Reviewed, UniProtKB/Swiss-Prot Q83F39 (TDH_COXBU)

Names and origin

Protein names

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

Gene names

Name:	tdh
Ordered Locus Names:	CBU_0112

Organism

Coxiella burnetii [Complete proteome] [HAMAP]

Taxonomic identifier

777 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella

Protein attributes

Sequence length	342 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 – 342	342	L-threonine 3-dehydrogenase HAMAP MF_00627		PRO_0000160835
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)
	Q83F39-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 71007C99C50DF6B6	FASTA	342	37,194
	10 20 30 40 50 60 MKVLSKLKPA PGLWLHKAPT PKPGRDEVLI KIKKTAICGT DLHIYKWDEW AQKTIPVPMH 70 80 90 100 110 120 VGHEFVGEIV EVGEAASALA VGDRVSGEGH ITCGDCRNCR AGKRHLCRYT VGVGVNRPGA 130 140 150 160 170 180 FAEYLVIPAK NAYKIPAKIS DDIAAILDPF GNAAHSALEF DLVGEDVLIT GAGPVGLMSA 190 200 210 220 230 240 AIARHVGARH VVITDVNDYR LALAEKVGVT AAVNSTKTPL TETMKNLGMT EGFDVGLEMS 250 260 270 280 290 300 GNAEAFRSML TVMNNGGKIA FLGIPPEPFA IDWNQVVFKS LLIKGIYGRR MFETWYKMTN 310 320 330 340 LLLSGLDISP IITHEFPMKD FQQAFDVMLS GKTGKVILNW EQ

References

[1]

"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed: 12704232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nine Mile phase I / RSA 493.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016828 Genomic DNA. Translation: AAO89676.1.
RefSeq	NP_819162.1.
3D structure databases
HSSP	HSSP built from PDB template 1F8F based on UniProtKB Q59096.
ModBase	Search...
Genome annotation databases
GeneID	1207983.
GenomeReviews	Gene locus CBU_0112 in contig AE016828_GR.
KEGG	cbu:CBU_0112.
NMPDR	fig|227377.1.peg.106.
TIGR	CBU_0112.
Phylogenomic databases
HOGENOM	Q83F39.
OMA	IWMVDAP.
Enzyme and pathway databases
BioCyc	CBUR227377:CBU_0112-MON.
BRENDA	1.1.1.103. 256353.
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_COXBU

Accession

Primary (citable) accession number: Q83F39

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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