ID C7QKB2_CATAD Unreviewed; 394 AA.
AC C7QKB2;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN OrderedLocusNames=Caci_6332 {ECO:0000313|EMBL:ACU75186.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU75186.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU75186.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
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; CP001700; ACU75186.1; -; Genomic_DNA.
DR RefSeq; WP_015794915.1; NC_013131.1.
DR AlphaFoldDB; C7QKB2; -.
DR STRING; 479433.Caci_6332; -.
DR KEGG; cai:Caci_6332; -.
DR eggNOG; COG1168; Bacteria.
DR HOGENOM; CLU_017584_15_2_11; -.
DR InParanoid; C7QKB2; -.
DR OrthoDB; 3224382at2; -.
DR Proteomes; UP000000851; Chromosome.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43525:SF2; CYSTATHIONINE BETA-LYASE-RELATED; 1.
DR PANTHER; PTHR43525; 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:ACU75186.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW Transferase {ECO:0000313|EMBL:ACU75186.1}.
FT DOMAIN 98..379
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 394 AA; 41928 MW; B70EB3A44A8A0706 CRC64;
MSDASAVSAD PDWLRSKPGL KWATAAPDVL PAWVAEMDFA VPPPVRQVLT DFAAIGDLGY
PAWMEGSGTP LREAFRDRMT ARYDWSPDPA HVREFTDLNQ ALQAVLHVAT EPGDAVAMHV
PGYPTFLRAV PKMGRRLIPV PLHRDEDGWS SDADCLDAAV TASGARTLIL VNPNNPVGRV
LTRSELSAIA TVAEARDLLV ISDEIHADLT YAPAVHIPFA SLSADAQART VTMTSASKAF
NIAGACCAVA YVGSERVRDG LDRLPPDLLG RLGAVGVAAT LAAWREGDPW LAAVLETLSA
NRDVLGAALP KDIGYVPPEA TCLAWLDCRS LGLSDPADFF LRKAGVDLIS GSSFGTFGEG
FVRLNFGTTP AILTEICARM TEAVTSLGQR PCEP
//
