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Protein

Dihydrolipoyl dehydrogenase

Gene

m-6

Organism
Neisseria meningitidis
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.UniRule annotation

Cofactori

FADUniRule annotationNote: Binds 1 FAD per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551FAD; via amide nitrogenCombined sources
Binding sitei165 – 1651FADCombined sources
Binding sitei246 – 2461FADCombined sources
Binding sitei435 – 4351FADCombined sources
Binding sitei443 – 4431FAD; via amide nitrogenCombined sources
Binding sitei567 – 5671FAD; via carbonyl oxygenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi127 – 1282FADCombined sources
Nucleotide bindingi147 – 1482FADCombined sources
Nucleotide bindingi160 – 1612FADCombined sources
Nucleotide bindingi227 – 2282FADCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Ligandi

FADUniRule annotationCombined sources, Flavoprotein, NADUniRule annotation, Nucleotide-bindingCombined sources

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenaseUniRule annotation (EC:1.8.1.4UniRule annotation)
Gene namesi
Name:m-6Imported
OrganismiNeisseria meningitidisImported
Taxonomic identifieri487 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi156 ↔ 161Combined sources

Proteomic databases

PaxDbiQ51225.

Interactioni

Protein-protein interaction databases

STRINGi122586.NMB1344.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BHYX-ray4.18A112-593[»]
1OJTX-ray2.75A112-593[»]
ProteinModelPortaliQ51225.
SMRiQ51225. Positions 2-82, 112-593.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ51225.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 7775Lipoyl-bindingInterPro annotationAdd
BLAST

Sequence similaritiesi

Contains lipoyl-binding domain.SAAS annotation

Keywords - Domaini

LipoylSAAS annotation, Redox-active centerUniRule annotation

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q51225-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALVELKVPD IGGHENVDII AVEVNVGDTI AVDDTLITLE TDKATMDVPA
60 70 80 90 100
EVAGVVKEVK VKVGDKISEG GLIVVVEAEG TAAAPKAEAA AAPAQEAPKA
110 120 130 140 150
AAPAPQAAQF GGSADAEYDV VVLGGGPGGY SAAFAAADEG LKVAIVERYK
160 170 180 190 200
TLGGVCLNVG CIPSKALLHN AAVIDEVRHL AANGIKYPEP ELDIDMLRAY
210 220 230 240 250
KDGVVSRLTG GLAGMAKSRK VDVIQGDGQF LDPHHLEVSL TAGDAYEQAA
260 270 280 290 300
PTGEKKIVAF KNCIIAAGSR VTKLPFIPED PRIIDSSGAL ALKEVPGKLL
310 320 330 340 350
IIGGGIIGLE MGTVYSTLGS RLDVVEMMDG LMQGADRDLV KVWQKQNEYR
360 370 380 390 400
FDNIMVNTKT VAVEPKEDGV YVTFEGANAP KEPQRYDAVL VAAGRAPNGK
410 420 430 440 450
LISAEKAGVA VTDRGFIEVD KQMRTNVPHI YAIGDIVGQP MLAHKAVHEG
460 470 480 490 500
HVAAENCAGH KAYFDARVIP GVAYTSPEVA WVGETELSAK ASGRKITKAN
510 520 530 540 550
FPWAASGRAI ANGCDKPFTK LIFDAETGRI IGGGIVGPNG GDMIGEVCLA
560 570 580 590
IEMGCDAADI GKTIHPHPTL GESIGMAAEV ALGTCTDLPP QKKK
Length:594
Mass (Da):61,883
Last modified:November 1, 1996 - v1
Checksum:i24823E854A29CA62
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77920 Genomic DNA. Translation: CAA54878.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77920 Genomic DNA. Translation: CAA54878.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BHYX-ray4.18A112-593[»]
1OJTX-ray2.75A112-593[»]
ProteinModelPortaliQ51225.
SMRiQ51225. Positions 2-82, 112-593.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi122586.NMB1344.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Proteomic databases

PaxDbiQ51225.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.

Miscellaneous databases

EvolutionaryTraceiQ51225.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Loeffler M.
    Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: B:4:P1.15Imported.
  2. "Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis."
    Li de la Sierra I., Pernot L., Prange T., Saludjian P., Schiltz M., Fourme R., Padron G.
    J. Mol. Biol. 269:129-141(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 112-593 IN COMPLEX WITH FAD, DISULFIDE BONDS.
  3. "Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values."
    Ramin M., Shepard W., Fourme R., Kahn R.
    Acta Crystallogr. D 55:157-167(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.18 ANGSTROMS) OF 112-593 IN COMPLEX WITH FAD, DISULFIDE BONDS.
  4. "Characterisation of the lpdA gene from Neisseria meningitidis by polymerase chain reaction, restriction fragment length polymorphism and sequencing."
    Silva R., Menendez T., Alonso L.M., Iglesias E., Musacchio A., de Jesus Leal M., Alvarez A., Couizeau E., Martin A., Herrera L.S., Guillen G.
    FEMS Microbiol. Lett. 174:191-199(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: B:4:P1.15Imported.

Entry informationi

Entry nameiQ51225_NEIME
AccessioniPrimary (citable) accession number: Q51225
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: March 16, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.UniRule annotation

Keywords - Technical termi

3D-structureCombined sources

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.