ID A0A087EAW3_9BIFI Unreviewed; 442 AA.
AC A0A087EAW3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN ORFNames=BITS_1434 {ECO:0000313|EMBL:KFJ04914.1};
OS Bifidobacterium tsurumiense.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=356829 {ECO:0000313|EMBL:KFJ04914.1, ECO:0000313|Proteomes:UP000029080};
RN [1] {ECO:0000313|EMBL:KFJ04914.1, ECO:0000313|Proteomes:UP000029080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13495 {ECO:0000313|EMBL:KFJ04914.1,
RC ECO:0000313|Proteomes:UP000029080};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFJ04914.1}.
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DR EMBL; JGZU01000017; KFJ04914.1; -; Genomic_DNA.
DR RefSeq; WP_026642444.1; NZ_JGZU01000017.1.
DR AlphaFoldDB; A0A087EAW3; -.
DR STRING; 356829.BITS_1434; -.
DR eggNOG; COG1168; Bacteria.
DR OrthoDB; 3224382at2; -.
DR Proteomes; UP000029080; 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:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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 Aminotransferase {ECO:0000313|EMBL:KFJ04914.1};
KW Lyase {ECO:0000313|EMBL:KFJ04914.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029080};
KW Transferase {ECO:0000313|EMBL:KFJ04914.1}.
FT DOMAIN 49..437
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 442 AA; 47894 MW; 46BB1A2354C1F960 CRC64;
MTGDQFDFDA IHSRMGTGSA KWDHALQQIP VQIAKQYAPI AADIADMEFQ CAPAIREAVM
KVAQHGIFGY ASLPETFQEA VSCWFARRYD CKLDIHEIGL SAGTIPAFSS IIRSLSSPGD
GVMLCTPVYG IFFNCIRNSG RRCVEVPLHW SAATDGCSES ESAGRWIMDF AAMEDILQCD
RISVFVLCSP HNPTGTIWDA QELRQLLELM GKYNVAVLSD EAHADISAPG KRYTPLAAVA
GPHDWAVSIN SPSKPFNMAG LQISAVVSRN RSLLERVLVG INRDEAGEQN IFALPALLAA
YSPEGERWLD VMRSYVWQNR QLVADHLRGS GAELLPADAT YLGWIDIRKV LEVRAGGISA
ADIDGDGGIE GVDASGSAFP EPQSSMVQLT DEFVAHVRDH YALTLSSGTS FGPAGAGFIR
MNLAMPASVV DEACRRLVAA LQ
//
