B1X950 (TDH_ECODH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-threonine 3-dehydrogenase
EC=1.1.1.103

Gene names

Name:	tdh
Ordered Locus Names:	ECDH10B_3798

Organism

Escherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP]

Taxonomic identifier

316385 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH. HAMAP MF_00627
Cofactor	Binds 2 zinc ions per subunit By similarity. HAMAP MF_00627
Pathway	Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2. HAMAP MF_00627
Subunit structure	Homotetramer By similarity. HAMAP MF_00627
Subcellular location	Cytoplasm By similarity HAMAP MF_00627.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	threonine catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-threonine 3-dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 341	341	L-threonine 3-dehydrogenase HAMAP MF_00627		PRO_1000130548
Sites
	Metal binding	38	1	Zinc 1; catalytic By similarity
	Metal binding	63	1	Zinc 1; catalytic By similarity
	Metal binding	93	1	Zinc 2 By similarity
	Metal binding	96	1	Zinc 2 By similarity
	Metal binding	99	1	Zinc 2 By similarity
	Metal binding	107	1	Zinc 2 By similarity
	Metal binding	148	1	Zinc 1; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	B1X950 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: 039FBD6B1CE8C2B2	FASTA	341	37,239
	10 20 30 40 50 60 MKALSKLKAE EGIWMTDVPV PELGHNDLLI KIRKTAICGT DVHIYNWDEW SQKTIPVPMV 70 80 90 100 110 120 VGHEYVGEVV GIGQEVKGFK IGDRVSGEGH ITCGHCRNCR GGRTHLCRNT IGVGVNRPGC 130 140 150 160 170 180 FAEYLVIPAF NAFKIPDNIS DDLAAIFDPF GNAVHTALSF DLVGEDVLVS GAGPIGIMAA 190 200 210 220 230 240 AVAKHVGARN VVITDVNEYR LELARKMGIT RAVNVAKENL NDVMAELGMT EGFDVGLEMS 250 260 270 280 290 300 GAPPAFRTML DTMNHGGRIA MLGIPPSDMS IDWTKVIFKG LFIKGIYGRE MFETWYKMAA 310 320 330 340 LIQSGLDLSP IITHRFSIDD FQKGFDAMRS GQSGKVILSW D

References

[1]

"The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse." Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R. J. Bacteriol. 190:2597-2606(2008) [PubMed: 18245285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / DH10B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000948 Genomic DNA. Translation: ACB04666.1.
RefSeq	YP_001732444.1. NC_010473.1.
3D structure databases
ProteinModelPortal	B1X950.
SMR	B1X950. Positions 1-341.
ModBase	Search...
Protein-protein interaction databases
STRING	B1X950.
Proteomic databases
PRIDE	B1X950.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000013771; EBESCP00000013299; EBESCG00000012833.
GeneID	6059902.
GenomeReviews	Gene locus ECDH10B_3798 in contig CP000948_GR.
KEGG	ecd:ECDH10B_3798.
PATRIC	18467566. VBIEscCol59506_3836.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000008795.
HOGENOM	HBG753318.
OMA	MMRSGMS.
ProtClustDB	PRK05396.
Enzyme and pathway databases
BioCyc	ECOL316385:ECDH10B_3798-MONOMER.
Family and domain databases
HAMAP	MF_00627. Thr_dehydrog. [Tree]
InterPro	IPR013149. ADH_C. IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn-type. IPR002328. ADH_Zn_CS. IPR011032. GroES-like. IPR004627. L-Threonine_3-DHase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00060.
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
SUPFAM	SSF50129. GroES_like. 1 hit.
TIGRFAMs	TIGR00692. Tdh. 1 hit.
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TDH_ECODH

Accession

Primary (citable) accession number: B1X950

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	May 20, 2008
Last modified:	January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program