Skip Header

Contribute Send feedback
Read comments (?) or add your own

A8A670 (LLDD_ECOHS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-lactate dehydrogenase [cytochrome]
EC=1.1.2.3
Gene names
Name:lldD
Ordered Locus Names:EcHS_A3817
OrganismEscherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]
Taxonomic identifier331112 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+. HAMAP MF_01559

Cofactor

FMN By similarity. HAMAP MF_01559

Sequence similarities

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.

Contains 1 FMN hydroxy acid dehydrogenase domain.

Ontologies

Keywords
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processlactate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionFMN binding

Inferred from electronic annotation. Source: InterPro

L-lactate dehydrogenase (cytochrome) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396L-lactate dehydrogenase [cytochrome] HAMAP MF_01559
PRO_1000068980

Regions

Domain1 – 380380FMN hydroxy acid dehydrogenase
Nucleotide binding306 – 33025FMN By similarity

Sites

Active site2751Proton acceptor By similarity
Binding site241Substrate Potential
Binding site1061FMN By similarity
Binding site1271FMN By similarity
Binding site1291Substrate By similarity
Binding site1551FMN By similarity
Binding site1641Substrate By similarity
Binding site2511FMN By similarity
Binding site2781Substrate Potential

Sequences

Sequence LengthMass (Da)Tools
A8A670 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: CA0D8E308713BF83

FASTA39642,728
        10         20         30         40         50         60 
MIISAASDYR AAAQRILPPF LFHYMDGGAY SEYTLRRNVE DLSEVALRQR ILKNMSDLSL 

        70         80         90        100        110        120 
ETTLFNEKLS MPVALAPVGL CGMYARRGEV QAAKAADAHG IPFTLSTVSV CPIEEVAPAI 

       130        140        150        160        170        180 
KRPMWFQLYV LRDRGFMRNA LERAKAAGCS TLVFTVDMPT PGARYRDAHS GMSGPNAAMR 

       190        200        210        220        230        240 
RYLQAVTHPQ WAWDVGLNGR PHDLGNISAY LGKPTGLEDY IGWLGNNFDP SISWKDLEWI 

       250        260        270        280        290        300 
RDFWDGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD 

       310        320        330        340        350        360 
IAILADSGIR NGLDVVRMIA LGADTVLLGR AFLYALATAG QAGVANLLNL IEKEMKVAMT 

       370        380        390 
LTGAKSISEI TQDSLVQGLG KELPAALAPM AKGNAA

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000802 Genomic DNA. Translation: ABV08024.1.
RefSeqYP_001460407.1. NC_009800.1.

3D structure databases

ProteinModelPortalA8A670.
SMRA8A670. Positions 3-377.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8A670.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000054903; EBESCP00000052888; EBESCG00000053951.
GeneID5593203.
GenomeReviewsGene locus EcHS_A3817 in contig CP000802_GR.
KEGGecx:EcHS_A3817.
PATRIC18317603. VBIEscCol77814_3728.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1304.
GeneTreeEBGT00050000009653.
HOGENOMHBG517781.
OMAIGWLTEN.
ProtClustDBPRK11197.

Family and domain databases

HAMAPMF_01559. L-lact_dehydr.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
IPR020920. L-lactate_DHase_cyt.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK00101.
PfamPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLLDD_ECOHS
AccessionPrimary (citable) accession number: A8A670
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents