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P00341

- LDHA_SQUAC

UniProt

P00341 - LDHA_SQUAC

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Protein

L-lactate dehydrogenase A chain

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

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001NAD
Binding sitei107 – 1071Substrate By similarity
Binding sitei139 – 1391NAD or substrate By similarity
Binding sitei170 – 1701Substrate
Active sitei194 – 1941Proton acceptor
Binding sitei249 – 2491Substrate By similarity

Regions

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

GO - Molecular functioni

  1. L-lactate dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

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

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
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.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP00341.

Family & Domainsi

Sequence similaritiesi

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

MATLKDKLIG HLATSQEPRS YNKITVVGVG AVGMACAISI LMKDLADEVA    50
LVDVMEDKLK GEMMDLQHGS LFLHTAKIVS GKDYSVSAGS KLVVITAGAR 100
QQEGESRLNL VQRNVNIFKF IIPDIVKHSP DCIILVVSNP VDVLTYVAWK 150
LSGLPMHRII GSGCNLDSAR FRYLMGERLG VHSSSCHGWV IGEHGDSSVP 200
VWSGMNVAGV SLKELHPELG TDKDKENWKK LHKDVVDSAY EVIKLKGYTS 250
WAIGLSVADL AETIMKNLCR VHPVSTMVKD FYGIKNDVFL SLPCVLDNHG 300
ISNIVKMKLK PDEEQQLQKS ATTLWDIQKD LKF 333
Length:333
Mass (Da):36,695
Last modified:January 23, 2007 - v4
Checksum:i20C3B5F84B6C0117
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241D → N AA sequence 1 Publication
Sequence conflicti184 – 1841S → C AA sequence 1 Publication
Sequence conflicti198 – 2003SVP → VPS AA sequence 1 Publication
Sequence conflicti206 – 2116NVAGVS → WNA AA sequence 1 Publication
Sequence conflicti222 – 2221D → N AA sequence 1 Publication
Sequence conflicti226 – 2272EN → QD AA sequence 1 Publication
Sequence conflicti286 – 2872ND → DN AA sequence 1 Publication
Sequence conflicti297 – 2982DN → ND AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U38893 mRNA. Translation: AAA91038.1.
PIRiA00350. DEDFLM.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U38893 mRNA. Translation: AAA91038.1 .
PIRi A00350. DEDFLM.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LDM X-ray 2.10 A 2-333 [» ]
3LDH X-ray 3.00 A 4-333 [» ]
6LDH X-ray 2.00 A 2-333 [» ]
8LDH X-ray 2.80 A 2-333 [» ]
ProteinModelPortali P00341.
SMRi P00341. Positions 2-333.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P00341.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG000462.

Enzyme and pathway databases

UniPathwayi UPA00554 ; UER00611 .
SABIO-RK P00341.

Miscellaneous databases

EvolutionaryTracei P00341.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPi MF_00488. Lactate_dehydrog.
InterProi IPR001557. 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 ]
PANTHERi PTHR11540. PTHR11540. 1 hit.
Pfami PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
PRINTSi PR00086. LLDHDRGNASE.
SUPFAMi SSF56327. SSF56327. 1 hit.
TIGRFAMsi TIGR01771. L-LDH-NAD. 1 hit.
PROSITEi PS00064. L_LDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 110 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

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