ID   A6CV47_9VIBR            Unreviewed;       387 AA.
AC   A6CV47;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   ORFNames=VSAK1_17432 {ECO:0000313|EMBL:EDL55803.1};
OS   Vibrio mediterranei AK1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=391591 {ECO:0000313|EMBL:EDL55803.1, ECO:0000313|Proteomes:UP000003769};
RN   [1] {ECO:0000313|EMBL:EDL55803.1, ECO:0000313|Proteomes:UP000003769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK1 {ECO:0000313|EMBL:EDL55803.1,
RC   ECO:0000313|Proteomes:UP000003769};
RA   Rosenberg E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
CC       {ECO:0000256|ARBA:ARBA00037974}.
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:EDL55803.1}.
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DR   EMBL; ABCH01000001; EDL55803.1; -; Genomic_DNA.
DR   RefSeq; WP_006069209.1; NZ_ABCH01000001.1.
DR   AlphaFoldDB; A6CV47; -.
DR   Proteomes; UP000003769; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR027619; C-S_lyase_PatB-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR04350; C_S_lyase_PatB; 1.
DR   PANTHER; PTHR43525; PROTEIN MALY; 1.
DR   PANTHER; PTHR43525:SF1; PROTEIN MALY; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:EDL55803.1};
KW   Transferase {ECO:0000313|EMBL:EDL55803.1}.
FT   DOMAIN          40..382
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   387 AA;  42738 MW;  1CFAFB9F8BA1D892 CRC64;
     MFNFDEIVER RGTHSAKWDE MESSFGVSPD EGLPMWVADM DFKAPPAVNQ VLMEAADNGV
     NGYYGDDHRY RNAVITWMSK RHQWSVQPEW IVTCAGLVQG TALCVQAYSK PGDGVILFTP
     VYHAFSRVIN ANKRVVVESP LVQEDGHYKM DLPALAANLN GREKMVILCS PHNPGGRVWS
     ADEIREVAEF CAQHDLILVV DEIHHDLVFP PNKHIVATLA APKHEQNMVI LAATTKTFNI
     ASALTGAAII PNETLRAQYT SVLNAAGVGP NRIGMLMATA AYEQGEAWLE ALVEYLDENR
     RLFDEAINAI DGLQSMTLQA TYLSWVDFSG TGLTPDQVIE KVQSEAKIAA NHGSSFGTGG
     EQFLRFNLAT PRARVVEAIE RLQRVFA
//