ID A0A348AET2_9FIRM Unreviewed; 388 AA.
AC A0A348AET2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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_2 {ECO:0000313|EMBL:BBB89580.1};
GN ORFNames=MAMMFC1_00213 {ECO:0000313|EMBL:BBB89580.1};
OS Methylomusa anaerophila.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Methylomusa.
OX NCBI_TaxID=1930071 {ECO:0000313|EMBL:BBB89580.1, ECO:0000313|Proteomes:UP000276437};
RN [1] {ECO:0000313|EMBL:BBB89580.1, ECO:0000313|Proteomes:UP000276437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMFC1 {ECO:0000313|EMBL:BBB89580.1,
RC ECO:0000313|Proteomes:UP000276437};
RX PubMed=29458677; DOI=10.1099/ijsem.0.002635;
RA Amano N., Yamamuro A., Miyahara M., Kouzuma A., Abe T., Watanabe K.;
RT "Methylomusa anaerophila gen. nov., sp. nov., an anaerobic methanol-
RT utilizing bacterium isolated from a microbial fuel cell.";
RL Int. J. Syst. Evol. Microbiol. 68:1118-1122(2018).
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; AP018449; BBB89580.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A348AET2; -.
DR KEGG; mana:MAMMFC1_00213; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000276437; 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:BBB89580.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000276437}.
FT DOMAIN 28..379
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 388 AA; 44502 MW; EF191030F0E4800B CRC64;
MSRNFDEIIN RKNTWSLKWD FNFQQHDILP MSIADMDFYS PKAVENAIIE RAKHGLYGYV
GVPDTFKKII KSWINRRHEW DIDEEWLLYS YTVTASIRNI IPAFTDPGDK ILILTPCYGS
FSYSITLNNR ELVTSPLILQ ENYAIDFDDF EKKLSEGVKL FILCSPHNPI GKVWTKDELL
KLGELCMLYN VLIISDEIHS DIVFKGYKHI PIASLSFELA QNSITFMSAG KTFNLSGLGA
SYIIAPNSAL REKFKKQLKL TGVHEPNIFG IVAAEVAYSY GQQWLEAVLD YLQNNYDFMS
KFFSEKIPEI RAVNQEGTYL GWLDCRKINI DCNELNDFFT NKARVKLNDG KAFGENGTGF
QRINFACSRV ILIEALNRIQ LAVNKISI
//
