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Protein

Nicotinate dehydrogenase FAD-subunit

Gene

ndhF

Organism
Eubacterium barkeri (Clostridium barkeri)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydroxylation of nicotinate to 6-hydroxynicotinate. Also active against 2-pyrazinecarboxylic acid, but inactive against other nicotinate analogs.1 Publication

Catalytic activityi

Nicotinate + H2O + NADP+ = 6-hydroxynicotinate + NADPH.1 Publication

Cofactori

FAD2 PublicationsNote: Binds 1 FAD per subunit.2 Publications

Enzyme regulationi

Reversibly inactivated by selenide and sulfide. Not inhibited by cyanide.1 Publication

pH dependencei

Most stable at pH 8.0. Unstable at acidic pH values.1 Publication

Pathwayi: nicotinate degradation

This protein is involved in step 1 of the subpathway that synthesizes 6-hydroxynicotinate from nicotinate.1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Nicotinate dehydrogenase large molybdopterin subunit (ndhL), Nicotinate dehydrogenase small FeS subunit (ndhS), Nicotinate dehydrogenase medium molybdopterin subunit (ndhM), Nicotinate dehydrogenase FAD-subunit (ndhF)
This subpathway is part of the pathway nicotinate degradation, which is itself part of Cofactor degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 6-hydroxynicotinate from nicotinate, the pathway nicotinate degradation and in Cofactor degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei101FAD; via amide nitrogen1 Publication1
Binding sitei123FAD1 Publication1
Binding sitei160FAD1 Publication1
Binding sitei169FAD; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei187FAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi29 – 36FAD1 Publication8
Nucleotide bindingi110 – 114FAD1 Publication5

GO - Molecular functioni

GO - Biological processi

  • cofactor catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11707.
UniPathwayiUPA01010; UER01011.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinate dehydrogenase FAD-subunitImported (EC:1.17.1.5)
Short name:
NDH1 Publication
Alternative name(s):
Nicotinic acid hydroxylase FAD-subunit1 Publication
Short name:
NAH1 Publication
Gene namesi
Name:ndhF
OrganismiEubacterium barkeri (Clostridium barkeri)
Taxonomic identifieri1528 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesEubacteriaceaeEubacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004042451 – 296Nicotinate dehydrogenase FAD-subunitAdd BLAST296

Interactioni

Subunit structurei

Heterooctamer of NDHM, NDHL, NDHS and NDHF. Dimer of heterotetramers.2 Publications

Protein-protein interaction databases

DIPiDIP-48911N.

Structurei

Secondary structure

1296
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 7Combined sources3
Helixi12 – 21Combined sources10
Turni22 – 24Combined sources3
Beta strandi28 – 32Combined sources5
Helixi36 – 41Combined sources6
Beta strandi48 – 52Combined sources5
Helixi57 – 59Combined sources3
Beta strandi62 – 64Combined sources3
Beta strandi66 – 72Combined sources7
Helixi77 – 82Combined sources6
Helixi84 – 89Combined sources6
Helixi91 – 98Combined sources8
Helixi103 – 108Combined sources6
Helixi111 – 117Combined sources7
Helixi123 – 130Combined sources8
Beta strandi134 – 139Combined sources6
Beta strandi142 – 147Combined sources6
Helixi148 – 153Combined sources6
Beta strandi156 – 162Combined sources7
Beta strandi168 – 175Combined sources8
Beta strandi181 – 188Combined sources8
Beta strandi190 – 194Combined sources5
Beta strandi198 – 208Combined sources11
Turni209 – 211Combined sources3
Beta strandi212 – 221Combined sources10
Beta strandi223 – 226Combined sources4
Helixi231 – 237Combined sources7
Helixi244 – 248Combined sources5
Helixi251 – 261Combined sources11
Turni262 – 264Combined sources3
Helixi268 – 290Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HRDX-ray2.20C/G1-296[»]
ProteinModelPortaliQ0QLF4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ0QLF4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 179FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST179

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK20445.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
[Graphical view]
PfamiPF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
[Graphical view]
SMARTiSM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF55447. SSF55447. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0QLF4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDFEFFAPK TLEEAKGLLH QYKDVPPAII AGGTDLVIEI NDRWEKPDVV
60 70 80 90 100
IDIKKLKELE YIRVEENTIH IGALSTFTQI ENHPFIRSHV RALYKAASQV
110 120 130 140 150
GSPQIRNLGT IGGNLSTSSV AGDGVSAMTT LDATVVLESV RGTRQMKLTD
160 170 180 190 200
FFDGEGFKRR NALEADEIMT EVIIDRPDAH SASAFYKLAK RKSLAISVIG
210 220 230 240 250
GGMAVKVDDA GVCTWASMRG GCIGRYPLHF KQAEEMLVGA PLTMETMEAT
260 270 280 290
LPILHDTVYD MARARPSVLY KKESVQGVFK KLFVDILDQL EGGCNE
Length:296
Mass (Da):32,622
Last modified:September 5, 2006 - v1
Checksum:iB14B447981D8E7FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ310789 Genomic DNA. Translation: ABC88396.1.

Genome annotation databases

KEGGiag:ABC88396.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ310789 Genomic DNA. Translation: ABC88396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HRDX-ray2.20C/G1-296[»]
ProteinModelPortaliQ0QLF4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48911N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:ABC88396.

Phylogenomic databases

KOiK20445.

Enzyme and pathway databases

UniPathwayiUPA01010; UER01011.
BioCyciMetaCyc:MONOMER-11707.

Miscellaneous databases

EvolutionaryTraceiQ0QLF4.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
[Graphical view]
PfamiPF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
[Graphical view]
SMARTiSM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF55447. SSF55447. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNDFS_EUBBA
AccessioniPrimary (citable) accession number: Q0QLF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: September 5, 2006
Last modified: October 5, 2016
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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.