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A9IN89 (LLDD_BART1) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 42. 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:BT_0300
OrganismBartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]
Taxonomic identifier382640 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length383 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 – 383383L-lactate dehydrogenase [cytochrome] HAMAP-Rule MF_01559
PRO_0000383414

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
A9IN89 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 8D5A792088C79878

FASTA38341,985
        10         20         30         40         50         60 
MIIASTFDYR KAAKRRLPPF LFHYIDGGAY AEETLRRNCS DLQALALRQR ILRQVGGVDL 

        70         80         90        100        110        120 
SIKLFEQRLD LPIVLAPVGL TGMYARRGEV QAAHAATAKG IPFTLSSVSV CPIAEVQEAV 

       130        140        150        160        170        180 
GGGFWFQLYV LKDRGFMRDA LERAWASGVR TLVFTVDMPI PGARYRDAHS GMSGPYAGLR 

       190        200        210        220        230        240 
RFLQAFTHPH WAWNVGIMGR PHDLGNVSTY LEKKIALDDY VGWLGANFDP SIGWHDLQWI 

       250        260        270        280        290        300 
RDFWKGKMIL KGILDPEDAR EAVQFGADGI VVSNHGGRQL DGVLSTARAL PAIAEAVKND 

       310        320        330        340        350        360 
LVILADSGVR SGLDVVRMIA QGADAVMIGR AFVYALAAAG EKGVAHLLDL FANEMRVAMT 

       370        380 
LTGAQTLKEI TCESLVNTDA FKQ 

« Hide

References

[1]"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
Nat. Genet. 39:1469-1476(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIP 105476 / IBS 506.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260525 Genomic DNA. Translation: CAK00766.1.
RefSeqYP_001608761.1. NC_010161.1.

3D structure databases

ProteinModelPortalA9IN89.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING382640.Btr_0300.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5830085.
KEGGbtr:Btr_0300.
PATRIC20548332. VBIBarTri113218_0327.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1304.
KOK00101.
OMADANESML.
OrthoDBEOG6HMXBG.

Enzyme and pathway databases

BioCycBTRI382640:GJEK-263-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_BART1
AccessionPrimary (citable) accession number: A9IN89
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 5, 2008
Last modified: July 9, 2014
This is version 42 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