TDH_RUEPO
ID TDH_RUEPO Reviewed; 342 AA.
AC Q5LN53;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=L-threonine 3-dehydrogenase {ECO:0000250|UniProtKB:P07913};
DE Short=TDH {ECO:0000250|UniProtKB:P07913};
DE EC=1.1.1.103 {ECO:0000250|UniProtKB:P07913};
GN Name=tdh {ECO:0000250|UniProtKB:P07913}; OrderedLocusNames=SPO3359;
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-
CC amino-3-ketobutyrate. {ECO:0000250|UniProtKB:P07913}.
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:0000250|UniProtKB:P07913};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P07913};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000305};
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo-
CC reductase pathway; glycine from L-threonine: step 1/2.
CC {ECO:0000250|UniProtKB:P07913}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P07913}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07913}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV96586.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000031; AAV96586.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_044029362.1; NC_003911.12.
DR AlphaFoldDB; Q5LN53; -.
DR SMR; Q5LN53; -.
DR STRING; 246200.SPO3359; -.
DR EnsemblBacteria; AAV96586; AAV96586; SPO3359.
DR KEGG; sil:SPO3359; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_5; -.
DR OrthoDB; 972769at2; -.
DR UniPathway; UPA00046; UER00505.
DR Proteomes; UP000001023; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniPathway.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..342
FT /note="L-threonine 3-dehydrogenase"
FT /id="PRO_0000160858"
FT ACT_SITE 40
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT ACT_SITE 43
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 263..265
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 287..288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT SITE 148
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:0000250|UniProtKB:O58389"
SQ SEQUENCE 342 AA; 36895 MW; 9A78823B35A05305 CRC64;
MKALEKSKPE EGLWMVQAPV PEIGPDDVLI KIKKTGICGT DIHIWNWDEW AAHTVPVPMI
TGHEFAGEIV ELGRDVTGLS IGQRVSGEGH LIGTESRQSR AGKFHLDPGT RGIGVNVQGA
FAQYLRLPAF NVVPLPEDIP DEIGAILDPL GNAVHTALSF DLLGEDVLIT GAGPIGIMAA
AVAKHAGARH VVITDINADR LKLAQHVVPR ARTVDVTRED LGDVVHELGL KQGFDVGLEM
SGSQAALDQM VEALVMGGKI ALLGIPPGKS PVDWSRIVFK AITIKGVYGR EMFETWYKMI
AMLQNGLDVS RVITHRFGVD EFREGFAAMK SGLSGKVVLD WT
