ID   A3Y966_9GAMM            Unreviewed;       382 AA.
AC   A3Y966;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   ORFNames=MED121_06440 {ECO:0000313|EMBL:EAQ66299.1};
OS   Marinomonas sp. MED121.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=314277 {ECO:0000313|EMBL:EAQ66299.1, ECO:0000313|Proteomes:UP000003436};
RN   [1] {ECO:0000313|EMBL:EAQ66299.1, ECO:0000313|Proteomes:UP000003436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED121 {ECO:0000313|EMBL:EAQ66299.1,
RC   ECO:0000313|Proteomes:UP000003436};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (JAN-2006) 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:EAQ66299.1}.
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DR   EMBL; AANE01000003; EAQ66299.1; -; Genomic_DNA.
DR   RefSeq; WP_009835519.1; NZ_CH672433.1.
DR   AlphaFoldDB; A3Y966; -.
DR   STRING; 314277.MED121_06440; -.
DR   HOGENOM; CLU_017584_15_0_6; -.
DR   OrthoDB; 3224382at2; -.
DR   Proteomes; UP000003436; 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:EAQ66299.1};
KW   Transferase {ECO:0000313|EMBL:EAQ66299.1}.
FT   DOMAIN          37..378
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   382 AA;  43106 MW;  B5CEEBAA6AE9B697 CRC64;
     MSDFDLQETT LIKAKDRQNT QSIKWEKFPG DIIPMWVADM DFESPKPIIQ ALQERVSDGV
     FGYTKADDSL NQAIIDNAYK QYTWQIKSKD INYLPGLVCA LHVAVRAFTK EDEGVIIPGP
     VYFHLTKAAQ LANRTIHAIP MTLEENRWLP DMDAFAKACA DSKSKLILLC NPHNPGGTVF
     NREELTKIHA LAKQHDLTVV SDEIHCDLIL DEGLKHIPFA SLNEDAANRT VTLMAPSKTY
     NVAGLGLAYS VIQNLTLRNI FNLARSGIMP DPNLLAFNAT KSAYTECQDW HQDLIKYLRK
     NRDLIYQKLS HTQCKISKIE ATYLAWIDVS YLKLEDAEAY FLKAGVAISD GKQFGNSNFI
     RLNFGCSHQQ LDQALTRLLK VL
//