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Protein

L-lactate dehydrogenase

Gene
N/A
Organism
Botryococcus braunii (Green alga)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-lactate + NAD+ = pyruvate + NADH.

Pathwayi: pyruvate fermentation to lactate

This protein is involved in step 1 of the subpathway that synthesizes (S)-lactate from pyruvate.
Proteins known to be involved in this subpathway in this organism are:
  1. L-lactate dehydrogenase
This subpathway is part of the pathway pyruvate fermentation to lactate, which is itself part of Fermentation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-lactate from pyruvate, the pathway pyruvate fermentation to lactate and in Fermentation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891SubstrateBy similarity
Binding sitei121 – 1211NAD or substrateBy similarity
Binding sitei152 – 1521SubstrateBy similarity
Active sitei172 – 1721Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 396NADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17304.
UniPathwayiUPA00554; UER00611.

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenase (EC:1.1.1.27)
Short name:
LDH
OrganismiBotryococcus braunii (Green alga)
Taxonomic identifieri38881 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaTrebouxiophyceaeTrebouxiophyceae incertae sedisBotryococcaceaeBotryococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316L-lactate dehydrogenasePRO_0000168492Add
BLAST

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP93052.
SMRiP93052. Positions 3-309.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. LDH family.Curated

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00487. Malate_dehydrog_3.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR011275. Malate_DH_type3.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01763. MalateDH_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

P93052-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARKKYALIG AGNIGGTLAH LAALKGLGDI VLFDVVEGVP QGKALDLSQC
60 70 80 90 100
GPVEGFDANI KGSNDYADIA GADVIIVTAG VARKPGMSRD DLLGINLKVM
110 120 130 140 150
KAVGEGIRDN APDAFVICIT NPLDAMVWAL REFSGLPANK VVGMAGVLDS
160 170 180 190 200
GRFSHFLAEE FGVSVNSVLG GHGDNMVPVL EYSTVSGIPV SELIEMGFST
210 220 230 240 250
KEKVDEIIKR TRGGGGEIVA LLKTGSAYYA PATSGIAMAE AYLYDQKRIL
260 270 280 290 300
PAAAHLSGEY GIDNLYVGVP VVIGANGVEK VVEVKLSDEA KANLQVSVDA
310
VKELLVACKG IDESLA
Length:316
Mass (Da):32,875
Last modified:May 1, 1997 - v1
Checksum:i436AC40FB7A07A19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61Y → I AA sequence (PubMed:7649295).Curated
Sequence conflicti16 – 161G → W AA sequence (PubMed:7649295).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80676 Genomic DNA. Translation: AAB38970.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80676 Genomic DNA. Translation: AAB38970.1.

3D structure databases

ProteinModelPortaliP93052.
SMRiP93052. Positions 3-309.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00554; UER00611.
BioCyciMetaCyc:MONOMER-17304.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00487. Malate_dehydrog_3.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR011275. Malate_DH_type3.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01763. MalateDH_bact. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Malate dehydrogenase gene from Botryococcus braunii."
    Vioque J., Sirakova T., Kolattukudy P.E.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Race A.
  2. "Solubilization and purification of aldehyde-generating fatty acyl-CoA reductase from green alga Botryococcus braunii."
    Wang X., Kolattukudy P.E.
    FEBS Lett. 370:15-18(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-27.
  3. "Massive sequence comparisons as a help in annotating genomic sequences."
    Louis A., Ollivier E., Aude J.-C., Risler J.-L.
    Genome Res. 11:1296-1303(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROBABLE FUNCTION.

Entry informationi

Entry nameiLDH_BOTBR
AccessioniPrimary (citable) accession number: P93052
Secondary accession number(s): Q7M1E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: May 1, 1997
Last modified: March 16, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

Was originally (Ref. 1) thought to be a malate dehydrogenase or an NADH-dependent acyl-CoA reductase.1 Publication

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.