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Protein

L-lactate dehydrogenase

Gene

lldD

Organism
Bartonella tribocorum (strain CIP 105476 / IBS 506)
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)DescriptionActionsGraphical viewLength
Binding sitei24SubstrateUniRule annotation1
Binding sitei106FMNUniRule annotation1
Binding sitei127FMNUniRule annotation1
Binding sitei129SubstrateUniRule annotation1
Binding sitei155FMNUniRule annotation1
Binding sitei164SubstrateUniRule annotation1
Binding sitei251FMNUniRule annotation1
Active sitei275Proton acceptorUniRule annotation1
Binding sitei278SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi306 – 330FMNUniRule annotationAdd BLAST25

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenaseUniRule annotation (EC:1.1.-.-UniRule annotation)
Gene namesi
Name:lldDUniRule annotation
Ordered Locus Names:BT_0300
OrganismiBartonella tribocorum (strain CIP 105476 / IBS 506)
Taxonomic identifieri382640 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella
Proteomesi
  • UP000001592 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)DescriptionActionsGraphical viewLength
ChainiPRO_00003834141 – 383L-lactate dehydrogenaseAdd BLAST383

Proteomic databases

PRIDEiA9IN89.

Interactioni

Protein-protein interaction databases

STRINGi382640.Btr_0300.

Structurei

3D structure databases

ProteinModelPortaliA9IN89.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 380FMN hydroxy acid dehydrogenaseUniRule annotationAdd BLAST380

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

eggNOGiENOG4105DMF. Bacteria.
COG1304. LUCA.
KOiK00101.
OMAiTLKRPMW.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01559. L_lact_dehydr. 1 hit.
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.

A9IN89-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIIASTFDYR KAAKRRLPPF LFHYIDGGAY AEETLRRNCS DLQALALRQR
60 70 80 90 100
ILRQVGGVDL SIKLFEQRLD LPIVLAPVGL TGMYARRGEV QAAHAATAKG
110 120 130 140 150
IPFTLSSVSV CPIAEVQEAV GGGFWFQLYV LKDRGFMRDA LERAWASGVR
160 170 180 190 200
TLVFTVDMPI PGARYRDAHS GMSGPYAGLR RFLQAFTHPH WAWNVGIMGR
210 220 230 240 250
PHDLGNVSTY LEKKIALDDY VGWLGANFDP SIGWHDLQWI RDFWKGKMIL
260 270 280 290 300
KGILDPEDAR EAVQFGADGI VVSNHGGRQL DGVLSTARAL PAIAEAVKND
310 320 330 340 350
LVILADSGVR SGLDVVRMIA QGADAVMIGR AFVYALAAAG EKGVAHLLDL
360 370 380
FANEMRVAMT LTGAQTLKEI TCESLVNTDA FKQ
Length:383
Mass (Da):41,985
Last modified:February 5, 2008 - v1
Checksum:i8D5A792088C79878
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM260525 Genomic DNA. Translation: CAK00766.1.
RefSeqiWP_012230738.1. NC_010161.1.

Genome annotation databases

KEGGibtr:BT_0300.
PATRICi20548332. VBIBarTri113218_0327.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM260525 Genomic DNA. Translation: CAK00766.1.
RefSeqiWP_012230738.1. NC_010161.1.

3D structure databases

ProteinModelPortaliA9IN89.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi382640.Btr_0300.

Proteomic databases

PRIDEiA9IN89.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGibtr:BT_0300.
PATRICi20548332. VBIBarTri113218_0327.

Phylogenomic databases

eggNOGiENOG4105DMF. Bacteria.
COG1304. LUCA.
KOiK00101.
OMAiTLKRPMW.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01559. L_lact_dehydr. 1 hit.
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...

Entry informationi

Entry nameiLLDD_BART1
AccessioniPrimary (citable) accession number: A9IN89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 5, 2008
Last modified: November 2, 2016
This is version 60 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

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 one 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.