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A4KSK1 (A4KSK1_FRATU) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-threonine 3-dehydrogenase HAMAP MF_00627

EC=1.1.1.103 HAMAP MF_00627
Gene names
Name:tdh HAMAP MF_00627
ORF Names:FTHG_01419 EMBL EBA52994.1
OrganismFrancisella tularensis subsp. holarctica 257 EMBL EBA52994.1
Taxonomic identifier412422 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH. HAMAP MF_00627 SAAS SAAS002328

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_00627 SAAS SAAS002328

Pathway

Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2. HAMAP MF_00627 SAAS SAAS002328

Subunit structure

Homotetramer By similarity. HAMAP MF_00627

Subcellular location

Cytoplasm By similarity HAMAP MF_00627 SAAS SAAS002328.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. HAMAP MF_00627 RuleBase RU000468

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding391Zinc 1; catalytic By similarity HAMAP MF_00627
Metal binding641Zinc 1; catalytic By similarity HAMAP MF_00627
Metal binding941Zinc 2 By similarity HAMAP MF_00627
Metal binding971Zinc 2 By similarity HAMAP MF_00627
Metal binding1001Zinc 2 By similarity HAMAP MF_00627
Metal binding1081Zinc 2 By similarity HAMAP MF_00627
Metal binding1491Zinc 1; catalytic By similarity HAMAP MF_00627

Sequences

Sequence LengthMass (Da)Tools
A4KSK1 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 1E07E9CCC5A58A79

FASTA35138,400
        10         20         30         40         50         60 
MKALAKLKKQ PGIWMINDAP IPEYGYNDVL IKIKKTAICG TDLHIYNWDK WSQNTIPVPM 

        70         80         90        100        110        120 
ITGHEFAGEV VAKGDGVTSV DIGDRVSGEG HLVCGQCRNC RAGKRHLCRK TIGIGVNVQG 

       130        140        150        160        170        180 
AFAEYLVMPA VNVFKIPDSI SDDIASTFDP MGNAIHTALS FNLTGEDVLI TGAGPIGLMA 

       190        200        210        220        230        240 
VKIARFCGAR RIVITDINEY RLQMARDFGA TVALNVAPFK NQDELVKQMR KVMSDIGMTE 

       250        260        270        280        290        300 
GFDVGLEMSG INSAISMMLD VMNHGGKLSL LGISAGDISV DWGAILFKGL TLKGIYGREM 

       310        320        330        340        350 
FETWYLMTSM LQAGMDMNPI ITHRLHIDEF QKGFEIMKSG QCGKVILDWS S 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS229056 Genomic DNA. Translation: EBA52994.1.

3D structure databases

ProteinModelPortalA4KSK1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC27637789. VBIFraTul12999_1883.

Family and domain databases

HAMAPMF_00627. Thr_dehydrog.
[Tree]
InterProIPR013149. 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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
TIGRFAMsTIGR00692. Tdh. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA4KSK1_FRATU
AccessionPrimary (citable) accession number: A4KSK1
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2007
Last sequence update: May 1, 2007
Last modified: December 14, 2011
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)