ID A0A0E9MKF7_9SPHN Unreviewed; 355 AA.
AC A0A0E9MKF7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=L-threonine dehydrogenase {ECO:0000313|EMBL:GAO37988.1};
GN Name=tdh {ECO:0000313|EMBL:GAO37988.1};
GN ORFNames=SCH01S_01_01510 {ECO:0000313|EMBL:GAO37988.1};
OS Sphingomonas changbaiensis NBRC 104936.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219043 {ECO:0000313|EMBL:GAO37988.1, ECO:0000313|Proteomes:UP000033202};
RN [1] {ECO:0000313|EMBL:GAO37988.1, ECO:0000313|Proteomes:UP000033202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 104936 {ECO:0000313|EMBL:GAO37988.1,
RC ECO:0000313|Proteomes:UP000033202};
RA Katano-Makiyama Y., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K.,
RA Ohji S., Yamazoe A., Ichikawa N., Kimura A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas changbaiensis NBRC 104936.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAO37988.1}.
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DR EMBL; BBWU01000001; GAO37988.1; -; Genomic_DNA.
DR RefSeq; WP_046346824.1; NZ_BBWU01000001.1.
DR AlphaFoldDB; A0A0E9MKF7; -.
DR STRING; 1219043.SCH01S_01_01510; -.
DR Proteomes; UP000033202; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 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:UP000033202};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..353
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 355 AA; 37932 MW; 953CFD0B5E7E0AB1 CRC64;
MSTSPRLIDD TAHTMKGLAK LEAREGIWMT QAPVPEPGPN DVLIKVKRTA ICGTDIHIYN
WDAWASKTIP VPMIVGHEFS GEIVAIGSEV TRPLKIGERV SGEGHIIDMN SAAARAGRFH
LDPGTRGVGV NRQGAFAEYL CIPAFNVVPL PDEVSDDVGA ILDPFGNAVH TAQQFDLLGE
DVLVTGAGPI GIMAAAVARH AGARSVVLTD VNPTRLDLAT KLADVRPVNV ANEDLRDVMA
AEKIPDGFGV ALEMSGAQPA IRQAIDALTM GGKLAMLGIP SGAMDVVWSD VIMKALTIKG
VYGREMFETW RKMFGLIKGG LNLEPLITHR LPVEQFQEGF DAMRSGASGK VVLSW
//
