Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

L-lactate dehydrogenase A chain

Gene

ldha

Organism
Squalus acanthias (Spiny dogfish)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathway:ipyruvate 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 B chain (ldhb), L-lactate dehydrogenase A chain (ldha)
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 sitei100 – 1001NAD1 Publication
Binding sitei107 – 1071SubstrateBy similarity
Binding sitei139 – 1391NAD or substrateBy similarity
Binding sitei170 – 1701Substrate
Active sitei194 – 1941Proton acceptor
Binding sitei249 – 2491SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 5829NAD1 PublicationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

SABIO-RKP00341.
UniPathwayiUPA00554; UER00611.

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenase A chain (EC:1.1.1.27)
Short name:
LDH-A
Alternative name(s):
LDH-M
Gene namesi
Name:ldha
OrganismiSqualus acanthias (Spiny dogfish)
Taxonomic identifieri7797 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiSqualimorphiiSqualiformesSqualidaeSqualus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 333332L-lactate dehydrogenase A chainPRO_0000168455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP00341.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
333
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 85Combined sources
Beta strandi21 – 277Combined sources
Helixi31 – 4111Combined sources
Turni42 – 443Combined sources
Beta strandi47 – 526Combined sources
Helixi56 – 6813Combined sources
Helixi69 – 724Combined sources
Beta strandi78 – 836Combined sources
Helixi84 – 874Combined sources
Beta strandi91 – 955Combined sources
Helixi107 – 12822Combined sources
Beta strandi133 – 1364Combined sources
Beta strandi138 – 1403Combined sources
Helixi141 – 15212Combined sources
Helixi156 – 1583Combined sources
Beta strandi159 – 1613Combined sources
Helixi165 – 17915Combined sources
Turni183 – 1853Combined sources
Beta strandi188 – 1903Combined sources
Beta strandi192 – 1954Combined sources
Helixi202 – 2043Combined sources
Helixi215 – 2184Combined sources
Beta strandi223 – 2286Combined sources
Helixi230 – 24617Combined sources
Helixi251 – 26515Combined sources
Beta strandi270 – 2778Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi289 – 2979Combined sources
Beta strandi300 – 3045Combined sources
Helixi311 – 32717Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LDMX-ray2.10A2-333[»]
3LDHX-ray3.00A4-333[»]
6LDHX-ray2.00A2-333[»]
8LDHX-ray2.80A2-333[»]
ProteinModelPortaliP00341.
SMRiP00341. Positions 2-333.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00341.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG000462.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog.
InterProiIPR001557. L-lactate/malate_DH.
IPR011304. L-lactate_DH.
IPR018177. L-lactate_DH_AS.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
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.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00341-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLKDKLIG HLATSQEPRS YNKITVVGVG AVGMACAISI LMKDLADEVA
60 70 80 90 100
LVDVMEDKLK GEMMDLQHGS LFLHTAKIVS GKDYSVSAGS KLVVITAGAR
110 120 130 140 150
QQEGESRLNL VQRNVNIFKF IIPDIVKHSP DCIILVVSNP VDVLTYVAWK
160 170 180 190 200
LSGLPMHRII GSGCNLDSAR FRYLMGERLG VHSSSCHGWV IGEHGDSSVP
210 220 230 240 250
VWSGMNVAGV SLKELHPELG TDKDKENWKK LHKDVVDSAY EVIKLKGYTS
260 270 280 290 300
WAIGLSVADL AETIMKNLCR VHPVSTMVKD FYGIKNDVFL SLPCVLDNHG
310 320 330
ISNIVKMKLK PDEEQQLQKS ATTLWDIQKD LKF
Length:333
Mass (Da):36,695
Last modified:January 23, 2007 - v4
Checksum:i20C3B5F84B6C0117
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241D → N AA sequence (PubMed:838743).Curated
Sequence conflicti184 – 1841S → C AA sequence (PubMed:838743).Curated
Sequence conflicti198 – 2003SVP → VPS AA sequence (PubMed:838743).Curated
Sequence conflicti206 – 2116NVAGVS → WNA AA sequence (PubMed:838743).Curated
Sequence conflicti222 – 2221D → N AA sequence (PubMed:838743).Curated
Sequence conflicti226 – 2272EN → QD AA sequence (PubMed:838743).Curated
Sequence conflicti286 – 2872ND → DN AA sequence (PubMed:838743).Curated
Sequence conflicti297 – 2982DN → ND AA sequence (PubMed:838743).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38893 mRNA. Translation: AAA91038.1.
PIRiA00350. DEDFLM.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38893 mRNA. Translation: AAA91038.1.
PIRiA00350. DEDFLM.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LDMX-ray2.10A2-333[»]
3LDHX-ray3.00A4-333[»]
6LDHX-ray2.00A2-333[»]
8LDHX-ray2.80A2-333[»]
ProteinModelPortaliP00341.
SMRiP00341. Positions 2-333.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP00341.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG000462.

Enzyme and pathway databases

UniPathwayiUPA00554; UER00611.
SABIO-RKP00341.

Miscellaneous databases

EvolutionaryTraceiP00341.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog.
InterProiIPR001557. L-lactate/malate_DH.
IPR011304. L-lactate_DH.
IPR018177. L-lactate_DH_AS.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
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.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The cDNA sequence of the lactate dehydrogenase-A of the spiny dogfish (Squalus acanthias): corrections to the amino acid sequence and an analysis of the phylogeny of vertebrate lactate dehydrogenases."
    Stock D.W., Powers D.A.
    Mol. Mar. Biol. Biotechnol. 4:284-294(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  2. "Amino acid sequence of dogfish muscle lactate dehydrogenase."
    Taylor S.S.
    J. Biol. Chem. 252:1799-1806(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-333.
  3. "Atomic co-ordinates for dogfish M4 apo-lactate dehydrogenase."
    Adams M.J., Ford G.C., Liljas A., Rossmann M.G.
    Biochem. Biophys. Res. Commun. 53:46-51(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  5. "Refined crystal structure of dogfish M4 apo-lactate dehydrogenase."
    Abad-Zapatero C., Griffith J.P., Sussman J.L., Rossmann M.G.
    J. Mol. Biol. 198:445-467(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG.

Entry informationi

Entry nameiLDHA_SQUAC
AccessioniPrimary (citable) accession number: P00341
Secondary accession number(s): Q92114
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 115 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.