Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nicotinate dehydrogenase small FeS subunit

Gene

ndhS

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

[2Fe-2S] cluster2 PublicationsNote: Binds 2 [2Fe-2S] clusters 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
Metal bindingi42Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation1 Publication1
Metal bindingi47Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation1 Publication1
Metal bindingi50Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation1 Publication1
Metal bindingi62Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation1 Publication1
Metal bindingi101Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation1 Publication1
Metal bindingi104Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation1 Publication1
Metal bindingi136Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation1 Publication1
Metal bindingi138Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11708.
UniPathwayiUPA01010; UER01011.

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004042461 – 157Nicotinate dehydrogenase small FeS subunitAdd BLAST157

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-48912N.

Structurei

Secondary structure

1157
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Beta strandi13 – 19Combined sources7
Beta strandi21 – 24Combined sources4
Helixi25 – 30Combined sources6
Beta strandi41 – 47Combined sources7
Beta strandi51 – 54Combined sources4
Beta strandi57 – 60Combined sources4
Helixi61 – 63Combined sources3
Helixi66 – 69Combined sources4
Beta strandi72 – 75Combined sources4
Helixi77 – 79Combined sources3
Helixi88 – 96Combined sources9
Helixi105 – 116Combined sources12
Helixi124 – 131Combined sources8
Beta strandi137 – 139Combined sources3
Helixi142 – 157Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HRDX-ray2.20D/H1-157[»]
ProteinModelPortaliQ0QLF3.
SMRiQ0QLF3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ0QLF3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 802Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST77

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK20446.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0QLF3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKITINLNL NGEARSIVTE PNKRLLDLLR EDFGLTSVKE GCSEGECGAC
60 70 80 90 100
TVIFNGDPVT TCCMLAGQAD ESTIITLEGV AEDGKPSLLQ QCFLEAGAVQ
110 120 130 140 150
CGYCTPGMIL TAKALLDKNP DPTDEEITVA MSGNLCRCTG YIKIHAAVRY

AVERCAN
Length:157
Mass (Da):16,766
Last modified:September 5, 2006 - v1
Checksum:i4750940AB90ED093
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ310789 Genomic DNA. Translation: ABC88397.1.

Genome annotation databases

KEGGiag:ABC88397.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ310789 Genomic DNA. Translation: ABC88397.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HRDX-ray2.20D/H1-157[»]
ProteinModelPortaliQ0QLF3.
SMRiQ0QLF3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48912N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:ABC88397.

Phylogenomic databases

KOiK20446.

Enzyme and pathway databases

UniPathwayiUPA01010; UER01011.
BioCyciMetaCyc:MONOMER-11708.

Miscellaneous databases

EvolutionaryTraceiQ0QLF3.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNDSFS_EUBBA
AccessioniPrimary (citable) accession number: Q0QLF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: September 5, 2006
Last modified: November 2, 2016
This is version 55 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.