ID C4FF97_9BIFI Unreviewed; 403 AA.
AC C4FF97;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN ORFNames=BIFANG_02997 {ECO:0000313|EMBL:EEP21628.1};
OS Bifidobacterium angulatum DSM 20098 = JCM 7096.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=518635 {ECO:0000313|EMBL:EEP21628.1, ECO:0000313|Proteomes:UP000006408};
RN [1] {ECO:0000313|EMBL:EEP21628.1, ECO:0000313|Proteomes:UP000006408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20098 {ECO:0000313|EMBL:EEP21628.1,
RC ECO:0000313|Proteomes:UP000006408};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-2009) 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:EEP21628.1}.
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DR EMBL; ABYS02000004; EEP21628.1; -; Genomic_DNA.
DR AlphaFoldDB; C4FF97; -.
DR STRING; 1683.Bang102_006735; -.
DR PATRIC; fig|518635.7.peg.930; -.
DR eggNOG; COG1168; Bacteria.
DR HOGENOM; CLU_017584_15_0_11; -.
DR Proteomes; UP000006408; Unassembled WGS sequence.
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; 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 Aminotransferase {ECO:0000313|EMBL:EEP21628.1};
KW Transferase {ECO:0000313|EMBL:EEP21628.1}.
FT DOMAIN 41..390
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 403 AA; 45463 MW; 1351F4CA0305B390 CRC64;
MLRSSRITVM TYDFDTPIDR SGTYSLKWEE AGDALPMWVA DMDFQTAPEI RKALRRRVEH
GVFGYSIVPS EWNRAYVDWW GRRHGLAVDP QWLVFCTGVV PAISSMVRKL TTPNENVLIQ
TPVYNIFFNS ILNNGCRVLE SPLVYDGEGH YAIDWTDLEA KLADPQTTLM ILCNPHNPID
RIWDRETLER IGELCWEHHV TVISDEIHCD LTDPGFAYVP FASVSEHCAM NSVTCMAPTK
TFNIAGLNSA AVMIPDPVLR HKVWRALNTD EVAEPNAFAM SATLAAFTEG EPWLDELRAY
LAGNKTVARS MFDEYNASAP AGRRIIMVEG HATYLLWVDC SAITHDTDAL CDYLKHECKV
MFSQGSEYGG NGHDFVRINV ACPRARMVEG LTRFLEGLNT YHA
//
