ID A0A1I4XPB1_9ACTN Unreviewed; 393 AA.
AC A0A1I4XPB1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Threonine dehydrogenase {ECO:0000313|EMBL:SFN27681.1};
GN ORFNames=SAMN04489713_101957 {ECO:0000313|EMBL:SFN27681.1};
OS Actinomadura madurae.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=1993 {ECO:0000313|EMBL:SFN27681.1, ECO:0000313|Proteomes:UP000183413};
RN [1] {ECO:0000313|EMBL:SFN27681.1, ECO:0000313|Proteomes:UP000183413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43067 {ECO:0000313|EMBL:SFN27681.1,
RC ECO:0000313|Proteomes:UP000183413};
RA de Groot N.N.;
RL Submitted (OCT-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; FOVH01000001; SFN27681.1; -; Genomic_DNA.
DR RefSeq; WP_075019984.1; NZ_UAPP01000012.1.
DR AlphaFoldDB; A0A1I4XPB1; -.
DR STRING; 1993.SAMN04489713_101957; -.
DR GeneID; 73575110; -.
DR eggNOG; COG1063; Bacteria.
DR InParanoid; A0A1I4XPB1; -.
DR OrthoDB; 241504at2; -.
DR Proteomes; UP000183413; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000183413};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..391
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 393 AA; 42446 MW; E6D2643C00663EC9 CRC64;
MKAVTWHGKR DVRVDTVPDP EIKEPDDAII RVTSSGICGS DLHLYEVLGP FLTEGDVLGH
EPMGIVEETG SEVTHVKPGD RVVIPFNISC GRCHMCEMEL FAQCETTQVR EHGMGAALFG
YTRLYGQVPG AQAEYLRVPQ AHFGPIKVPE GPPDERFVYL SDVLPTAWQA VDWADIPAGG
SVTVLGLGPI GQMAARIARH LGHRVIAVDL VPERLEMARR HGVEVIDSDE ADDVPDAVRQ
LTGGRGTDSV IEAVGMEAHG SRGAKLAQTL TGLMPGTAAA PLMQRVGVDR LAALGTAIEI
VRRGGTISVI GVYGGMTDPL PMLRMFDKGI GLRMGQAHVK KWIGDLMPLV TDDADPLGVM
DLATHRRPLD EAPRAYEMFQ KKQDGAIKVL LQP
//