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P13491

- LDHA_RABIT

UniProt

P13491 - LDHA_RABIT

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Protein

L-lactate dehydrogenase A chain

Gene
LDHA
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991NAD
Binding sitei106 – 1061Substrate
Binding sitei138 – 1381NAD or substrate
Binding sitei169 – 1691Substrate
Active sitei193 – 1931Proton acceptor1 Publication
Binding sitei248 – 2481Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 5729NADUniRule annotationAdd
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-RKP13491.
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 muscle subunit
Short name:
LDH-M
Gene namesi
Name:LDHA
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

Cytoplasm UniRule annotation

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 By similarity
Chaini2 – 332331L-lactate dehydrogenase A chainUniRule annotationPRO_0000168418Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei5 – 51N6-acetyllysine; alternate By similarity
Modified residuei5 – 51N6-succinyllysine; alternate By similarity
Modified residuei14 – 141N6-acetyllysine By similarity
Modified residuei57 – 571N6-acetyllysine By similarity
Modified residuei81 – 811N6-acetyllysine By similarity
Modified residuei118 – 1181N6-acetyllysine; alternate By similarity
Modified residuei118 – 1181N6-succinyllysine; alternate By similarity
Modified residuei126 – 1261N6-acetyllysine By similarity
Modified residuei224 – 2241N6-acetyllysine By similarity
Modified residuei232 – 2321N6-acetyllysine By similarity
Modified residuei239 – 2391Phosphotyrosine By similarity
Modified residuei243 – 2431N6-acetyllysine By similarity
Modified residuei318 – 3181N6-acetyllysine; alternate By similarity
Modified residuei318 – 3181N6-succinyllysine; alternate By similarity

Post-translational modificationi

ISGylated By similarity.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP13491.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

IntActiP13491. 1 interaction.
STRINGi9986.ENSOCUP00000021667.

Structurei

Secondary structure

1
332
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 85
Beta strandi9 – 113
Beta strandi20 – 267
Helixi30 – 4112
Beta strandi46 – 516
Helixi55 – 6612
Helixi67 – 715
Beta strandi76 – 794
Helixi83 – 864
Beta strandi90 – 945
Helixi109 – 12719
Beta strandi132 – 1354
Beta strandi137 – 1393
Helixi140 – 15112
Helixi155 – 1573
Beta strandi158 – 1603
Helixi164 – 17815
Helixi182 – 1843
Beta strandi189 – 1946
Helixi201 – 2033
Helixi211 – 2144
Turni216 – 2194
Helixi228 – 24518
Helixi250 – 26415
Beta strandi269 – 2768
Beta strandi288 – 2969
Beta strandi299 – 3046
Helixi310 – 32718

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H3FX-ray2.38A/B/C/D/E/F/G/H2-332[»]
4I8XX-ray2.23A/B/C/D/E/F/G/H2-332[»]
4I9HX-ray2.17A/B/C/D/E/F/G/H2-332[»]
4I9NX-ray2.35A/B/C/D/E/F/G/H2-332[»]
4I9UX-ray2.50A/B/C/D/E/F/G/H2-332[»]
ProteinModelPortaliP13491.
SMRiP13491. Positions 2-332.

Miscellaneous databases

EvolutionaryTraceiP13491.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0039.
HOGENOMiHOG000213793.
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.

P13491-1 [UniParc]FASTAAdd to Basket

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MAALKDQLIH NLLKEEHVPQ NKITVVGVGA VGMACAISIL MKDLADELAL    50
VDVMEDKLKG EMMDLQHGSL FLRTPKIVSG KDYSVTANSK LVIITAGARQ 100
QEGESRLNLV QRNVNIFKFI IPNVVKYSPH CKLLVVSNPV DILTYVAWKI 150
SGFPKNRVIG SGCNLDSARF RYLMGERLGV HALSCHGWIL GEHGDSSVPV 200
WSGMNVAGVS LKTLHPELGT DADKEQWKQV HKQVVDSAYE VIKLKGYTTW 250
AIGLSVADLA ESIMKNLRRV HPISTMLKGL YGIKEDVFLS VPCVLGQNGI 300
SDVVKVTLTS EEEAHLKKSA DTLWGIQKEL QF 332
Length:332
Mass (Da):36,565
Last modified:January 23, 2007 - v3
Checksum:i84E86C2E7D018EF7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M22585 mRNA. Translation: AAA31382.1.
PIRiA32957.
RefSeqiNP_001075746.1. NM_001082277.1.
UniGeneiOcu.1108.

Genome annotation databases

GeneIDi100009107.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M22585 mRNA. Translation: AAA31382.1 .
PIRi A32957.
RefSeqi NP_001075746.1. NM_001082277.1.
UniGenei Ocu.1108.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3H3F X-ray 2.38 A/B/C/D/E/F/G/H 2-332 [» ]
4I8X X-ray 2.23 A/B/C/D/E/F/G/H 2-332 [» ]
4I9H X-ray 2.17 A/B/C/D/E/F/G/H 2-332 [» ]
4I9N X-ray 2.35 A/B/C/D/E/F/G/H 2-332 [» ]
4I9U X-ray 2.50 A/B/C/D/E/F/G/H 2-332 [» ]
ProteinModelPortali P13491.
SMRi P13491. Positions 2-332.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P13491. 1 interaction.
STRINGi 9986.ENSOCUP00000021667.

Proteomic databases

PRIDEi P13491.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009107.

Organism-specific databases

CTDi 3939.

Phylogenomic databases

eggNOGi COG0039.
HOGENOMi HOG000213793.
HOVERGENi HBG000462.

Enzyme and pathway databases

UniPathwayi UPA00554 ; UER00611 .
SABIO-RK P13491.

Miscellaneous databases

EvolutionaryTracei P13491.

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. "Characterization of rabbit lactate dehydrogenase-M and lactate dehydrogenase-H cDNAs. Control of lactate dehydrogenase expression in rabbit muscle."
    Sass C., Briand M., Benslimane S., Renaud M., Briand Y.
    J. Biol. Chem. 264:4076-4081(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Modeling of isotope effects on binding oxamate to lactic dehydrogenase."
    Swiderek K., Panczakiewicz A., Bujacz A., Bujacz G., Paneth P.
    J. Phys. Chem. B 113:12782-12789(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-332 IN COMPLEX WITH NADH AMD INHIBITOR, SUBUNIT, ACTIVE SITE, SUBSTRATE-BINDING SITES, NAD-BINDING SITES.

Entry informationi

Entry nameiLDHA_RABIT
AccessioniPrimary (citable) accession number: P13491
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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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