ID F3AJV1_9FIRM Unreviewed; 358 AA.
AC F3AJV1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=L-threonine 3-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00627};
DE Short=TDH {ECO:0000256|HAMAP-Rule:MF_00627};
DE EC=1.1.1.103 {ECO:0000256|HAMAP-Rule:MF_00627};
GN Name=tdh {ECO:0000256|HAMAP-Rule:MF_00627};
GN ORFNames=HMPREF0987_00725 {ECO:0000313|EMBL:EGG87609.1};
OS Lachnospiraceae bacterium 9_1_43BFAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=658088 {ECO:0000313|EMBL:EGG87609.1, ECO:0000313|Proteomes:UP000003620};
RN [1] {ECO:0000313|EMBL:EGG87609.1, ECO:0000313|Proteomes:UP000003620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9_1_43BFAA {ECO:0000313|EMBL:EGG87609.1,
RC ECO:0000313|Proteomes:UP000003620};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Ambrose C., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J.,
RA Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 9_1_43BFAA.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-
CC amino-3-ketobutyrate. {ECO:0000256|HAMAP-Rule:MF_00627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) +
CC NADH; Xref=Rhea:RHEA:13161, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57926, ChEBI:CHEBI:57945, ChEBI:CHEBI:78948;
CC EC=1.1.1.103; Evidence={ECO:0000256|HAMAP-Rule:MF_00627};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00627};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00627};
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo-
CC reductase pathway; glycine from L-threonine: step 1/2.
CC {ECO:0000256|HAMAP-Rule:MF_00627}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00627}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|HAMAP-Rule:MF_00627}.
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:EGG87609.1}.
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DR EMBL; ACTX01000003; EGG87609.1; -; Genomic_DNA.
DR AlphaFoldDB; F3AJV1; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_9; -.
DR UniPathway; UPA00046; UER00505.
DR Proteomes; UP000003620; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniPathway.
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 HAMAP; MF_00627; Thr_dehydrog; 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; IPR004627; L-Threonine_3-DHase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00692; tdh; 1.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00627};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00627};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00627};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00627}; Reference proteome {ECO:0000313|Proteomes:UP000003620};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00627}.
FT DOMAIN 31..139
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 179..307
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
FT ACT_SITE 45
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT ACT_SITE 48
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT BINDING 180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT BINDING 200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT BINDING 267..269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT BINDING 291..292
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT SITE 153
FT /note="Important for catalytic activity for the proton
FT relay mechanism but does not participate directly in the
FT coordination of zinc atom"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
SQ SEQUENCE 358 AA; 39237 MW; 37134CFC37B04FC8 CRC64;
MNDNKMWALV KETAAPGLAL KRVPIPEVGT NDVKIKIHKT AICGTDVHIY QWNEWAQHTI
AVGQTAGHEY VGEIVEMGSG VEGFNIGDIV SGEGHIVCGK CRNCLEGHKE NCKDAKGVGV
NRDGAFAEYL VIPAANVWPT NPAIPEEMYA IFDPFGNATH TALSYEVLGE DVLITGAGPI
GIMAAAIAKF AGARHVVITD FNQYRLDLAK KLGATRTVNL ANEKLEEVMK EIGMTEGFDV
GMEMSGAQAG FRDMIDNMKH GGKIAVLGLQ RPDAQINWET VIWNGLNIRG IYGRKVWDTW
YKMTTMLQAG LDISDIITHR LNIKDYKAGF DAMISGQSGK VILNWEDLDQ LEAQSQEF
//