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A5UFG9 (LLDD_HAEIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:CGSHiGG_02435
OrganismHaemophilus influenzae (strain PittGG) [Complete proteome] [HAMAP]
Taxonomic identifier374931 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

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_1000068986

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
A5UFG9 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: E1BC67F5B5F2482D

FASTA38141,907
        10         20         30         40         50         60 
MIISSASDYR EAARRRVPPF MFHYADGGSY AEQTLARNVS DLENIALRQR VLKDMSELDT 

        70         80         90        100        110        120 
SIELFGEKLS MPTILAPVGA CGMYARRGEV QAAQAADNKG VPFTLSTVSI CPIEEVAPAI 

       130        140        150        160        170        180 
KRPMWFQLYV LKDRGFMKNA LERAKAAGCS TLVFTVDMPT PGARYRDMHS GMSGPYKEIR 

       190        200        210        220        230        240 
RVLQGFTHPF WAYDVGIKGK PHTLGNVSTY MGRQIGLDDY IGWLTENFDP SISWKDLEWI 

       250        260        270        280        290        300 
REFWEGPMVI KGILDPEDAK DAVRFGADGI VVSNHGGRQL DGVLSSARAL PPIADAVKGD 

       310        320        330        340        350        360 
IKIIADSGIR NGLDIVRMLA LGADATMLGR AFVYALGAAG RQGVENMLDI FKKEMHVAMT 

       370        380 
LTSNRTIADI KPEALVDLSK L 

« Hide

References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PittGG.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000672 Genomic DNA. Translation: ABQ99524.1.
RefSeqYP_001291908.1. NC_009567.1.

3D structure databases

ProteinModelPortalA5UFG9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374931.CGSHiGG_02435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ99524; ABQ99524; CGSHiGG_02435.
GeneID5227002.
KEGGhiq:CGSHiGG_02435.
PATRIC20185142. VBIHaeInf102487_0491.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycHINF374931:GJA4-411-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_HAEIG
AccessionPrimary (citable) accession number: A5UFG9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 10, 2007
Last modified: February 19, 2014
This is version 43 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