ID   H0UP79_9BACT            Unreviewed;       407 AA.
AC   H0UP79;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   ORFNames=TheveDRAFT_0322 {ECO:0000313|EMBL:EHM09492.1};
OS   Thermanaerovibrio velox DSM 12556.
OC   Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC   Thermanaerovibrio.
OX   NCBI_TaxID=926567 {ECO:0000313|EMBL:EHM09492.1};
RN   [1] {ECO:0000313|EMBL:EHM09492.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12556 {ECO:0000313|EMBL:EHM09492.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Spring S., Brambilla E.-M., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The Noncontiguous Finished genome of Thermanaerovibrio velox DSM 12556.";
RL   Submitted (OCT-2011) 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; CM001377; EHM09492.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0UP79; -.
DR   STRING; 926567.TheveDRAFT_0322; -.
DR   eggNOG; COG1168; Bacteria.
DR   HOGENOM; CLU_017584_15_0_0; -.
DR   OrthoDB; 9802872at2; -.
DR   Proteomes; UP000005730; Chromosome.
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;
FT   DOMAIN          70..397
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   407 AA;  46043 MW;  AF8F5DE366E2307D CRC64;
     MVVRDIHKFD DPYFEEFQRL VDRRGTGCKK WDLLDKIFGE HPKGMLPFWI ADTEFRSPDP
     VIGALRDRVE HGVFGYPVRD GQVSQAVAEW WGRRHRFDVD PRWVCHSHGV MGGIAVSLRV
     FTSPGDPVVV QTPIYPPFRW VVENNQRRLV ENPLVERDGV YRMDLAGLER AFRGGARAML
     LCSPHNPTGR VWTREELREV AGLAERYRVL VISDEIHGDL VYPGDHAHIP FPSVSPWALD
     NSLLFASPSK SFNLAGFYTA YAIIPDGAKR KAYEAEMNRL FMDQGNELGQ VAMKAAYLEG
     EAWLNGLVRY LEGNRGRAVE FLRGMRGVRV TIPEGTFLMW IDFGGMLRGR GLTAGEFLKG
     AGVALNKGES FGEGFELYGR LNFGCPRQML DEGLQRIRSR AEELGLL
//