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Database: UniProt
Entry: A0A132C255_9RHOB
LinkDB: A0A132C255_9RHOB
Original site: A0A132C255_9RHOB 
ID   A0A132C255_9RHOB        Unreviewed;       390 AA.
AC   A0A132C255;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   Name=patB {ECO:0000313|EMBL:KUP94120.1};
GN   ORFNames=TRIHO_09750 {ECO:0000313|EMBL:KUP94120.1};
OS   Tritonibacter horizontis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Tritonibacter.
OX   NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP94120.1, ECO:0000313|Proteomes:UP000068382};
RN   [1] {ECO:0000313|EMBL:KUP94120.1, ECO:0000313|Proteomes:UP000068382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O3.65 {ECO:0000313|EMBL:KUP94120.1,
RC   ECO:0000313|Proteomes:UP000068382};
RA   Poehlein A., Giebel H.A., Voget S., Brinkhoff T.;
RT   "Genome sequence of the marine Rhodobacteraceae strain O3.65, Candidatus
RT   Tritonibacter horizontis.";
RL   Submitted (DEC-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   -!- 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:KUP94120.1}.
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DR   EMBL; LPUY01000027; KUP94120.1; -; Genomic_DNA.
DR   RefSeq; WP_068240885.1; NZ_LPUY01000027.1.
DR   AlphaFoldDB; A0A132C255; -.
DR   PATRIC; fig|1768241.3.peg.1013; -.
DR   OrthoDB; 3224382at2; -.
DR   Proteomes; UP000068382; Unassembled WGS sequence.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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   Lyase {ECO:0000313|EMBL:KUP94120.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068382}.
FT   DOMAIN          39..382
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   390 AA;  43137 MW;  01EE2E41F837A2DE CRC64;
     MDFDTIIDRR GTHCAKWDMM EPLYGVSPED GLAMWVADMD FAVPDVVTDR LREMVDHGIH
     GYVNRESEYK GAIQWWMENR HGWRVDADAI FTTTGLVNGV GMCLDAFTQA GDGIVLFTPV
     YHAFAKVIRL AGRAVVECPM VQEDGAYRMD FAAYDAQMTG TERMVILCSP HNPGGRVWTQ
     AELQGVADFC KRHDLLLISD EIHHDLVFGD AKHLPMPVAV PEVSERLIML TAPSKTFNFA
     GLHTGQVTIP DAALREQFRR RMQAIYLQGN TAGEVATIAA YSPDGAAYVD ALVPYIDGNR
     QIFDAAVNAI PGLRSMGLQA TYLAWVDFSG TGMDRAEFTR RVEQGARIAA NHGTTFGTGG
     ESFLRFNLGT QRSRVEEACA RLTEAFGDLQ
//
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