ID A0A285KZK6_9NOCA Unreviewed; 350 AA.
AC A0A285KZK6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Threonine dehydrogenase {ECO:0000313|EMBL:SNY78100.1};
GN ORFNames=SAMN04244553_1184 {ECO:0000313|EMBL:SNY78100.1};
OS Nocardia amikacinitolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=756689 {ECO:0000313|EMBL:SNY78100.1, ECO:0000313|Proteomes:UP000219565};
RN [1] {ECO:0000313|EMBL:SNY78100.1, ECO:0000313|Proteomes:UP000219565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45537 {ECO:0000313|EMBL:SNY78100.1,
RC ECO:0000313|Proteomes:UP000219565};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; OBEG01000001; SNY78100.1; -; Genomic_DNA.
DR RefSeq; WP_067783631.1; NZ_JAMTCX010000006.1.
DR AlphaFoldDB; A0A285KZK6; -.
DR STRING; 1379680.GCA_001612615_02374; -.
DR OrthoDB; 9797931at2; -.
DR Proteomes; UP000219565; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08285; NADP_ADH; 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; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42813:SF4; DEHYDROGENASE 1, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000219565};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 7..347
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 350 AA; 36817 MW; CE7D57A25A75CDDB CRC64;
MKAFVMKEIG SVGFTEKPVP EPGPFDAVVR TTTALICTSD SHTVQGGIGP RENLTLGHEA
VGVVHAVGSE VRHIRPNDRV LAGAITPDWG DAAAQNGFPS QSGGPLGGFK FANSKDGVFA
EYFHVNDADA NLAVIPDGIP DEWAVYCSDM LSTGFMGAEK GNIPIGGTVA VLAQGPVGLM
STAGAKLRGA GLIIGVESVP ARQALARRYG AGEIIDFTSE DVVERVLELT GGEGVDTAIE
ALGADVTFQT AVKITKPGGT ISNVGYFGDG EFVRIPRVEW GVGMADKTIA TGLCPGGRLR
MERLLRILES GQVDPTPMTT HEFAFDDMEQ AFEVSDKKLD DVVKVLIRFG
//