ID   A0A2V3WK49_9BACI        Unreviewed;       380 AA.
AC   A0A2V3WK49;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:PXW93048.1};
GN   ORFNames=DES38_101129 {ECO:0000313|EMBL:PXW93048.1};
OS   Streptohalobacillus salinus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Streptohalobacillus.
OX   NCBI_TaxID=621096 {ECO:0000313|EMBL:PXW93048.1, ECO:0000313|Proteomes:UP000247922};
RN   [1] {ECO:0000313|EMBL:PXW93048.1, ECO:0000313|Proteomes:UP000247922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22440 {ECO:0000313|EMBL:PXW93048.1,
RC   ECO:0000313|Proteomes:UP000247922};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-2018) 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}.
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:PXW93048.1}.
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DR   EMBL; QJJR01000001; PXW93048.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V3WK49; -.
DR   OrthoDB; 9803887at2; -.
DR   Proteomes; UP000247922; 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: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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247922}.
FT   MOD_RES         205
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   380 AA;  40973 MW;  56DBFFE20B6C1A34 CRC64;
     MTKSFETRAV HINHEKPLPT NSKVTPIYQS SAFSFKDLDD VEAFYQGKKD YLYSRVGNPN
     PDELADSVAQ LEGAPSGVSA SSGLAAILIG VLSMVEAGDE IIASTDIYGG TYELFQTELT
     SFGITVHFAD FKDIDAVEAL ITDQTKCLYT ESITNPLLYV EDLQSIVALA KKHQLKTMID
     NTFATPYLIN PYSTGINLVV HSATKYLGGH SDITAGVVVG DSELIQKAKT RGVNLGTTLA
     PMEAWLTVRG IKTLALRMEK QVTNAQALAT RLTAHEGVKT VYYPKHASEK GNGAIVTIDL
     ADPIDVGTFF KSLGWVKIVP TLAGVETTVS YPKTTSHRAL PTDVQQSLGI TEGLVRISVG
     IENIDDIEAA FVQAINAAKK
//