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Protein

L-lactate dehydrogenase

Gene

lldD

Organism
Yersinia pestis bv. Antiqua (strain Angola)
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

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:YpAngola_A1696
OrganismiYersinia pestis bv. Antiqua (strain Angola)
Taxonomic identifieri349746 [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_00003834551 – 381L-lactate dehydrogenaseAdd BLAST381

Structurei

3D structure databases

ProteinModelPortaliA9R623.
SMRiA9R623.
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.
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.

A9R623-1 [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:February 5, 2008 - v1
Checksum:iECC708A08D5E4634
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000901 Genomic DNA. Translation: ABX85222.1.
RefSeqiWP_002211919.1. NZ_CP009935.1.

Genome annotation databases

EnsemblBacteriaiABX85222; ABX85222; YpAngola_A1696.
KEGGiypg:YpAngola_A1696.
PATRICifig|349746.12.peg.2667.

Similar proteinsi

Entry informationi

Entry nameiLLDD_YERPG
AccessioniPrimary (citable) accession number: A9R623
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 5, 2008
Last modified: August 30, 2017
This is version 59 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families