Q9L233 (TDH_STRCO) 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:	SCO6799
ORF Names:	SC1A2.08

Organism

Streptomyces coelicolor

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	342 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 Reference 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 – 342	342	L-threonine 3-dehydrogenase HAMAP MF_00627		PRO_0000160860
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)
	Q9L233 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 25BC561F49C0E9E1	FASTA	342	36,458
	10 20 30 40 50 60 MKALVKENAE PGLWLADVPE PTIGSGDVLI KVLRTGICGT DLHIRAWDGW AQQAIRTPLV 70 80 90 100 110 120 VGHEFVGEVV DTGRDVTDIK AGDRVSGEGH LVCGKCRNCL AGRRHLCRAT VGLGVGRDGA 130 140 150 160 170 180 FAEYVALPAS NVWVHRVPVD LDVAAIFDPF GNAVHTALSF PLVGEDVLIT GAGPIGLMAA 190 200 210 220 230 240 AVARHAGARN VVITDVSEER LELARKVGAT LALNVSDATI ADGQRELGLR EGFDIGLEMS 250 260 270 280 290 300 GRPEAMRDMI ANMTHGGRIA MLGLPAEEFP VDWARVVTSM ITVKGIYGRE MFETWYAMSV 310 320 330 340 LLEGGLDLAP VITGRYSHRD FEAAFADAAS GRGGKVILDW TA

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL939129 Genomic DNA. Translation: CAB71246.1.
RefSeq	NP_630871.1. NC_003888.3.
3D structure databases
ProteinModelPortal	Q9L233.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1102238.
GenomeReviews	Gene locus SCO6799 in contig AL645882_GR.
KEGG	sco:SCO6799.
NMPDR	fig|100226.1.peg.6736.
PATRIC	23743527. VBIStrCoe124346_6909.
Phylogenomic databases
HOGENOM	HBG753318.
OMA	HIRAWDG.
PhylomeDB	Q9L233.
ProtClustDB	PRK05396.
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.
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TDH_STRCO

Accession

Primary (citable) accession number: Q9L233

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program