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Protein

L(+)-tartrate dehydratase subunit alpha

Gene

ttdA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(R,R)-tartrate = oxaloacetate + H2O.1 Publication

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi71 – 711Iron-sulfurBy similarity
Metal bindingi190 – 1901Iron-sulfurBy similarity
Metal bindingi277 – 2771Iron-sulfurBy similarity

GO - Molecular functioni

GO - Biological processi

  • single-species biofilm formation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:TTDA-MONOMER.
ECOL316407:JW3033-MONOMER.
MetaCyc:TTDA-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
L(+)-tartrate dehydratase subunit alpha (EC:4.2.1.32)
Short name:
L-TTD alpha
Gene namesi
Name:ttdA
Synonyms:ygjA
Ordered Locus Names:b3061, JW3033
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11168. ttdA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303L(+)-tartrate dehydratase subunit alphaPRO_0000195663Add
BLAST

Proteomic databases

PaxDbiP05847.
PRIDEiP05847.

Expressioni

Inductioni

Induced by tartrate, via TtdR.1 Publication

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
glpRP0ACL02EBI-1113137,EBI-1123685

Protein-protein interaction databases

BioGridi4263296. 17 interactions.
IntActiP05847. 6 interactions.
STRINGi511145.b3061.

Structurei

3D structure databases

ProteinModelPortaliP05847.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-I fumarase family.Curated

Phylogenomic databases

eggNOGiENOG4106DSS. Bacteria.
COG1951. LUCA.
HOGENOMiHOG000225707.
InParanoidiP05847.
KOiK03779.
OMAiIQCWANR.
OrthoDBiEOG6TXR10.
PhylomeDBiP05847.

Family and domain databases

InterProiIPR004646. Fe-S_hydro-lyase_TtdA-typ_cat.
[Graphical view]
PfamiPF05681. Fumerase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00722. ttdA_fumA_fumB. 1 hit.

Sequencei

Sequence statusi: Complete.

P05847-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSESNKQQA VNKLTEIVAN FTAMISTRMP DDVVDKLKQL KDAETSSMGK
60 70 80 90 100
IIYHTMFDNM QKAIDLNRPA CQDTGEIMFF VKVGSRFPLL GELQSILKQA
110 120 130 140 150
VEEATVKAPL RHNAVEIFDE VNTGKNTGSG VPWVTWDIIP DNDDAEIEVY
160 170 180 190 200
MAGGGCTLPG RSKVLMPSEG YEGVVKFVFE NISTLAVNAC PPVLVGVGIA
210 220 230 240 250
TSVETAAVLS RKAILRPIGS RHPNPKAAEL ELRLEEGLNR LGIGPQGLTG
260 270 280 290 300
NSSVMGVHIE SAARHPSTIG VAVSTGCWAH RRGTLLVHAD LTFENLSHTR

SAL
Length:303
Mass (Da):32,734
Last modified:August 29, 2003 - v3
Checksum:iCBE29FEB6C47DB81
GO

Sequence cautioni

The sequence AAA72573.1 differs from that shown. Reason: Frameshift at position 198. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111V → L (PubMed:8371115).Curated
Sequence conflicti11 – 111V → L (PubMed:3297921).Curated
Sequence conflicti231 – 2322EL → DV (PubMed:8371115).Curated
Sequence conflicti231 – 2322EL → DV (PubMed:3297921).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14781 Unassigned DNA. Translation: AAA03061.1.
M16194 Genomic DNA. Translation: AAA72573.1. Frameshift.
U28379 Genomic DNA. Translation: AAA89141.1.
U00096 Genomic DNA. Translation: AAC76097.1.
AP009048 Genomic DNA. Translation: BAE77112.1.
PIRiC65094. QQECRT.
RefSeqiNP_417533.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76097; AAC76097; b3061.
BAE77112; BAE77112; BAE77112.
GeneIDi947565.
KEGGiecj:JW3033.
eco:b3061.
PATRICi32121536. VBIEscCol129921_3155.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14781 Unassigned DNA. Translation: AAA03061.1.
M16194 Genomic DNA. Translation: AAA72573.1. Frameshift.
U28379 Genomic DNA. Translation: AAA89141.1.
U00096 Genomic DNA. Translation: AAC76097.1.
AP009048 Genomic DNA. Translation: BAE77112.1.
PIRiC65094. QQECRT.
RefSeqiNP_417533.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP05847.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263296. 17 interactions.
IntActiP05847. 6 interactions.
STRINGi511145.b3061.

Proteomic databases

PaxDbiP05847.
PRIDEiP05847.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76097; AAC76097; b3061.
BAE77112; BAE77112; BAE77112.
GeneIDi947565.
KEGGiecj:JW3033.
eco:b3061.
PATRICi32121536. VBIEscCol129921_3155.

Organism-specific databases

EchoBASEiEB1156.
EcoGeneiEG11168. ttdA.

Phylogenomic databases

eggNOGiENOG4106DSS. Bacteria.
COG1951. LUCA.
HOGENOMiHOG000225707.
InParanoidiP05847.
KOiK03779.
OMAiIQCWANR.
OrthoDBiEOG6TXR10.
PhylomeDBiP05847.

Enzyme and pathway databases

BioCyciEcoCyc:TTDA-MONOMER.
ECOL316407:JW3033-MONOMER.
MetaCyc:TTDA-MONOMER.

Miscellaneous databases

PROiP05847.

Family and domain databases

InterProiIPR004646. Fe-S_hydro-lyase_TtdA-typ_cat.
[Graphical view]
PfamiPF05681. Fumerase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00722. ttdA_fumA_fumB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the L-tartrate dehydratase genes (ttdA and ttdB) of Escherichia coli and evolutionary relationship with the class I fumarase genes."
    Reaney S.K., Begg C., Bungard S.I., Guest J.R.
    J. Gen. Microbiol. 139:1523-1530(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, SUBUNIT.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "Possible new genes as revealed by molecular analysis of a 5-kb Escherichia coli chromosomal region 5' to the rpsU-dnaG-rpoD macromolecular-synthesis operon."
    Nesin M., Lupski J.R., Svec P., Godson G.N.
    Gene 51:149-161(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Functional identification of ygiP as a positive regulator of the ttdA-ttdB-ygjE operon."
    Oshima T., Biville F.
    Microbiology 152:2129-2135(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiTTDA_ECOLI
AccessioniPrimary (citable) accession number: P05847
Secondary accession number(s): P33130, Q2M9E4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: August 29, 2003
Last modified: January 20, 2016
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.