ID   G7MA79_9CLOT            Unreviewed;       435 AA.
AC   G7MA79;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Cysteine synthase {ECO:0000313|EMBL:EHJ01845.1};
DE            EC=2.5.1.47 {ECO:0000313|EMBL:EHJ01845.1};
GN   ORFNames=CDLVIII_5363 {ECO:0000313|EMBL:EHJ01845.1};
OS   Clostridium sp. DL-VIII.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=641107 {ECO:0000313|EMBL:EHJ01845.1, ECO:0000313|Proteomes:UP000005106};
RN   [1] {ECO:0000313|EMBL:EHJ01845.1, ECO:0000313|Proteomes:UP000005106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DL-VIII {ECO:0000313|EMBL:EHJ01845.1,
RC   ECO:0000313|Proteomes:UP000005106};
RX   PubMed=23929491;
RA   Taghavi S., Izquierdo J.A., van der Lelie D.;
RT   "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT   Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL   Genome Announc. 1:e00605-e00613(2013).
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|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; CM001240; EHJ01845.1; -; Genomic_DNA.
DR   RefSeq; WP_009172483.1; NZ_CM001240.1.
DR   AlphaFoldDB; G7MA79; -.
DR   STRING; 641107.CDLVIII_5363; -.
DR   eggNOG; COG2873; Bacteria.
DR   HOGENOM; CLU_018986_4_0_9; -.
DR   Proteomes; UP000005106; Chromosome.
DR   GO; GO:0004124; F:cysteine synthase activity; 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; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR   PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR   PANTHER; PTHR43797:SF2; HOMOCYSTEINE_CYSTEINE SYNTHASE; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005106};
KW   Transferase {ECO:0000313|EMBL:EHJ01845.1}.
FT   MOD_RES         208
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   435 AA;  47738 MW;  EDA81E74978E55D6 CRC64;
     MGDYKFDTIK VRGGYNPKNH NDAVSVPIYA TASFEVGEAE RFDRLASLSE EGYIYSRLGN
     PTVSVLESRI AALDGGASAV GVASGMAAIT YALLAVAEGG GRILTTHQLY GGTVDALKKL
     YPKFGIQIDR IDNDSDIEEF RRAIKEDTKA IFIETISNPN AVISDIEKIA EVAHENDIPL
     IVDNTFATPY LLNPIKYGAD VVIYSATKAL SGHGNVIAGV IVDSGNFNWA NGKYPQFTQP
     HFTLKDLEGN ERSYIEAFKE SAFAGKIRLD YLTYFGAVLS PFDAYLILIG LETLSERVQK
     QVLNTEKIVE FLKTEEAVSW ISYPTVEGSP YKALADKYFP KGVGSTFTFG FNGNSEGIYK
     LINSVKLFSY QANVGDARSL IVNVPKTTHG ELTEEQLKLA KIPQETIRLS IGIEDAEDLI
     EDLKQAFKKA LNLFS
//