ID   A0A0V8JLI2_9BACI        Unreviewed;       392 AA.
AC   A0A0V8JLI2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KSU87857.1};
DE            EC=2.5.1.48 {ECO:0000313|EMBL:KSU87857.1};
GN   ORFNames=AS180_11135 {ECO:0000313|EMBL:KSU87857.1};
OS   Priestia veravalensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1414648 {ECO:0000313|EMBL:KSU87857.1, ECO:0000313|Proteomes:UP000053681};
RN   [1] {ECO:0000313|EMBL:KSU87857.1, ECO:0000313|Proteomes:UP000053681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SGD-V-76 {ECO:0000313|EMBL:KSU87857.1,
RC   ECO:0000313|Proteomes:UP000053681};
RA   Dastager S.G., Mawlankar R.;
RT   "Bacillus caseinolyticus sp nov.";
RL   Submitted (NOV-2015) 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:KSU87857.1}.
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DR   EMBL; LNQP01000034; KSU87857.1; -; Genomic_DNA.
DR   RefSeq; WP_062686819.1; NZ_KQ758650.1.
DR   AlphaFoldDB; A0A0V8JLI2; -.
DR   Proteomes; UP000053681; Unassembled WGS sequence.
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:SF15; 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:UP000053681};
KW   Transferase {ECO:0000313|EMBL:KSU87857.1}.
FT   MOD_RES         201
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   392 AA;  43200 MW;  1553811C38E2E393 CRC64;
     MHTTNKHSFG TNLIHAKTGI DGHFGAVNVP IYQVSTFNLE DETNGGRYDY SRSGNPTREA
     LENTIAQLEN GAAGFAFSSG MAAVSSVLCL FEAGDEIIVS NDIYGGTYRV LTRLFSKFGI
     KTTFVNMTNV DEVEEVISSQ TKAIYIESPS NPFLQVTDIK SVAALAKRYD LLTIVDNTFM
     TPYLQQPINL GANIVIHSAT KYISGHSDVI GGLVVVSDEK LADEVKFVQN AFGAILGPQD
     CFLFLRGIKT LKVRLDQQQQ TALELAKWFE EQRDVEAVYY PGLKTHPDYE LITEQANGYG
     AIISFKLNND ELAQHILKNV RLSSIGVSLG AVESILTHPA TMSHASIPKE VREKKGITES
     LLRLSVGLEE YEDLKEDFNN ALISFQEKAV TK
//