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Protein

L-lactate dehydrogenase

Gene

lldD

Organism
Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377)
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:A1S_0069
OrganismiAcinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377)
Taxonomic identifieri400667 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

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_00003834071 – 383L-lactate dehydrogenaseAdd BLAST383

Structurei

3D structure databases

ProteinModelPortaliA3M0X0
SMRiA3M0X0
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
OrthoDBiPOG091H00L7

Family and domain databases

CDDicd02809 alpha_hydroxyacid_oxid_FMN, 1 hit
Gene3Di3.20.20.701 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.

A3M0X0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIISSGNDYR AAAQRRLPPF LFHYIDGGAY AEYTLKRNVQ DLSEIALRQR
60 70 80 90 100
VLNDMSALSL ETKLFNETLS MPVALAPVGL TGMYARRGEV QAAMAADKKG
110 120 130 140 150
IPFTLSTVSV CPIEEVAPAI NRPMWFQLYV LRDRGFMRNA LERAKAAGCS
160 170 180 190 200
TLVFTVDMPV PGARYRDAHS GMSGPNAAMR RYMQSVFHPH WSWNVGLMGR
210 220 230 240 250
PHDLGNISKY LGKPTGLEDY IGWLGSNFDP SISWKDLEWI REFWDGPMVI
260 270 280 290 300
KGILDPEDAK DAVRFGADGI VVSNHGGRQL DGVMSSARAL PAIADAVKGD
310 320 330 340 350
LAILADSGIR NGLDVVRMLA LGADTVLLGR AFVYALAAAG GQGVSNLLDL
360 370 380
IDKEMRVAMT LTGAKSISDI NADCLVQAIK QGL
Length:383
Mass (Da):41,648
Last modified:September 2, 2008 - v2
Checksum:i5F274546464F785C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000521 Genomic DNA Translation: ABO10564.2

Genome annotation databases

EnsemblBacteriaiABO10564; ABO10564; A1S_0069
KEGGiacb:A1S_0069

Similar proteinsi

Entry informationi

Entry nameiLLDD_ACIBT
AccessioniPrimary (citable) accession number: A3M0X0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 2, 2008
Last modified: December 20, 2017
This is version 64 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program