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Protein

L-lactate dehydrogenase

Gene

lldD

Organism
Haemophilus influenzae (strain PittGG)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain.UniRule annotation

Catalytic activityi

(S)-lactate + an oxidized electron acceptor = pyruvate + a reduced electron acceptor.UniRule annotation

Cofactori

FMNUniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei24 – 241SubstrateUniRule annotation
Binding sitei106 – 1061FMNUniRule annotation
Binding sitei127 – 1271FMNUniRule annotation
Binding sitei129 – 1291SubstrateUniRule annotation
Binding sitei155 – 1551FMNUniRule annotation
Binding sitei164 – 1641SubstrateUniRule annotation
Binding sitei251 – 2511FMNUniRule annotation
Active sitei275 – 2751Proton acceptorUniRule annotation
Binding sitei278 – 2781SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi306 – 33025FMNUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. lactate dehydrogenase activity Source: InterPro

GO - Biological processi

  1. lactate oxidation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciHINF374931:GJA4-411-MONOMER.
RETL1328306-WGS:GSTH-3179-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenaseUniRule annotation (EC:1.1.-.-UniRule annotation)
Gene namesi
Name:lldDUniRule annotation
Ordered Locus Names:CGSHiGG_02435
OrganismiHaemophilus influenzae (strain PittGG)
Taxonomic identifieri374931 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000001990: Chromosome

Subcellular locationi

Cell inner membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381L-lactate dehydrogenasePRO_1000068986Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi374931.CGSHiGG_02435.

Structurei

3D structure databases

ProteinModelPortaliA5UFG9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 380380FMN hydroxy acid dehydrogenaseUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.UniRule annotation
Contains 1 FMN hydroxy acid dehydrogenase domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG1304.
HOGENOMiHOG000217464.
KOiK00101.
OMAiAWIKEQW.
OrthoDBiEOG6HMXBG.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01559. L_lact_dehydr.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
IPR020920. L-lactate_DHase_bac.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A5UFG9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIISSASDYR EAARRRVPPF MFHYADGGSY AEQTLARNVS DLENIALRQR
60 70 80 90 100
VLKDMSELDT SIELFGEKLS MPTILAPVGA CGMYARRGEV QAAQAADNKG
110 120 130 140 150
VPFTLSTVSI CPIEEVAPAI KRPMWFQLYV LKDRGFMKNA LERAKAAGCS
160 170 180 190 200
TLVFTVDMPT PGARYRDMHS GMSGPYKEIR RVLQGFTHPF WAYDVGIKGK
210 220 230 240 250
PHTLGNVSTY MGRQIGLDDY IGWLTENFDP SISWKDLEWI REFWEGPMVI
260 270 280 290 300
KGILDPEDAK DAVRFGADGI VVSNHGGRQL DGVLSSARAL PPIADAVKGD
310 320 330 340 350
IKIIADSGIR NGLDIVRMLA LGADATMLGR AFVYALGAAG RQGVENMLDI
360 370 380
FKKEMHVAMT LTSNRTIADI KPEALVDLSK L
Length:381
Mass (Da):41,907
Last modified:July 10, 2007 - v1
Checksum:iE1BC67F5B5F2482D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000672 Genomic DNA. Translation: ABQ99524.1.
RefSeqiWP_005671721.1. NC_009567.1.
YP_001291908.1. NC_009567.1.

Genome annotation databases

EnsemblBacteriaiABQ99524; ABQ99524; CGSHiGG_02435.
GeneIDi5227002.
KEGGihiq:CGSHiGG_02435.
PATRICi20185142. VBIHaeInf102487_0491.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000672 Genomic DNA. Translation: ABQ99524.1.
RefSeqiWP_005671721.1. NC_009567.1.
YP_001291908.1. NC_009567.1.

3D structure databases

ProteinModelPortaliA5UFG9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi374931.CGSHiGG_02435.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ99524; ABQ99524; CGSHiGG_02435.
GeneIDi5227002.
KEGGihiq:CGSHiGG_02435.
PATRICi20185142. VBIHaeInf102487_0491.

Phylogenomic databases

eggNOGiCOG1304.
HOGENOMiHOG000217464.
KOiK00101.
OMAiAWIKEQW.
OrthoDBiEOG6HMXBG.

Enzyme and pathway databases

BioCyciHINF374931:GJA4-411-MONOMER.
RETL1328306-WGS:GSTH-3179-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01559. L_lact_dehydr.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
IPR020920. L-lactate_DHase_bac.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiLLDD_HAEIG
AccessioniPrimary (citable) accession number: A5UFG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 10, 2007
Last modified: February 4, 2015
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.