ID A0A0G3IHZ7_9MYCO Unreviewed; 352 AA.
AC A0A0G3IHZ7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Theronine dehydrogenase {ECO:0000313|EMBL:AKK27135.1};
GN ORFNames=AB431_11095 {ECO:0000313|EMBL:AKK27135.1};
OS Mycobacterium sp. EPa45.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1545728 {ECO:0000313|EMBL:AKK27135.1, 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:AKK27135.1, ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|EMBL:AKK27135.1,
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP011773; AKK27135.1; -; Genomic_DNA.
DR RefSeq; WP_047329962.1; NZ_CP011773.1.
DR AlphaFoldDB; A0A0G3IHZ7; -.
DR STRING; 1545728.AB431_11095; -.
DR KEGG; mye:AB431_11095; -.
DR PATRIC; fig|1545728.4.peg.2262; -.
DR OrthoDB; 9797931at2; -.
DR Proteomes; UP000035237; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd08230; glucose_DH; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR031640; Glu_dehyd_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF16912; Glu_dehyd_C; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 27..139
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 144..348
FT /note="Glucose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16912"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 352 AA; 37272 MW; 935FB733D6793923 CRC64;
MQALTVQPGK ADSLAVEEMQ EPTAGPDELR VAGLAIGVCG TDREIAAGEY GWAPSGRDRL
VLGHESLGRV LSAPKGSHFA EGDLVVGVVR RPDPVPCGAC AHGEFDMCRN GRYTERGIKE
IDGYGSEFWC VEADYAVKLE DGLADVGMLM EPTTVVAKAW EQVYRIGQRA WFEPRTVLVT
GAGPIGLLAA MLGVQHGLEV HVLDRVTTGP KPGIVDALNA TYHHDGVQAA IGKIRPDIVI
EATGVGSLVF DAMTVTGSYG IVALTGVSPK GRTLTVDPGG LSRDIVLEND AVVGSVNANL
RHYQQAAEAL GKADPKWLAS LITRRIPLSA ATQAFTEADD DVKVVITLDD SR
//
