ID D4M311_9FIRM Unreviewed; 368 AA.
AC D4M311;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=L-threonine 3-dehydrogenase {ECO:0000313|EMBL:CBL25623.1};
DE EC=1.1.1.103 {ECO:0000313|EMBL:CBL25623.1};
DE EC=1.1.1.14 {ECO:0000313|EMBL:CBL25623.1};
GN ORFNames=RTO_09250 {ECO:0000313|EMBL:CBL25623.1};
OS [Ruminococcus] torques L2-14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL25623.1, ECO:0000313|Proteomes:UP000008956};
RN [1] {ECO:0000313|EMBL:CBL25623.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL25623.1,
RC ECO:0000313|Proteomes:UP000008956};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Ruminococcus torques L2-14.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL25623.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL25623.1,
RC ECO:0000313|Proteomes:UP000008956};
RA Pajon A.;
RL Submitted (MAR-2010) 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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; FP929055; CBL25623.1; -; Genomic_DNA.
DR RefSeq; WP_015528250.1; NC_021015.1.
DR AlphaFoldDB; D4M311; -.
DR KEGG; rto:RTO_09250; -.
DR PATRIC; fig|657313.3.peg.598; -.
DR HOGENOM; CLU_026673_11_0_9; -.
DR Proteomes; UP000008956; Chromosome.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IEA:UniProtKB-EC.
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:CBL25623.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 15..364
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 368 AA; 39419 MW; B0A827C1DDE099C5 CRC64;
MNYEIPEKMK AWVLGNPGEL TLEEKPVPEP KRAEVLIHVD AVAICATDLE IIKNGPPALI
QGGLPFNKGF TPGHEYMGTI VKLGPGVDEY KVGDRVAVEI HAGCDSCERC REGMYTSCLN
YGQNYEGHDK GHRANGFTTD GGFAEYVINS VKTLCHVGDN VTDEEATLIV TAGTAMYGLD
TLGGLFAGQS LVVTGPGPIG LMAVAVAKTL GANPVILTGT RDNRLELGKK LGADYTINVR
NENVVEKVKE LTNGEGVHYV MECSGAPNAV NEAAAMVKRG GKVCLAAFPS KPVEVDVAAL
VRNNISLFGI RGEGRSAVHR AASLISEKRF DASLIHTHTF KFDELLTALK YSRERIDDAI
KVVVKIPG
//
