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Reviewed, UniProtKB/Swiss-Prot Q31V17 (LLDD_SHIBS)

Last modified November 25, 2008. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    L-lactate dehydrogenase [cytochrome]
    EC=1.1.2.3
Gene names
Name: lldD
Ordered Locus Names: SBO_3610
OrganismShigella boydii serotype 4 (strain Sb227) [Complete proteome] [HAMAP]
Taxonomic identifier300268 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

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Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

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

Cofactor

FMN By similarity.

Sequence similarities

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

Contains 1 FMN hydroxy acid dehydrogenase domain.

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Ontologies

Keywords

   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionFMN binding

Inferred from electronic annotation. Source: InterPro

L-lactate dehydrogenase (cytochrome) activity

Inferred from electronic annotation. Source: HAMAP

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396L-lactate dehydrogenase [cytochrome]
PRO_0000206348

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

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Sequences

Sequence LengthMass (Da)Tools
Q31V17-1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: CA022F258717A133

FASTA39642,758
        10         20         30         40         50         60 
MIISAASDYR AAAQRILPPF LFHYMDGGAY SEYTLRRNVE DLSEVALRQR ILKNMSDLSL 

        70         80         90        100        110        120 
ETTLFNEKLS MPVALAPVGL CGMYARRGEV QAAKAADTHG 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

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References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed: 16275786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000036 Genomic DNA. Translation: ABB68091.1.
RefSeqYP_409919.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3782593.
GenomeReviewsGene locus SBO_3610 in contig CP000036_GR.
KEGGsbo:SBO_3610.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ31V17.

Enzyme and pathway databases

BioCycSBOY300268:SBO_3610-MON.

Family and domain databases

HAMAPMF_01559.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012133. Alpha_OHA_DHase_FMN.
IPR008259. FMN_hydac_DHase_AS.
IPR000262. FMN_OHA_DHase.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
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...

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Entry information

Entry nameLLDD_SHIBS
AccessionPrimary (citable) accession number: Q31V17
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: December 6, 2005
Last modified: November 25, 2008
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents