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Reviewed, UniProtKB/Swiss-Prot A6W1W3 (TDH_MARMS)

Last modified November 3, 2009. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    L-threonine 3-dehydrogenase
    EC=1.1.1.103
Gene names
Name: tdh
Ordered Locus Names: Mmwyl1_3793
OrganismMarinomonas sp. (strain MWYL1) [Complete proteome] [HAMAP]
Taxonomic identifier400668 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesMarinomonas

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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 componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

threonine catabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341L-threonine 3-dehydrogenase HAMAP MF_00627
PRO_1000082612

Sites

Metal binding381Zinc 1; catalytic By similarity
Metal binding631Zinc 1; catalytic By similarity
Metal binding931Zinc 2 By similarity
Metal binding961Zinc 2 By similarity
Metal binding991Zinc 2 By similarity
Metal binding1071Zinc 2 By similarity
Metal binding1481Zinc 1; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A6W1W3-1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 9180E66CFDDEE13F

FASTA34137,328
        10         20         30         40         50         60 
MKTLAKLHAE KGIWMTDVPH PDCGHNDVVI KISKTAICGT DMHIYQWDDW AQNTIPVPMT 

        70         80         90        100        110        120 
VGHEFVGVIT EVGPEVSGFK IGDRVSGEGH ITCGHCRNCR AGRRHLCRKT LGVGVNRTGA 

       130        140        150        160        170        180 
FAEYLVIPAS NAFKIPNNIS DDMAAIFDPF GNATHTALSF DLIGEDVLIT GAGPIGAMAA 

       190        200        210        220        230        240 
AIAKHVGARN VVITDVNDFR LDLAKKMGAT RTVNVSRESL KDVMTEIDMH EGFDVGLEMS 

       250        260        270        280        290        300 
GNDMAFRSML ECMNHGGKIA MLGIPGKDTL IDWNQVIFKG LIIKGIYGRE MYETWYKMVA 

       310        320        330        340 
MLQSGLDISP IITHRFKVDE FQQGFDTMGS GLSGKVILDW N 

« Hide

References

[1]"Complete sequence of Marinomonas sp. MWYL1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000749 Genomic DNA. Translation: ABR72692.1.
RefSeqYP_001342627.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA6W1W3.

Genome annotation databases

GeneID5365579.
GenomeReviewsGene locus Mmwyl1_3793 in contig CP000749_GR.
KEGGmmw:Mmwyl1_3793.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAWAASTIN.

Family and domain databases

HAMAPMF_00627.
[Tree]
InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
IPR004627. L-Threonine_3-DHase.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR00692. tdh. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTDH_MARMS
AccessionPrimary (citable) accession number: A6W1W3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: November 3, 2009
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents