Q65JE7 (TDH_BACLD) 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:	BLi01923, BL03658

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	346 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 – 346	346	L-threonine 3-dehydrogenase HAMAP MF_00627		PRO_0000160830
Sites
	Metal binding	42	1	Zinc 1; catalytic By similarity
	Metal binding	67	1	Zinc 1; catalytic By similarity
	Metal binding	97	1	Zinc 2 By similarity
	Metal binding	100	1	Zinc 2 By similarity
	Metal binding	103	1	Zinc 2 By similarity
	Metal binding	111	1	Zinc 2 By similarity
	Metal binding	152	1	Zinc 1; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q65JE7 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 80F6CC46AA96215F	FASTA	346	37,240
	10 20 30 40 50 60 MDGNMKALIK KPGEPGASFE LVPIPKIDKH EVLIKVKAAS ICGTDVHIYN WDEWAKSRVK 70 80 90 100 110 120 PPYVFGHEFS GEVVQVGENV TTVKEGEYVS AETHIVCGKC LPCLTGKEHV CKKTLILGVD 130 140 150 160 170 180 TDGCFAEYVK MPAANIWKNP AGMPEDLASI QEPLGNAVHT VLTGMTAGVK VAVVGCGPIG 190 200 210 220 230 240 LMAVAVAKAS GAAQVIAIDK NEYRLDLALQ MGATDIISVE KEDPLKNVSA LTNGEGADLV 250 260 270 280 290 300 CEMSGHPTAI RQSLKMAANG GRVHVLSLPE HPVCIDMTND IVFKGLTVQG ITGRKMFETW 310 320 330 340 RQVSGLLQSG TIQIKPVITH RFPMEEFEKG FELMRKGQCG KVVLIP

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000002 Genomic DNA. Translation: AAU23458.1. AE017333 Genomic DNA. Translation: AAU40817.1.
RefSeq	YP_079096.1. NC_006270.3. YP_091510.1. NC_006322.1.
3D structure databases
ProteinModelPortal	Q65JE7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q65JE7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000054394; EBBACP00000052925; EBBACG00000054385. EBBACT00000060787; EBBACP00000059220; EBBACG00000060778.
GeneID	3031140. 3099859.
GenomeReviews	Gene locus BLi01923 in contig AE017333_GR. Gene locus BL03658 in contig CP000002_GR.
KEGG	bld:BLi01923. bli:BL03658.
NMPDR	fig|279010.5.peg.2626.
PATRIC	18949453. VBIBacLic203714_1930.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1063.
GeneTree	EBGT00050000000383.
HOGENOM	HBG753318.
OMA	ADLVCEM.
PhylomeDB	Q65JE7.
ProtClustDB	PRK05396.
Enzyme and pathway databases
BioCyc	BLIC279010-1:BLI01923-MONOMER. BLIC279010:BL03658-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_BACLD

Accession

Primary (citable) accession number: Q65JE7
Secondary accession number(s): Q62UV1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program