ID F4LWV7_TEPAE Unreviewed; 390 AA.
AC F4LWV7; L0S2G2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN OrderedLocusNames=TEPIRE1_1825 {ECO:0000313|EMBL:CCP26624.1};
OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Tepidanaerobacteraceae; Tepidanaerobacter.
OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CCP26624.1, ECO:0000313|Proteomes:UP000010802};
RN [1] {ECO:0000313|Proteomes:UP000010802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT Tepidanaerobacter acetatoxydans strain Re1.";
RL Genome Announc. 1:E00213-E00213(2013).
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; HF563609; CCP26624.1; -; Genomic_DNA.
DR RefSeq; WP_013778751.1; NC_019954.2.
DR AlphaFoldDB; F4LWV7; -.
DR STRING; 1209989.TepRe1_1693; -.
DR KEGG; tae:TepiRe1_1825; -.
DR KEGG; tep:TepRe1_1693; -.
DR PATRIC; fig|1209989.3.peg.2104; -.
DR eggNOG; COG1168; Bacteria.
DR HOGENOM; CLU_017584_15_0_9; -.
DR OrthoDB; 9802872at2; -.
DR Proteomes; UP000010802; Chromosome.
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:CCP26624.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010802}.
FT DOMAIN 54..383
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 390 AA; 45348 MW; 548A4D534065C22F CRC64;
MYEFDYVDNA KQYSSEKWYG LKEKFGSEDL IPLWVADMDF KAPQPVIDRL MEVVEFGVYG
NIRRPETYYN AIINWMRKRY NWEIKREWIG IASRIIPSIG FAIRALTQPG DNIIIQPPVY
DNFSNIIKKS ERKVVTNPLI FKEQKYHMDF LDLEKKAQDP KTKMLIISNP HNPVGRVWTR
SELTELGRIC LKHNVIVICD QAYADLTYPN IEYTPYASIC EDFAQNCITC TSLSKPFNLA
GIHTAYMIIP NKNLFDAYDS FIESLHLKRG TIFSVIATEA AYEESEEWLN NVTKYINENL
QYMKCFIKDR IPNINVIEPE FAYLVWLDLR NIKVDSSQLN NFLVQKAKIA VNDGRMYGEN
GAGFVRMNIA CPRNILKSAL ERIEFAVNIC
//
