ID F6ELP4_HOYSD Unreviewed; 405 AA.
AC F6ELP4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN OrderedLocusNames=AS9A_3045 {ECO:0000313|EMBL:AEF41492.1};
OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS (Amycolicicoccus subflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC Hoyosella.
OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF41492.1, ECO:0000313|Proteomes:UP000009235};
RN [1] {ECO:0000313|EMBL:AEF41492.1, ECO:0000313|Proteomes:UP000009235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
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; CP002786; AEF41492.1; -; Genomic_DNA.
DR RefSeq; WP_013807841.1; NC_015564.1.
DR AlphaFoldDB; F6ELP4; -.
DR STRING; 443218.AS9A_3045; -.
DR KEGG; asd:AS9A_3045; -.
DR eggNOG; COG1168; Bacteria.
DR HOGENOM; CLU_017584_15_2_11; -.
DR Proteomes; UP000009235; 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:AEF41492.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009235};
KW Transferase {ECO:0000313|EMBL:AEF41492.1}.
FT DOMAIN 98..391
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 405 AA; 43494 MW; 355495B5BE70B269 CRC64;
MPQRTPLTEL SLDELRARTS VKWRTHPSDV LPLWVAEMDT PLAPPVAQAI RDAVDIGDTG
YPAGNVYGEA LDGFARRRWQ WNGVAADRCA IVPDVMLGIV EVLRLVTEPG DSVVVNSPVY
APFYAFIEHS GRSVLEAPLG PDLRIDMTNL ESAFQSAAMH TRRSAFVLCN PHNPTGVVHT
RAELEQVAEL AHRYGVRVIA DEIHAPLILD GAQFVPYLSV PGSGDAFSLM SASKGWNLAG
LKAALAIAGE DAVPDLQRMP EEVSHGPSHV GIIAHAAAFN HGEVWLDDLL AGLNSNRMLL
GELLHEHLPT VRYRQPEGTY LAWLDCRPLG FTSERSSSGP RVFSEVGGPA AMFLDKGRVA
LSSGHVFGTG GAGHVRLNFA CSPETLRQAL SQMGGAVGQA DAEGS
//
