ID D4M011_9FIRM Unreviewed; 342 AA.
AC D4M011;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=Threonine dehydrogenase and related Zn-dependent dehydrogenases {ECO:0000313|EMBL:CBL27371.1};
DE EC=1.1.1.103 {ECO:0000313|EMBL:CBL27371.1};
DE EC=1.1.1.14 {ECO:0000313|EMBL:CBL27371.1};
GN ORFNames=RTO_29560 {ECO:0000313|EMBL:CBL27371.1};
OS [Ruminococcus] torques L2-14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL27371.1, ECO:0000313|Proteomes:UP000008956};
RN [1] {ECO:0000313|EMBL:CBL27371.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL27371.1,
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:CBL27371.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL27371.1,
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|ARBA:ARBA00001947,
CC 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; CBL27371.1; -; Genomic_DNA.
DR RefSeq; WP_015529930.1; NC_021015.1.
DR AlphaFoldDB; D4M011; -.
DR STRING; 33039.ERS852502_02446; -.
DR KEGG; rto:RTO_29560; -.
DR PATRIC; fig|657313.3.peg.2843; -.
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 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; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43161:SF9; SORBITOL 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:CBL27371.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 7..337
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 342 AA; 37474 MW; E35DE35FDC54DE90 CRC64;
MLQQVMTNPG EIIFREVPVP EVKDDQVLVK IMNIGICGSD IHVYHGKHPF TKYPVTQGHE
VSGEIAKVGK DVTEFHEGQK VTIEPQVYCG QCYPCRHGKY NLCEELKVMG FQTTGTASEY
FAVDASKVTP IPEDMSYEEG AMIEPLAVAV HGVKQVGDVK GLNIAVLGAG PIGNLVAQAA
KGMGAAKVMI TDVSDLRLDK AKECGIDVCV NTMEKDFGEA MVEAFGPDKA DVIYDCAGNN
ITMGQAIKYA RKGSIIVLVA VFAGMATVDL AVANDHELDI KSTMMYRHDD YVDGIELVNE
GKVHLRPLIS KTFAFKDYLK AYQYIDDNRE TTMKVIINVQ EK
//