Reviewed, UniProtKB/Swiss-Prot Q9RTU4 (TDH_DEIRA)

Names and origin

Protein names

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

Gene names

Name:	tdh
Ordered Locus Names:	DR_1662

Organism

Deinococcus radiodurans [Complete proteome] [HAMAP]

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW threonine catabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-threonine 3-dehydrogenase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 348	348	L-threonine 3-dehydrogenase HAMAP MF_00627		PRO_0000160836
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)
	Q9RTU4-1 [UniParc]. Last modified March 28, 2003. Version 2. Checksum: C9A8AE6BDE546BF7	FASTA	348	37,752
	10 20 30 40 50 60 MRALSKQQPG EGIWMIETEV PTPGPNDLLI RIRKGSICGT DVHIYKWDDW ASQTVPVPMV 70 80 90 100 110 120 VGHEYVGVVA GMGSEVRGFE IGDRVSGEGH VTCGHCRNCR AGRRHLCRNT QGVGVNRPGS 130 140 150 160 170 180 FAEYLVLPAF NAFKLPDDIP DDVAAIFDPF GNAVHTALSF DLVGEDVLIT GAGPIGCMAA 190 200 210 220 230 240 AVARHVGARN VVITDVNDYR LDLARQMGVT RAVNVAREDL WTVATQELDM HEGFDVGMEM 250 260 270 280 290 300 SGSGPAFAQM VSVMNNGGKV ALLGIPSGEV QIDWNAVIFK MLTIKGIYGR EMFETWYKMA 310 320 330 340 ALIQSGLDLT PVITHHYGIG DFQQGFDAML SGQSGKVILD WETEEQSA

References

[1]

"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000513 Genomic DNA. Translation: AAF11215.1. Different initiation.
PIR	A75371.
RefSeq	NP_295385.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1798709.
GenomeReviews	Gene locus DR_1662 in contig AE000513_GR.
KEGG	dra:DR_1662.
NMPDR	fig|243230.1.peg.1844.
TIGR	DR_1662.
Phylogenomic databases
HOGENOM	Q9RTU4.
Enzyme and pathway databases
BioCyc	DRAD243230:DR_1662-MON.
BRENDA	1.1.1.103. 96172.
Family and domain databases
HAMAP	MF_00627. [Tree]
InterPro	IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. IPR004627. L-Threonine_3-DHase. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
ProDom	PD040557. GroES_related. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00692. tdh. 1 hit.
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TDH_DEIRA

Accession

Primary (citable) accession number: Q9RTU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	March 28, 2003
Last modified:	September 22, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)