ID A0A0V8HJD8_9BACI Unreviewed; 373 AA.
AC A0A0V8HJD8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cysteine synthase {ECO:0000313|EMBL:SCC07599.1};
GN ORFNames=GA0061094_2305 {ECO:0000313|EMBL:SCC07599.1};
OS [Bacillus] enclensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=1402860 {ECO:0000313|EMBL:SCC07599.1, ECO:0000313|Proteomes:UP000181997};
RN [1] {ECO:0000313|EMBL:SCC07599.1, ECO:0000313|Proteomes:UP000181997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGD-1123 {ECO:0000313|EMBL:SCC07599.1,
RC ECO:0000313|Proteomes:UP000181997};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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; FMAU01000002; SCC07599.1; -; Genomic_DNA.
DR RefSeq; WP_058298489.1; NZ_KQ758483.1.
DR AlphaFoldDB; A0A0V8HJD8; -.
DR OrthoDB; 9803887at2; -.
DR Proteomes; UP000181997; Unassembled WGS sequence.
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; 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: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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 373 AA; 41225 MW; E5C98BC2F7DA185E CRC64;
MSKHIDTILV QSGNRTDSRT GAVSPAIYLS TAYEHQGIGK STGFDYSRTG NPTRFILEDT
LAQLEEGRRA FAFSSGMAAI QAILNLFSSG DELIVSEDLY GGSYRLFLQY ENQYNIRFHF
VDTADESRII EKINGSTKGI FLETPTNPLM NETSISTVSS VAKDNGLLLI VDNTFYTPIL
QKPITEGADI VVHSATKYLG GHNDVLAGAV IARDEDLGEK IYTVQNSIGA VLSPFDSWLL
LRGMKTLSLR IAQHEKNARV IAEYLTNNEC VTDVLYPGRG GMLSFRISRE EWVGPFLEKL
KVITFAESLG GVESFITYPA TQTHADIPVK ERNKIGICNR LLRFSVGIEN VGDIIADLDN
VFNQLKGEVL TYE
//
