ID A0A1C4Z0M0_9ACTN Unreviewed; 390 AA.
AC A0A1C4Z0M0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Threonine dehydrogenase {ECO:0000313|EMBL:SCF26535.1};
GN ORFNames=GA0074696_3913 {ECO:0000313|EMBL:SCF26535.1};
OS Micromonospora purpureochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47872 {ECO:0000313|EMBL:SCF26535.1, ECO:0000313|Proteomes:UP000198228};
RN [1] {ECO:0000313|EMBL:SCF26535.1, ECO:0000313|Proteomes:UP000198228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43821 {ECO:0000313|EMBL:SCF26535.1,
RC ECO:0000313|Proteomes:UP000198228};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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|RuleBase:RU361277}.
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DR EMBL; LT607410; SCF26535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4Z0M0; -.
DR Proteomes; UP000198228; Chromosome i.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08283; FDH_like_1; 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:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..388
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 390 AA; 42098 MW; DBF0BD505148ACDB CRC64;
MRATTWTGKD SVKVVDVPDP RIMNARDAIV KISSTAICGS DLHLYHGYIP AMRKGDILGH
EFMGEVVEVG PEVDNLAVGD RVVVPFPIAC GNCASCQQGR YSVCENSNPN AGIAEKIMGH
SPAGIFGYSH LLGGYAGGQA EYARVPFADV GPIKIPDEVP DDQALMLADI FPTAYMGAEM
CDIAPGDVVA VWGAGPVGLL AAASARLLGA ERVIVIDRYP YRLRLAAERA GAETINYEQL
DVLDELNRLT AGRGPDACID AVGLEGHHGN AAMYAYDRVK QAGRLETERP FALREAILSC
RSGGVVSVIG AYGGFVDKFP MGAFMNRSLI MRTGQCHVQR YTRPLLERIV KGEIDPSFVI
SHRMPLKDAA KGYKIFQKKQ DDCTKVVLKV
//