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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.

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 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)DescriptionActionsGraphical viewLength
Binding sitei100NAD1 Publication1
Binding sitei107SubstrateBy similarity1
Binding sitei139NAD or substrateBy similarity1
Binding sitei170Substrate1
Active sitei194Proton acceptor1
Binding sitei249SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi30 – 58NAD1 PublicationAdd BLAST29

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001684552 – 333L-lactate dehydrogenase A chainAdd BLAST332

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP00341.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 8Combined sources5
Beta strandi21 – 27Combined sources7
Helixi31 – 41Combined sources11
Turni42 – 44Combined sources3
Beta strandi47 – 52Combined sources6
Helixi56 – 68Combined sources13
Helixi69 – 72Combined sources4
Beta strandi78 – 83Combined sources6
Helixi84 – 87Combined sources4
Beta strandi91 – 95Combined sources5
Helixi107 – 128Combined sources22
Beta strandi133 – 136Combined sources4
Beta strandi138 – 140Combined sources3
Helixi141 – 152Combined sources12
Helixi156 – 158Combined sources3
Beta strandi159 – 161Combined sources3
Helixi165 – 179Combined sources15
Turni183 – 185Combined sources3
Beta strandi188 – 190Combined sources3
Beta strandi192 – 195Combined sources4
Helixi202 – 204Combined sources3
Helixi215 – 218Combined sources4
Beta strandi223 – 228Combined sources6
Helixi230 – 246Combined sources17
Helixi251 – 265Combined sources15
Beta strandi270 – 277Combined sources8
Beta strandi281 – 283Combined sources3
Beta strandi289 – 297Combined sources9
Beta strandi300 – 304Combined sources5
Helixi311 – 327Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LDMX-ray2.10A2-333[»]
3LDHX-ray3.00A4-333[»]
6LDHX-ray2.00A2-333[»]
8LDHX-ray2.80A2-333[»]
ProteinModelPortaliP00341.
SMRiP00341.
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. 1 hit.
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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. 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)DescriptionActionsGraphical viewLength
Sequence conflicti124D → N AA sequence (PubMed:838743).Curated1
Sequence conflicti184S → C AA sequence (PubMed:838743).Curated1
Sequence conflicti198 – 200SVP → VPS AA sequence (PubMed:838743).Curated3
Sequence conflicti206 – 211NVAGVS → WNA AA sequence (PubMed:838743).Curated6
Sequence conflicti222D → N AA sequence (PubMed:838743).Curated1
Sequence conflicti226 – 227EN → QD AA sequence (PubMed:838743).Curated2
Sequence conflicti286 – 287ND → DN AA sequence (PubMed:838743).Curated2
Sequence conflicti297 – 298DN → ND AA sequence (PubMed:838743).Curated2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LDMX-ray2.10A2-333[»]
3LDHX-ray3.00A4-333[»]
6LDHX-ray2.00A2-333[»]
8LDHX-ray2.80A2-333[»]
ProteinModelPortaliP00341.
SMRiP00341.
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. 1 hit.
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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 122 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

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.