ID A0A0G3IP69_9MYCO Unreviewed; 283 AA.
AC A0A0G3IP69;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase {ECO:0000313|EMBL:AKK27907.1};
GN ORFNames=AB431_15785 {ECO:0000313|EMBL:AKK27907.1};
OS Mycobacterium sp. EPa45.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1545728 {ECO:0000313|EMBL:AKK27907.1, ECO:0000313|Proteomes:UP000035237};
RN [1] {ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|Proteomes:UP000035237};
RA Kato H., Ogawa N., Ohtsubo Y., Ohshima K., Toyoda A., Yamazoe A., Mori H.,
RA Maruyama F., Nagata Y., Hattori M., Fujiyama A., Kurokawa K., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45, Isolated from a Phenanthrene-Degrading Consortium.";
RL Genome Announc.0:0-0(2015).
RN [2] {ECO:0000313|EMBL:AKK27907.1, ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|EMBL:AKK27907.1,
RC ECO:0000313|Proteomes:UP000035237};
RX PubMed=26184940;
RA Kato H., Ogawa N., Ohtsubo Y., Oshima K., Toyoda A., Mori H., Nagata Y.,
RA Kurokawa K., Hattori M., Fujiyama A., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45 (NBRC 110737), Isolated from a Phenanthrene-Degrading
RT Consortium.";
RL Genome Announc. 3:e00782-15(2015).
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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DR EMBL; CP011773; AKK27907.1; -; Genomic_DNA.
DR RefSeq; WP_047330730.1; NZ_CP011773.1.
DR AlphaFoldDB; A0A0G3IP69; -.
DR STRING; 1545728.AB431_15785; -.
DR KEGG; mye:AB431_15785; -.
DR PATRIC; fig|1545728.4.peg.3216; -.
DR OrthoDB; 9803333at2; -.
DR Proteomes; UP000035237; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43008; BENZIL REDUCTASE; 1.
DR PANTHER; PTHR43008:SF4; CHAIN DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G08710)-RELATED; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 283 AA; 28926 MW; 7A1A39C70DFBAFBA CRC64;
MSWLTGRVAL VTGGAAGIGL AVVERFLSEG AQVGVLDRSV GDLAGLGYAD RKLRAVTGDV
TSYADNVRAV HETVDAFGKL DVFVGNAGIF DYFASLMSFD GDDLGGAFDE IFSVNVKGYL
LGARAAVPEL LKSDAPSIIF TVSNSGFYTS GGGPLYTASK HAVVGVVREL AYELAPKIRV
NGVAPGGTIT GLRGIEDLGQ GETVLSSVPG IADMMSTTNP LQYAQQPADH AGLYVLLASA
DNSRAVTGVV INSDGGLGVR GMNQPAGGLG LAANVARTDL PTA
//