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Protein

L-lactate dehydrogenase

Gene

lldD

Organism
Yersinia pseudotuberculosis serotype IB (strain PB1/+)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionOxidoreductase
LigandFlavoprotein, FMN

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenaseUniRule annotation (EC:1.1.-.-UniRule annotation)
Gene namesi
Name:lldDUniRule annotation
Ordered Locus Names:YPTS_1692
OrganismiYersinia pseudotuberculosis serotype IB (strain PB1/+)
Taxonomic identifieri502801 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeYersinia

Subcellular locationi

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

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003834561 – 381L-lactate dehydrogenaseAdd BLAST381

Structurei

3D structure databases

ProteinModelPortaliB2JZQ1
SMRiB2JZQ1
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

Phylogenomic databases

HOGENOMiHOG000217464
KOiK00101
OMAiMQLYIYK

Family and domain databases

CDDicd02809 alpha_hydroxyacid_oxid_FMN, 1 hit
Gene3Di3.20.20.70, 1 hit
HAMAPiMF_01559 L_lact_dehydr, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR012133 Alpha-hydoxy_acid_DH_FMN
IPR000262 FMN-dep_DH
IPR037396 FMN_HAD
IPR008259 FMN_hydac_DH_AS
IPR020920 LldD
PfamiView protein in Pfam
PF01070 FMN_dh, 1 hit
PIRSFiPIRSF000138 Al-hdrx_acd_dh, 1 hit
PROSITEiView protein in PROSITE
PS00557 FMN_HYDROXY_ACID_DH_1, 1 hit
PS51349 FMN_HYDROXY_ACID_DH_2, 1 hit

Sequencei

Sequence statusi: Complete.

B2JZQ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIISASTDYR AAAQRKLPPF LFHYIDGGAY NEQTLRRNTA DLADIALRQR
60 70 80 90 100
VLKNMSELSL ETQLFGETQA MPVVLGPVGL SGMYARRGEV QAARAADKKG
110 120 130 140 150
IPFTLSTLSV CPIEEVAPAI ARPMWFQLYV LKDRGFMRNA LTRAQAAGVK
160 170 180 190 200
TLVFTVDMPV PGARYRDAHS GMSGPNAAAR RLLQAIAHPQ WAWDVGLNGK
210 220 230 240 250
PHDLGNISAY LGKPTTLEDY MGWIATNFDP SISWKDLEWV REFWQGPMII
260 270 280 290 300
KGILDPEDAK DAVKFGADGI VVSNHGGRQL DGVLSTARAL PAIADAVKGD
310 320 330 340 350
ITILADSGIR TGLDVVRMIA LGADSVLLGR AFVYALATAG EAGVINLLTL
360 370 380
IEQEMRVAMT LTGAKRIADI NRDSLAVSER G
Length:381
Mass (Da):41,259
Last modified:June 10, 2008 - v1
Checksum:iECC708A08D5E4634
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001048 Genomic DNA Translation: ACC88661.1
RefSeqiWP_002211919.1, NZ_CP009780.1

Genome annotation databases

EnsemblBacteriaiACC88661; ACC88661; YPTS_1692
KEGGiypb:YPTS_1692
PATRICifig|502801.10.peg.1067

Similar proteinsi

Entry informationi

Entry nameiLLDD_YERPB
AccessioniPrimary (citable) accession number: B2JZQ1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 10, 2008
Last modified: December 20, 2017
This is version 54 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health