ID   A3JRL5_9RHOB            Unreviewed;       390 AA.
AC   A3JRL5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   ORFNames=RB2150_07878 {ECO:0000313|EMBL:EBA04405.1};
OS   Rhodobacteraceae bacterium HTCC2150.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA04405.1, ECO:0000313|Proteomes:UP000004731};
RN   [1] {ECO:0000313|EMBL:EBA04405.1, ECO:0000313|Proteomes:UP000004731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA04405.1,
RC   ECO:0000313|Proteomes:UP000004731};
RX   PubMed=20889754; DOI=10.1128/JB.01088-10;
RA   Kang I., Oh H.M., Vergin K.L., Giovannoni S.J., Cho J.C.;
RT   "Genome sequence of the marine alphaproteobacterium HTCC2150, assigned to
RT   the Roseobacter clade.";
RL   J. Bacteriol. 192:6315-6316(2010).
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:EBA04405.1}.
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DR   EMBL; AAXZ01000002; EBA04405.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3JRL5; -.
DR   eggNOG; COG1168; Bacteria.
DR   OrthoDB; 3224382at2; -.
DR   Proteomes; UP000004731; 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:EBA04405.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004731};
KW   Transferase {ECO:0000313|EMBL:EBA04405.1}.
FT   DOMAIN          42..382
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   390 AA;  43586 MW;  0D2604FB6C236D02 CRC64;
     MNFDKVTDRR GSRSVKWDSM ESNYGVSNID GIAMWVADTD FPPPACVTNA LQSMVDHNVY
     GYYGDDTDYK ASIQWWMKNR HNWPIELDWI FTTFGLVNAV GICVDIFSES DDGVVLFTPV
     YHAFARVIEN AERKVVELEL RNENGHLSMD FDAYDAQMQG HEKIMIISSP HNPGGRVWTK
     DELLEITAFA KRHDLILLSD EIHHDLVFAG NKHIPTALAD PSAADRLLTL TAASKTFNVA
     GGYTGNVIIQ DEILRKKFAK RLAMLGMSKN SFGVEIVRAA YSPEGAEWVD ELIAYIDGNR
     RVFDEGINAI PGLKSMPLQS TYLAWVDFSG TGMSREEFTD RVEKQAKIAA NHGTTFGKGG
     DNFLRFNLGA PRSVIEEAVS RLQAAFSDLQ
//