ID A0A1X6YK20_9RHOB Unreviewed; 397 AA.
AC A0A1X6YK20;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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:SLN22828.1};
GN ORFNames=CLV79_101421 {ECO:0000313|EMBL:PSK88581.1}, LOS8367_00666
GN {ECO:0000313|EMBL:SLN22828.1};
OS Limimaricola soesokkakensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Limimaricola.
OX NCBI_TaxID=1343159 {ECO:0000313|EMBL:SLN22828.1, ECO:0000313|Proteomes:UP000193495};
RN [1] {ECO:0000313|EMBL:SLN22828.1, ECO:0000313|Proteomes:UP000193495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8367 {ECO:0000313|EMBL:SLN22828.1,
RC ECO:0000313|Proteomes:UP000193495};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSK88581.1, ECO:0000313|Proteomes:UP000240624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29956 {ECO:0000313|EMBL:PSK88581.1,
RC ECO:0000313|Proteomes:UP000240624};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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}.
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DR EMBL; PYGB01000001; PSK88581.1; -; Genomic_DNA.
DR EMBL; FWFY01000002; SLN22828.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6YK20; -.
DR OrthoDB; 3224382at2; -.
DR Proteomes; UP000193495; Unassembled WGS sequence.
DR Proteomes; UP000240624; 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:SLN22828.1}.
FT DOMAIN 51..389
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 397 AA; 43697 MW; F01C795DB87DB9A7 CRC64;
MSPDRQTAPD FDEIIDRRGT NCSKWDMMEP VYGVSPDEGL AMWVADMDFR PPACVQRAVE
EMAAHGVYGY AASDAAQREA IGWWMDRRHG WRPDPGDIFT THGLVNATGL CVDAFTEPGE
GVVLFTPVYH AFARVIRAAG RQVIECPLAL DEGRYVPDFE AWDAMMTGRE RMMILCSPQN
PGGRVWSRAE LEGWAEFARR HDLILVSDEI HCDLTMPGVT HTAMTRIDGV ADRLLMLTAT
TKTFNIAGAH IGNVIVSDPK LKARFAARMG ALGLSPNSFG LAMATAAMSP DGVEWLEALR
RYLDGNRRLF EEGVAAIPGL KPMPLESTYL EWVDFSGTGM TREEVLARIE GEAKIAVNHG
TSFGLGGESF QRFNIATPRA RVAEAVARLK SAFADLQ
//
