ID E8N178_ANATU Unreviewed; 331 AA.
AC E8N178;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative L-threonine dehydrogenase {ECO:0000313|EMBL:BAJ64821.1};
DE EC=1.1.1.103 {ECO:0000313|EMBL:BAJ64821.1};
GN OrderedLocusNames=ANT_27950 {ECO:0000313|EMBL:BAJ64821.1};
OS Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 /
OS UNI-1).
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Anaerolinea.
OX NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ64821.1, ECO:0000313|Proteomes:UP000008922};
RN [1] {ECO:0000313|EMBL:BAJ64821.1, ECO:0000313|Proteomes:UP000008922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1
RC {ECO:0000313|Proteomes:UP000008922};
RA Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., Oguchi A.,
RA Fukui S., Takahashi M., Yashiro I., Hosoyama A., Sekiguchi Y., Hanada S.,
RA Fujita N.;
RT "Whole genome sequence of Anaerolinea thermophila UNI-1.";
RL Submitted (DEC-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|RuleBase:RU361277}.
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DR EMBL; AP012029; BAJ64821.1; -; Genomic_DNA.
DR RefSeq; WP_013561168.1; NC_014960.1.
DR AlphaFoldDB; E8N178; -.
DR STRING; 926569.ANT_27950; -.
DR GeneID; 78351062; -.
DR KEGG; atm:ANT_27950; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_0; -.
DR InParanoid; E8N178; -.
DR OrthoDB; 9766898at2; -.
DR Proteomes; UP000008922; Chromosome.
DR GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08234; threonine_DH_like; 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 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 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:BAJ64821.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008922};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 25..128
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 169..285
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 331 AA; 35690 MW; 82342C22E636231B CRC64;
MKAVRIVQPH QVEIVDLPIP TPGEKEILIR VEASGICGTD LHILRGEYMG NYPVIPGHEF
SGTVVETGAG VTRFRVGDRV AVEPNLSCDA CEECLNNRQN FCRNWQAVGV TLPGGMAEYV
VVPEKAAFAV GDLPAEQAAF MEPLSCVLHG MENLSPRMGD RLLIIGAGPI GIQLMRVARL
QGAAHITMVE RNPARLMFAA EAGADRALSS LDDLSPDSFD AVIDATGVPA VLARTLDYVR
SGGKVLWFGV PRSDATMALE PFKIFRKGLT VMGSFTSKRN SYQAVALLQS GALRVDDLIS
HRLPLADFLR GCELLEQGAE GVKKVMILPQ A
//
