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Reviewed, UniProtKB/Swiss-Prot P70787 (TTUC2_AGRVI)

Last modified November 25, 2008. Version 51. 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:
    Probable tartrate dehydrogenase/decarboxylase ttuC
      Short name=TDH
    EC=1.1.1.93
    EC=4.1.1.73
Alternative name(s):
    D-malate dehydrogenase [decarboxylating]
    EC=1.1.1.83
Gene names
Name: ttuC
Encoded onPlasmid pTrAB3
OrganismAgrobacterium vitis (Rhizobium vitis)
Taxonomic identifier373 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

Tartrate + NAD(+) = oxaloglycolate + NADH.

Meso-tartrate + NAD(+) = oxaloglycolate + NADH.

(R,R)-tartrate + NAD(+) = oxaloglycolate + NADH.

(R,R)-tartrate = D-glycerate + CO(2).

(R)-malate + NAD(+) = pyruvate + CO(2) + NADH.

Pathway

Carbohydrate acid metabolism; tartaric acid degradation; 2-hydroxy-3-oxosuccinic acid from L-tartaric acid: step 1/1.

Carbohydrate acid metabolism; tartaric acid degradation; 2-hydroxy-3-oxosuccinic acid from meso-tartaric acid: step 1/1.

Carbohydrate acid metabolism; tartaric acid degradation; D-glyceric acid from L-tartaric acid: step 1/1.

Subcellular location

CytoplasmBy similarity.

Induction

By tartrate.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords

   Cellular componentCytoplasm
   LigandNAD
   Molecular functionLyase
Oxidoreductase
   Technical termPlasmid

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionD-malate dehydrogenase (decarboxylating) activity

Inferred from electronic annotation. Source: EC

NAD binding

Inferred from electronic annotation. Source: InterPro

tartrate decarboxylase activity

Inferred from electronic annotation. Source: EC

tartrate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364Probable tartrate dehydrogenase/decarboxylase ttuC
PRO_0000083814

Sequences

Sequence LengthMass (Da)Tools
P70787-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: D05BED66A360BA3E

FASTA36439,271
        10         20         30         40         50         60 
MREYKIAAIP ADGIGPEVIA AGLQVLEALE KRSGDFSIHT ETFDWGSDYY KKNGVMMPAD 

        70         80         90        100        110        120 
GLEQLKKFDA IFFGAVGAPD VPDHITLWGL RLPICQGFDQ YANVRPTKVL PGITPPLRNC 

       130        140        150        160        170        180 
GPGDLDWVIV RENSEGEYSG HGGRAHKGLP EEVGTEVAIF TRVGVTRIMR YAFKLAQARP 

       190        200        210        220        230        240 
RKLLTVVTKS NAQRHGMVMW DEIAAEVSKE FPDVTWDKML VDAMTVRMTL KPQSLDTIVA 

       250        260        270        280        290        300 
TNLHADILSD LAGALAGSLG VAPTANIDPE RRFPSMFEPI HGSAFDITGK GIANPVATFW 

       310        320        330        340        350        360 
TAAQMLEHLG EKDAATRLMS AVERVTEAGI LTPDVGGTAD TQQVTDAVCE AIAGSNILNM 


AAVG 

« Hide

References

[1]"Characterization and distribution of tartrate utilization genes in the grapevine pathogen Agrobacterium vitis."
Salomone J.-Y., Crouzet P., de Ruffray P., Otten L.
Mol. Plant Microbe Interact. 9:401-408(1996) [PubMed: 8672817] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: AB3.

Cross-references

Sequence databases

U32375 Genomic DNA. Translation: AAB61623.1.

3D structure databases

HSSPHSSP built from PDB template 1XAA based on UniProtKB P00351.
ModBaseSearch...

Family and domain databases

InterProIPR001804. IsoCit_IM_DHase.
IPR011829. TTC_DH.
[Graphical view]
Gene3DG3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHERPTHR11835. IDH_IMDH_dimeric. 1 hit.
PTHR11835:SF8. TTC_DH. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR02089. TTC. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTTUC2_AGRVI
AccessionPrimary (citable) accession number: P70787
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 1, 1997
Last modified: November 25, 2008
This is version 51 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