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
Submitted name:

Fermentative D-lactate dehydrogenase, NAD-dependent

Gene

ldhA

Organism
Escherichia coli O103:H2 (strain 12009 / EHEC)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Protein inferred from homologyi

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Enzyme and pathway databases

BioCyciECOL585395:GJA9-1561-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Fermentative D-lactate dehydrogenase, NAD-dependentImported
Gene namesi
Name:ldhAImported
Ordered Locus Names:ECO103_1516Imported
OrganismiEscherichia coli O103:H2 (strain 12009 / EHEC)Imported
Taxonomic identifieri585395 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000959 Componenti: Chromosome

Structurei

3D structure databases

ProteinModelPortaliC8U864.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1052.
HOGENOMiHOG000136695.
KOiK03778.
OMAiLMMTLNR.
OrthoDBiEOG61VZ8G.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C8U864-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLAVYSTKQ YDKKYLQQVN ESFGFELEFF DFLLTEKTAK TANGCEAVCI
60 70 80 90 100
FVNDDGSRPV LEELKKHGVK YIALRCAGFN NVDLDAAKEL GLKVVRVPAY
110 120 130 140 150
DPEAVAEHAI GMMMTLNRRI HRAYQRTRDA NFSLEGLTGF TMYGKTAGVI
160 170 180 190 200
GTGKIGVAML RILKGFGMRL LAFDPYPSAA ALELGVEYVD LPTLFSESDV
210 220 230 240 250
ISLHCPLTPE NYHLLNEAAF DQMKNGVMIV NTSRGALIDS QAAIEALKNQ
260 270 280 290 300
KIGSLGMDVY ENERDLFFED KSNDVIQDDV FRRLSACHNV LFTGHQAFLT
310 320
AEALTSISQT TLQNLSNLEK GETCPNELV
Length:329
Mass (Da):36,521
Last modified:November 3, 2009 - v1
Checksum:i84E8F685F913993C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010958 Genomic DNA. Translation: BAI30342.1.
RefSeqiWP_000762229.1. NC_013353.1.
YP_003221476.1. NC_013353.1.

Genome annotation databases

EnsemblBacteriaiBAI30342; BAI30342; ECO103_1516.
KEGGieoh:ECO103_1516.
PATRICi32094779. VBIEscCol146794_1591.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010958 Genomic DNA. Translation: BAI30342.1.
RefSeqiWP_000762229.1. NC_013353.1.
YP_003221476.1. NC_013353.1.

3D structure databases

ProteinModelPortaliC8U864.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAI30342; BAI30342; ECO103_1516.
KEGGieoh:ECO103_1516.
PATRICi32094779. VBIEscCol146794_1591.

Phylogenomic databases

eggNOGiCOG1052.
HOGENOMiHOG000136695.
KOiK03778.
OMAiLMMTLNR.
OrthoDBiEOG61VZ8G.

Enzyme and pathway databases

BioCyciECOL585395:GJA9-1561-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
    Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
    Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 12009 / EHECImported.

Entry informationi

Entry nameiC8U864_ECO10
AccessioniPrimary (citable) accession number: C8U864
Entry historyi
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: June 24, 2015
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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.