ID   B0K2V1_THEPX            Unreviewed;       341 AA.
AC   B0K2V1;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:ABY93156.1};
DE            EC=2.5.1.48 {ECO:0000313|EMBL:ABY93156.1};
GN   OrderedLocusNames=Teth514_1876 {ECO:0000313|EMBL:ABY93156.1};
OS   Thermoanaerobacter sp. (strain X514).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=399726 {ECO:0000313|EMBL:ABY93156.1, ECO:0000313|Proteomes:UP000002155};
RN   [1] {ECO:0000313|EMBL:ABY93156.1, ECO:0000313|Proteomes:UP000002155}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X514 {ECO:0000313|EMBL:ABY93156.1,
RC   ECO:0000313|Proteomes:UP000002155};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT   "Complete sequence of Thermoanaerobacter sp. X514.";
RL   Submitted (JAN-2008) 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; CP000923; ABY93156.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0K2V1; -.
DR   KEGG; tex:Teth514_1876; -.
DR   HOGENOM; CLU_018986_5_0_9; -.
DR   Proteomes; UP000002155; 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:SF90; CYSTATHIONINE GAMMA-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:ABY93156.1}.
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   341 AA;  38451 MW;  B9E15A911F25A082 CRC64;
     MGVNKNYRFD TKVIHGNEFK KNPENALNPP IFQTTTFVFD DLEHVEKVMS FQSQDYVYTR
     GNNPTLRLFE NRLAELEYGK GAVAFSSGMA AISSVLFSLL KPKDNVIIHK TLYGSSYNVV
     TNILPKYGVN YKIVDLTDIS ELEKSIDDST KVVYFETPSN PNLSIIDIEE VARVCHKKDI
     KIVVDNTFAT PYFQNPLLLG ADVVVHSATK YIGGHGDALG GVAVSQDEKY IHYLKFDYMC
     EFGGVMSPFN AWLMLRGIKT LGIRMRQHEK NAIEVANFLN SHPKVKNVMY PGLKSFKGYE
     IAKKQMRGFG AIISFEIEGG TKNLEKFIVN SQIKSPKIFK L
//