Q0BKV5 (TDH_FRATO) 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:	FTH_1473

Organism

Francisella tularensis subsp. holarctica (strain OSU18) [Complete proteome] [HAMAP]

Taxonomic identifier

393011 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Francisellaceae › Francisella › Francisella tularensis › Francisella tularensis subsp. holarctica

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH. HAMAP-Rule MF_00627
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2. HAMAP-Rule MF_00627
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
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	L-threonine catabolic process to glycine Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	L-threonine 3-dehydrogenase activity Inferred from electronic annotation. Source: HAMAP nucleotide binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 351	351	L-threonine 3-dehydrogenase HAMAP-Rule MF_00627		PRO_1000051640
Sites
	Metal binding	39	1	Zinc 1; catalytic By similarity
	Metal binding	64	1	Zinc 1; catalytic By similarity
	Metal binding	94	1	Zinc 2 By similarity
	Metal binding	97	1	Zinc 2 By similarity
	Metal binding	100	1	Zinc 2 By similarity
	Metal binding	108	1	Zinc 2 By similarity
	Metal binding	149	1	Zinc 1; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0BKV5 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 1E07E9CCC5A58A79	FASTA	351	38,400
	10 20 30 40 50 60 MKALAKLKKQ PGIWMINDAP IPEYGYNDVL IKIKKTAICG TDLHIYNWDK WSQNTIPVPM 70 80 90 100 110 120 ITGHEFAGEV VAKGDGVTSV DIGDRVSGEG HLVCGQCRNC RAGKRHLCRK TIGIGVNVQG 130 140 150 160 170 180 AFAEYLVMPA VNVFKIPDSI SDDIASTFDP MGNAIHTALS FNLTGEDVLI TGAGPIGLMA 190 200 210 220 230 240 VKIARFCGAR RIVITDINEY RLQMARDFGA TVALNVAPFK NQDELVKQMR KVMSDIGMTE 250 260 270 280 290 300 GFDVGLEMSG INSAISMMLD VMNHGGKLSL LGISAGDISV DWGAILFKGL TLKGIYGREM 310 320 330 340 350 FETWYLMTSM LQAGMDMNPI ITHRLHIDEF QKGFEIMKSG QCGKVILDWS S

References

[1]

"Chromosome rearrangement and diversification of Francisella tularensis revealed by the type B (OSU18) genome sequence." Petrosino J.F., Xiang Q., Karpathy S.E., Jiang H., Yerrapragada S., Liu Y., Gioia J., Hemphill L., Gonzalez A., Raghavan T.M., Uzman A., Fox G.E., Highlander S., Reichard M., Morton R.J., Clinkenbeard K.D., Weinstock G.M. J. Bacteriol. 188:6977-6985(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: OSU18.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000437 Genomic DNA. Translation: ABI83279.1.
RefSeq	YP_763916.1. NC_008369.1.
3D structure databases
ProteinModelPortal	Q0BKV5.
ModBase	Search...
Protein-protein interaction databases
STRING	393011.FTH_1473.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABI83279; ABI83279; FTH_1473.
GeneID	4307881.
KEGG	fth:FTH_1473.
PATRIC	17953132. VBIFraTul3936_1691.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1063.
HOGENOM	HOG000294686.
KO	K00060.
OMA	MSIDWNK.
ProtClustDB	PRK05396.
Enzyme and pathway databases
BioCyc	FTUL393011:GHFN-1589-MONOMER.
UniPathway	UPA00046; UER00505.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_00627. Thr_dehydrog.
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]
PANTHER	PTHR11695. PTHR11695. 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_FRATO

Accession

Primary (citable) accession number: Q0BKV5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program