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Database: UniProt
Entry: A0A0H2KR45_9MICO
LinkDB: A0A0H2KR45_9MICO
Original site: A0A0H2KR45_9MICO 
ID   A0A0H2KR45_9MICO        Unreviewed;       415 AA.
AC   A0A0H2KR45;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   ORFNames=FB00_04965 {ECO:0000313|EMBL:KLN35638.1};
OS   Cellulosimicrobium funkei.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Cellulosimicrobium.
OX   NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN35638.1, ECO:0000313|Proteomes:UP000035265};
RN   [1] {ECO:0000313|EMBL:KLN35638.1, ECO:0000313|Proteomes:UP000035265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U11 {ECO:0000313|EMBL:KLN35638.1,
RC   ECO:0000313|Proteomes:UP000035265};
RA   Hu C., Gong Y., Wan W., Jiang M.;
RT   "Cellulosimicrobium funkei U11 genome.";
RL   Submitted (MAY-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:KLN35638.1}.
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DR   EMBL; JNBQ01000003; KLN35638.1; -; Genomic_DNA.
DR   RefSeq; WP_047231762.1; NZ_JNBQ01000003.1.
DR   AlphaFoldDB; A0A0H2KR45; -.
DR   STRING; 264251.FB00_04965; -.
DR   PATRIC; fig|264251.5.peg.1021; -.
DR   Proteomes; UP000035265; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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   Lyase {ECO:0000313|EMBL:KLN35638.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035265}.
FT   DOMAIN          36..406
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   415 AA;  43827 MW;  95428D4AF4149662 CRC64;
     MRTPLDVLTL DELRRRTSVK WRAFEPDVLP LFVAEMDVAP CEAVVDAVTA ALRAGDTGYD
     VGTTYGEAYA RFAARRWGWS FDASTSRTLP DVMLAIVEVL RVLTAPGDAV VVNPPVYPPF
     YGFTANEGRR VVDAPLGTDG RLDLDALERA FADATGVAAN GRGPGSGRRA VWLVCNPQNP
     TGTTHTPAEL EAGLALAARY GVRVVADEIH APLTRPGLDG RPATTHTPLL AVPGSEQAVA
     IVSASKAWNL PGLKAAAAVG GPAVADDLRR IPEEASHGVQ HVSVIAHVAA LDHGEAWLDA
     VLAGVERNAW LLADLLGEHL PEVGYRPGEA TYLAWLDCRR IDGAATGVDP VAGAADPAPA
     KDPRGWFLDR ARVALEDGRR FGPGGEGHVR LNLATGVDVL TEAVERMGES VRAAV
//
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