B7LVH6 (TDH_ESCF3) 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:	EFER_3906

Organism

Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73) [Complete proteome] [HAMAP]

Taxonomic identifier

585054 [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_1000130552
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)
	B7LVH6 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: F2801DF8D422BA76	FASTA	341	37,288
	10 20 30 40 50 60 MKALSKLKAE EGIWMTDVPE PELGHNDLLI KIRKTAICGT DVHIYNWDEW SQKTIPVPMV 70 80 90 100 110 120 VGHEYVGEVV GIGQEVKGFK IGDRVSGEGH ITCGHCRNCR AGRTHLCRNT IGVGVNRPGC 130 140 150 160 170 180 FAEYLVIPAF NAFKIPDNIS DDLASIFDPF GNAVHTALSF DLVGEDVLVS GAGPIGIMAA 190 200 210 220 230 240 AVAKHVGARN VVITDVNEYR LELARKMGIT RAVNVAKENL EDVMAELGMT EGFDVGLEMS 250 260 270 280 290 300 GAPAAFRTML DTMNHGGRIA MLGIPPSDMS IDWTKVIFKG LFIKGIYGRE MFETWYKMAA 310 320 330 340 LIQSGLDLSP IITHRFSIDD FQKGFDAMRS GQSGKVILSW D

References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed: 19165319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35469 / DSM 13698 / CDC 0568-73.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928158 Genomic DNA. Translation: CAQ91340.1.
RefSeq	YP_002384936.1. NC_011740.1.
3D structure databases
ProteinModelPortal	B7LVH6.
ModBase	Search...
Protein-protein interaction databases
STRING	B7LVH6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000125473; EBESCP00000113706; EBESCG00000124221.
GeneID	7120197.
GenomeReviews	Gene locus EFER_3906 in contig CU928158_GR.
KEGG	efe:EFER_3906.
PATRIC	32132128. VBIEscFer122920_3754.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000008795.
HOGENOM	HBG753318.
ProtClustDB	PRK05396.
Enzyme and pathway databases
BioCyc	EFER585054:EFER_3906-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_ESCF3

Accession

Primary (citable) accession number: B7LVH6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program