL; ACNG01000094; EEM69931.1; -; Genomic_DNA.
DR AlphaFoldDB; C3G867; -.
DR HOGENOM; CLU_018986_2_0_9; -.
DR Proteomes; UP000001380; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; 2.
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:SF91; CYSTATHIONINE GAMMA-SYNTHASE; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT MOD_RES 235
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 409 AA; 45900 MW; B54FB203139B89E8 CRC64;
MKDLTDEKKT LFKPKAFFLE GFFYFIFNYW FNLKRRNFYM STIETKLAQI GNRSETTTGT
VNPPVYFSTA YRHEGIGKST GFDYSRTGNP TRGLLEQAIA DLEYGEQGYA CSSGMAAVLL
VLSLFRSGDE LIVSEDLYGG TYRLFSEHEK KWNVRCRYVN TQSIKQIEQA ITTETKAIFI
ETPTNPLMQV TDIAAVATVA KRHGLLLIVD NTFYTPYIQQ PLTEGADIVL HSATKYLGGH
NDVLSGLVVA KGKELCEEIA HYHNASGAVL SPFDSWLLIR GMKTLALRMR QHEENAKAVV
AYLNDEDGVT DVFYPGRGGM ISFRLKDETW INPFLQSLSL ITFAESLGGV ESLMTYPATQ
THADIPEEIR TANGVCNRLL RFSVGIENSN DLIQDLQQAI KLVKEGVRI
//
