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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi42 – 421Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation1 Publication
Metal bindingi47 – 471Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation1 Publication
Metal bindingi50 – 501Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation1 Publication
Metal bindingi62 – 621Iron-sulfur (2Fe-2S) 1PROSITE-ProRule annotation1 Publication
Metal bindingi101 – 1011Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation1 Publication
Metal bindingi104 – 1041Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation1 Publication
Metal bindingi136 – 1361Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation1 Publication
Metal bindingi138 – 1381Iron-sulfur (2Fe-2S) 2PROSITE-ProRule annotation1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 157157Nicotinate dehydrogenase small FeS subunitPRO_0000404246Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-48912N.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Beta strandi13 – 197Combined sources
Beta strandi21 – 244Combined sources
Helixi25 – 306Combined sources
Beta strandi41 – 477Combined sources
Beta strandi51 – 544Combined sources
Beta strandi57 – 604Combined sources
Helixi61 – 633Combined sources
Helixi66 – 694Combined sources
Beta strandi72 – 754Combined sources
Helixi77 – 793Combined sources
Helixi88 – 969Combined sources
Helixi105 – 11612Combined sources
Helixi124 – 1318Combined sources
Beta strandi137 – 1393Combined sources
Helixi142 – 15716Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ0QLF3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 80772Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Family and domain databases

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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3HRDX-ray2.20D/H1-157[»]
ProteinModelPortaliQ0QLF3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48912N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA01010; UER01011.
BioCyciMetaCyc:MONOMER-11708.

Miscellaneous databases

EvolutionaryTraceiQ0QLF3.

Family and domain databases

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...

Publicationsi

  1. "Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri."
    Alhapel A., Darley D.J., Wagener N., Eckel E., Elsner N., Pierik A.J.
    Proc. Natl. Acad. Sci. U.S.A. 103:12341-12346(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY.
    Strain: ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 10623Imported.
  2. "Properties of the selenium- and molybdenum-containing nicotinic acid hydroxylase from Clostridium barkeri."
    Gladyshev V.N., Khangulov S.V., Stadtman T.C.
    Biochemistry 35:212-223(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
    Strain: ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 106231 Publication.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH WITH FAD; IRON-SULFUR CLUSTERS; NDHM; NDHL AND NDHF, COFACTOR, SUBUNIT.
    Strain: ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 106231 Publication.

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: December 9, 2015
This is version 52 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.