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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei101 – 1011FAD; via amide nitrogen1 Publication
Binding sitei123 – 1231FAD1 Publication
Binding sitei160 – 1601FAD1 Publication
Binding sitei169 – 1691FAD; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei187 – 1871FAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 368FAD1 Publication
Nucleotide bindingi110 – 1145FAD1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296Nicotinate dehydrogenase FAD-subunitPRO_0000404245Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-48911N.

Structurei

Secondary structure

1
296
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Helixi12 – 2110Combined sources
Turni22 – 243Combined sources
Beta strandi28 – 325Combined sources
Helixi36 – 416Combined sources
Beta strandi48 – 525Combined sources
Helixi57 – 593Combined sources
Beta strandi62 – 643Combined sources
Beta strandi66 – 727Combined sources
Helixi77 – 826Combined sources
Helixi84 – 896Combined sources
Helixi91 – 988Combined sources
Helixi103 – 1086Combined sources
Helixi111 – 1177Combined sources
Helixi123 – 1308Combined sources
Beta strandi134 – 1396Combined sources
Beta strandi142 – 1476Combined sources
Helixi148 – 1536Combined sources
Beta strandi156 – 1627Combined sources
Beta strandi168 – 1758Combined sources
Beta strandi181 – 1888Combined sources
Beta strandi190 – 1945Combined sources
Beta strandi198 – 20811Combined sources
Turni209 – 2113Combined sources
Beta strandi212 – 22110Combined sources
Beta strandi223 – 2264Combined sources
Helixi231 – 2377Combined sources
Helixi244 – 2485Combined sources
Helixi251 – 26111Combined sources
Turni262 – 2643Combined sources
Helixi268 – 29023Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ0QLF4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 179179FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

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
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.

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: September 7, 2016
This is version 49 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.