Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B4SMK1 (LLDD_STRM5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 34. 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:Smal_2360
OrganismStenotrophomonas maltophilia (strain R551-3) [Complete proteome] [HAMAP]
Taxonomic identifier391008 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group

Protein attributes

Sequence length379 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 – 379379L-lactate dehydrogenase [cytochrome] HAMAP-Rule MF_01559
PRO_0000383450

Regions

Domain1 – 379379FMN 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
B4SMK1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 9B5E9439EFC94C2B

FASTA37941,175
        10         20         30         40         50         60 
MIISASTDYR AAAQRRLPPF LFHYIDGGAY AEHTLKRNVS DLSDIALRQR VLRNMSDLSL 

        70         80         90        100        110        120 
ETELFGETLA MPVALAPVGL TGMYARRGEV QAARAADSRG IPFTLSTVSV CPIEEVAPAI 

       130        140        150        160        170        180 
QRPMWFQLYV LRDRGFMRNA LERAQAAGVT TLVFTVDMPV PGARYRDAHS GMSGPNASLR 

       190        200        210        220        230        240 
RIGQAITHPH WAWDVGLFGR PHDLGNISTY RGNPTGLEDY IGWLGSNFDP SISWKDLEWI 

       250        260        270        280        290        300 
REFWKGPMVI KGILDPDDAR DAVKFGADGI VVSNHGGRQL DGVLSTARAL PAIADAVQGD 

       310        320        330        340        350        360 
LKILADSGIR TGLDVVRMLA LGADTVLLGR AFVYALAAQG EAGVANLLDL IAKEMRVAMT 

       370 
LTGARRIADI GRDSLVNLP 

« Hide

References

[1]"Complete sequence of Stenotrophomonas maltophilia R551-3."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Taghavi S., Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R551-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001111 Genomic DNA. Translation: ACF52063.1.
RefSeqYP_002028746.1. NC_011071.1.

3D structure databases

ProteinModelPortalB4SMK1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391008.Smal_2360.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF52063; ACF52063; Smal_2360.
GeneID6476843.
KEGGsmt:Smal_2360.
PATRIC23709664. VBISteMal40512_2384.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1304.
HOGENOMHOG000217464.
KOK00101.
OMAHADGEML.
OrthoDBEOG6HMXBG.
ProtClustDBCLSK2340224.

Enzyme and pathway databases

BioCycSMAL391008:GH1H-2414-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_STRM5
AccessionPrimary (citable) accession number: B4SMK1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 34 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