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Protein

L-lactate dehydrogenase

Gene

lldD

Organism
Pseudomonas putida (strain GB-1)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciPPUT76869:GIXB-4820-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenaseUniRule annotation (EC:1.1.-.-UniRule annotation)
Gene namesi
Name:lldDUniRule annotation
Ordered Locus Names:PputGB1_4737
OrganismiPseudomonas putida (strain GB-1)
Taxonomic identifieri76869 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002157 Componenti: Chromosome

Subcellular locationi

  • Cell inner membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

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_0000383435Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi76869.PputGB1_4737.

Structurei

3D structure databases

ProteinModelPortaliB0KIT4.
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. LldD.
[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.

B0KIT4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIISASTDYR AAAQRKLPPF LFHYADGGAY AEHTLRHNVS DLASIALRQR
60 70 80 90 100
VLNNMSELSL STRLFDETLS MPVALAPVGL TGMYARRGEV QAARAAAAHG
110 120 130 140 150
IPFTMSTVSV CPIEEVAPAI DRPMWFQLYV LKDRGFMRNA LERAKAAGVK
160 170 180 190 200
TLVFTVDMPV PGARYRDAHS GMSGKNGPLR RVLQAMTHPE WAWDVGVMGR
210 220 230 240 250
PHDLGNISKY RGNPTGLADY IGWLGNNFDP SISWKDLEWI REYWDGPMII
260 270 280 290 300
KGILDADDAR DAVKFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD
310 320 330 340 350
LKILADSGIR SGLDVVRMIA LGADTVLIGR AFLYALAVHG QAGVKNLLEL
360 370 380
FEKEMRVAMV LTGAKSISEI TRDSLVRELG A
Length:381
Mass (Da):41,425
Last modified:March 18, 2008 - v1
Checksum:i5D6ADA7B3C30459D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000926 Genomic DNA. Translation: ABZ00624.1.
RefSeqiWP_012274264.1. NC_010322.1.
YP_001670959.1. NC_010322.1.

Genome annotation databases

EnsemblBacteriaiABZ00624; ABZ00624; PputGB1_4737.
KEGGippg:PputGB1_4737.
PATRICi19936571. VBIPsePut76638_4745.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000926 Genomic DNA. Translation: ABZ00624.1.
RefSeqiWP_012274264.1. NC_010322.1.
YP_001670959.1. NC_010322.1.

3D structure databases

ProteinModelPortaliB0KIT4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi76869.PputGB1_4737.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABZ00624; ABZ00624; PputGB1_4737.
KEGGippg:PputGB1_4737.
PATRICi19936571. VBIPsePut76638_4745.

Phylogenomic databases

eggNOGiCOG1304.
HOGENOMiHOG000217464.
KOiK00101.
OMAiAWIKEQW.
OrthoDBiEOG6HMXBG.

Enzyme and pathway databases

BioCyciPPUT76869:GIXB-4820-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. LldD.
[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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GB-1.

Entry informationi

Entry nameiLLDD_PSEPG
AccessioniPrimary (citable) accession number: B0KIT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: March 18, 2008
Last modified: June 24, 2015
This is version 49 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.