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A9R623 (LLDD_YERPG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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

Names and origin

Protein namesRecommended name:
L-lactate dehydrogenase [cytochrome]

EC=1.1.2.3
Gene names
Name:lldD
Ordered Locus Names:YpAngola_A1696
OrganismYersinia pestis bv. Antiqua (strain Angola) [Complete proteome] [HAMAP]
Taxonomic identifier349746 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Cofactor

FMN By similarity. HAMAP-Rule MF_01559

Sequence similarities

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

Contains 1 FMN hydroxy acid dehydrogenase domain.

Ontologies

Keywords
   LigandFlavoprotein
FMN
   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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 381381L-lactate dehydrogenase [cytochrome] HAMAP-Rule MF_01559
PRO_0000383455

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
A9R623 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: ECC708A08D5E4634

FASTA38141,259
        10         20         30         40         50         60 
MIISASTDYR AAAQRKLPPF LFHYIDGGAY NEQTLRRNTA DLADIALRQR VLKNMSELSL 

        70         80         90        100        110        120 
ETQLFGETQA MPVVLGPVGL SGMYARRGEV QAARAADKKG IPFTLSTLSV CPIEEVAPAI 

       130        140        150        160        170        180 
ARPMWFQLYV LKDRGFMRNA LTRAQAAGVK TLVFTVDMPV PGARYRDAHS GMSGPNAAAR 

       190        200        210        220        230        240 
RLLQAIAHPQ WAWDVGLNGK PHDLGNISAY LGKPTTLEDY MGWIATNFDP SISWKDLEWV 

       250        260        270        280        290        300 
REFWQGPMII KGILDPEDAK DAVKFGADGI VVSNHGGRQL DGVLSTARAL PAIADAVKGD 

       310        320        330        340        350        360 
ITILADSGIR TGLDVVRMIA LGADSVLLGR AFVYALATAG EAGVINLLTL IEQEMRVAMT 

       370        380 
LTGAKRIADI NRDSLAVSER G 

« Hide

References

[1]"Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Angola.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000901 Genomic DNA. Translation: ABX85222.1.
RefSeqYP_001606191.1. NC_010159.1.

3D structure databases

ProteinModelPortalA9R623.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349746.YpAngola_A1696.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX85222; ABX85222; YpAngola_A1696.
GeneID5800167.
KEGGypg:YpAngola_A1696.
PATRIC18572574. VBIYerPes97331_2071.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1304.
HOGENOMHOG000217464.
KOK00101.
OMAHADGEML.
OrthoDBEOG6HMXBG.
ProtClustDBPRK11197.

Enzyme and pathway databases

BioCycYPES349746:GHPB-1703-MONOMER.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01559. L_lact_dehydr.
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]
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_YERPG
AccessionPrimary (citable) accession number: A9R623
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 5, 2008
Last modified: February 19, 2014
This is version 40 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