Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

L-threonine 3-dehydrogenase

Gene

tdh

Organism
Francisella tularensis subsp. holarctica (strain OSU18)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 2 Zn2+ ions per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi39 – 391Zinc 1; catalyticUniRule annotation
Metal bindingi64 – 641Zinc 1; catalyticUniRule annotation
Metal bindingi94 – 941Zinc 2UniRule annotation
Metal bindingi97 – 971Zinc 2UniRule annotation
Metal bindingi100 – 1001Zinc 2UniRule annotation
Metal bindingi108 – 1081Zinc 2UniRule annotation
Metal bindingi149 – 1491Zinc 1; catalyticUniRule annotation

GO - Molecular functioni

  1. L-threonine 3-dehydrogenase activity Source: UniProtKB-HAMAP
  2. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. L-threonine catabolic process to glycine Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciFTUL393011:GHFN-1509-MONOMER.
UniPathwayiUPA00046; UER00505.

Names & Taxonomyi

Protein namesi
Recommended name:
L-threonine 3-dehydrogenaseUniRule annotation (EC:1.1.1.103UniRule annotation)
Gene namesi
Name:tdhUniRule annotation
Ordered Locus Names:FTH_1473
OrganismiFrancisella tularensis subsp. holarctica (strain OSU18)
Taxonomic identifieri393011 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
ProteomesiUP000000650 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351L-threonine 3-dehydrogenasePRO_1000051640Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi393011.FTH_1473.

Family & Domainsi

Sequence similaritiesi

Belongs to the zinc-containing alcohol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1063.
HOGENOMiHOG000294686.
KOiK00060.
OMAiIPFTIIC.
OrthoDBiEOG60PH85.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
HAMAPiMF_00627. Thr_dehydrog.
InterProiIPR013149. 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]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
TIGRFAMsiTIGR00692. tdh. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0BKV5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALAKLKKQ PGIWMINDAP IPEYGYNDVL IKIKKTAICG TDLHIYNWDK
60 70 80 90 100
WSQNTIPVPM ITGHEFAGEV VAKGDGVTSV DIGDRVSGEG HLVCGQCRNC
110 120 130 140 150
RAGKRHLCRK TIGIGVNVQG AFAEYLVMPA VNVFKIPDSI SDDIASTFDP
160 170 180 190 200
MGNAIHTALS FNLTGEDVLI TGAGPIGLMA VKIARFCGAR RIVITDINEY
210 220 230 240 250
RLQMARDFGA TVALNVAPFK NQDELVKQMR KVMSDIGMTE GFDVGLEMSG
260 270 280 290 300
INSAISMMLD VMNHGGKLSL LGISAGDISV DWGAILFKGL TLKGIYGREM
310 320 330 340 350
FETWYLMTSM LQAGMDMNPI ITHRLHIDEF QKGFEIMKSG QCGKVILDWS

S
Length:351
Mass (Da):38,400
Last modified:October 16, 2006 - v1
Checksum:i1E07E9CCC5A58A79
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000437 Genomic DNA. Translation: ABI83279.1.
RefSeqiYP_763916.1. NC_008369.1.

Genome annotation databases

EnsemblBacteriaiABI83279; ABI83279; FTH_1473.
GeneIDi4307881.
KEGGifth:FTH_1473.
PATRICi17953132. VBIFraTul3936_1691.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000437 Genomic DNA. Translation: ABI83279.1.
RefSeqiYP_763916.1. NC_008369.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi393011.FTH_1473.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI83279; ABI83279; FTH_1473.
GeneIDi4307881.
KEGGifth:FTH_1473.
PATRICi17953132. VBIFraTul3936_1691.

Phylogenomic databases

eggNOGiCOG1063.
HOGENOMiHOG000294686.
KOiK00060.
OMAiIPFTIIC.
OrthoDBiEOG60PH85.

Enzyme and pathway databases

UniPathwayiUPA00046; UER00505.
BioCyciFTUL393011:GHFN-1509-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
HAMAPiMF_00627. Thr_dehydrog.
InterProiIPR013149. 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]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
TIGRFAMsiTIGR00692. tdh. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: OSU18.

Entry informationi

Entry nameiTDH_FRATO
AccessioniPrimary (citable) accession number: Q0BKV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 14, 2008
Last sequence update: October 16, 2006
Last modified: March 31, 2015
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.