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Q5PLQ7 (LLDD_SALPA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 60. 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
Synonyms:lctD
Ordered Locus Names:SPA3546
OrganismSalmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP]
Taxonomic identifier295319 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

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-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 – 396396L-lactate dehydrogenase [cytochrome] HAMAP-Rule MF_01559
PRO_0000206345

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
Q5PLQ7 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 1CFC8958AEB781CA

FASTA39642,700
        10         20         30         40         50         60 
MIISAASDYR AAAQRTLPPF LFHYIDGGAY AEYTLRRNVE DLSQVALRQR VLKNMSDLSL 

        70         80         90        100        110        120 
ETTLFNETLS MPVALAPVGL CGMYARRGEV QAAAAADAKG IPFTLSTVSV CPIEEVAPTI 

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

       190        200        210        220        230        240 
RYWQAVMHPK WAWDVGLNGR PHDLGNISAY LGKPTGLEDY IGWLANNFDP SISWKDLEWI 

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

       310        320        330        340        350        360 
IAILADSGIR NGLDVVRMIA LGADTVLLGR AYLYALATAG KAGVANLLDL VEKEMKVAMT 

       370        380        390 
LTGAKSISEI SGDSLVQELG KSLPAALAPM SKGDAA 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000026 Genomic DNA. Translation: AAV79347.1.
RefSeqYP_152659.1. NC_006511.1.

3D structure databases

ProteinModelPortalQ5PLQ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295319.SPA3546.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV79347; AAV79347; SPA3546.
PATRIC32356775. VBISalEnt134188_3770.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1304.
HOGENOMHOG000217464.
OMADCTLLGR.
OrthoDBEOG6HMXBG.

Enzyme and pathway databases

BioCycSENT295319:GJBZ-3544-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_bac.
[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_SALPA
AccessionPrimary (citable) accession number: Q5PLQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 4, 2005
Last modified: July 9, 2014
This is version 60 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