ID A0A0S4LFT8_9BACT Unreviewed; 344 AA.
AC A0A0S4LFT8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Threonine 3-dehydrogenase, NAD(P)-binding {ECO:0000313|EMBL:CUS36435.1};
DE EC=1.1.1.103 {ECO:0000313|EMBL:CUS36435.1};
GN Name=tdh {ECO:0000313|EMBL:CUS36435.1};
GN ORFNames=COMA2_230032 {ECO:0000313|EMBL:CUS36435.1};
OS Candidatus Nitrospira nitrificans.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1742973 {ECO:0000313|EMBL:CUS36435.1, ECO:0000313|Proteomes:UP000198736};
RN [1] {ECO:0000313|Proteomes:UP000198736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Luecker S., Luecker S.;
RL Submitted (OCT-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}.
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DR EMBL; CZPZ01000016; CUS36435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4LFT8; -.
DR STRING; 1742973.COMA2_230032; -.
DR OrthoDB; 9769198at2; -.
DR Proteomes; UP000198736; Unassembled WGS sequence.
DR GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:CUS36435.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198736};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 10..342
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 344 AA; 36545 MW; 57D7253F86067A0E CRC64;
MYALVKATAG PGLTPTDWAD PTPGPHDAVV KVAATSLCGT DVHIYRWDEW AQRRIHPPRI
IGHELCGHVV EVGREVSLVK VGDYVAAESH LTCGACFQCR TGQAHVCKNY KILGIDRDGS
YAQCVSLPEG VLWHTAPDIP PELACVQEPL GNAVDAALAE DLTGQTVLIT GCGPTGLFAA
AIARTAGAAT IIATDVSDYR LGLAKKIGVD HVLNARTESV AQVAEAILEM TDGEGVDASL
EMSGDPTALH QAFRAVKNGG RVTLFGIPTG PVCFDLPNEM IFKGIRVYGI TGRRLFGTWY
RLAGLFKAGL DIRPVVTHSL PLKEFAAGFE LIQSGQCGKV VLIP
//
