Q5QUN8 (TDH_IDILO) 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:	IL0269

Organism

Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]

Taxonomic identifier

283942 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Idiomarinaceae › Idiomarina

Protein attributes

Sequence length	341 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 – 341	341	L-threonine 3-dehydrogenase HAMAP MF_00627		PRO_0000160842
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)
	Q5QUN8 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: B4BBB6A8D6D4DD16	FASTA	341	37,314
	10 20 30 40 50 60 MKALSKLHAK PGIWMTDVEK PECGYNDLLI KIKKTAICGT DVHIYKWDDW SQKTIPVPMV 70 80 90 100 110 120 VGHEYVGEVA AMGDGVRGFE IGDRVSGEGH ITCGHCRNCR AGRRHLCRNT YGVGVNRPGA 130 140 150 160 170 180 FAEYLALPAE NAFKLPDDVT DEMAAVFDPF GNAVHTALAF DLVGEDVLIT GAGPIGIMAA 190 200 210 220 230 240 AVARHVGARH VVITDVNEYR LDLARKMGVT RAVDVSKEKL SDVMTELGMK EGFDVGLEMS 250 260 270 280 290 300 GVPSAFSQML ETMNHGGKIA MLGIPPENIA IDWNQVIFKG LVIKGIYGRE MFETWYKMAS 310 320 330 340 LLQSGLDISP ILTHEMPIDD FEKGFETMIS GQSGKVILNW D

References

[1]

"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy." Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. , Aizawa S., Shibata S., Malahoff A., Alam M. Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017340 Genomic DNA. Translation: AAV81112.1.
RefSeq	YP_154661.1. NC_006512.1.
3D structure databases
ProteinModelPortal	Q5QUN8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3174298.
GenomeReviews	Gene locus IL0269 in contig AE017340_GR.
KEGG	ilo:IL0269.
NMPDR	fig|283942.3.peg.258.
PATRIC	22138547. VBIIdiLoi21852_0270.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG753318.
OMA	MMRSGMS.
ProtClustDB	PRK05396.
Enzyme and pathway databases
BioCyc	ILOI283942:IL0269-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_IDILO

Accession

Primary (citable) accession number: Q5QUN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	January 4, 2005
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program