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Q0QLF2 (NDLMS_EUBBA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nicotinate dehydrogenase large molybdopterin subunit

Short name=NDH
EC=1.17.1.5
Alternative name(s):
Nicotinic acid hydroxylase large molybdopterin subunit
Short name=NAH
Gene names
Name:ndhL
OrganismEubacterium barkeri (Clostridium barkeri)
Taxonomic identifier1528 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesEubacteriaceaeEubacterium

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Nicotinate + H2O + NADP+ = 6-hydroxynicotinate + NADPH. Ref.2

Cofactor

Binds 1 hydroxyoxoselanylmolybdenum molybdopterin cytosine dinucleotide per heterotetramer. The cofactor is bound between the ndhL and ndhM subunits. Ref.2 Ref.3

Enzyme regulation

Reversibly inactivated by selenide and sulfide. Not inhibited by cyanide. Ref.2

Pathway

Cofactor degradation; nicotinate degradation; 6-hydroxynicotinate from nicotinate: step 1/1. Ref.1

Subunit structure

Heterooctamer of NDHM, NDHL, NDHS and NDHF. Dimer of heterotetramers. Ref.2 Ref.3

Sequence similarities

Belongs to the xanthine dehydrogenase family.

Biophysicochemical properties

pH dependence:

Most stable at pH 8.0. Unstable at acidic pH values. Ref.2

Ontologies

Keywords
   LigandMetal-binding
Molybdenum
NADP
Selenium
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcofactor catabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nicotinate dehydrogenase activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 425424Nicotinate dehydrogenase large molybdopterin subunit Ref.2
PRO_0000404243

Regions

Region238 – 2403Hydroxyoxoselanylmolybdenum molybdopterin cytosine dinucleotide binding Ref.3

Sites

Binding site2081Hydroxyoxoselanylmolybdenum molybdopterin cytosine dinucleotide Ref.3

Secondary structure

................................................................ 425
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q0QLF2 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: F8270B4ABECD71A5

FASTA42546,488
        10         20         30         40         50         60 
MGKDYQVLGK NKVKVDSLEK VMGTAKFAAD YSFPDMLYAG VFRSTVPHAR IVSLDLSKAR 

        70         80         90        100        110        120 
AIDGVEAVLD YHAIPGKNRF GIIIKDEPCL VDDKVRRYGD AIAVVAAQTP DLVQEALDAI 

       130        140        150        160        170        180 
TIEYEELEGI FTMERALEED SPAIHGDTNI HQVKHLEYGD VDAAFKQCDI VVEDTYSTHR 

       190        200        210        220        230        240 
LTHMFIEPDA GVSYYDNEGM LTVVVSTQNP HYDRGEVAGM LALPNSKVRI IQATTGGGFG 

       250        260        270        280        290        300 
GKLDLSVQCH CALLTYHTKK PVKMVRSREE STTVSSKRHP MTMHCKTGAT KDGRLQAVQV 

       310        320        330        340        350        360 
EMFGDTGAYA SYGPAVITRA TVHCMGPYVV PNVRVDAKFV YTNNPMSGAF RGFGVPQASV 

       370        380        390        400        410        420 
CHEGQMNALA KALGMDPIDI RILNAHQVGA KLATGQVLEN SVGLIETLEK AREKAVEVMG 


YEKTR 

« Hide

References

[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 10623.
[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 2-26, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
Strain: ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 10623.
[3]"The Mo-Se active site of nicotinate dehydrogenase."
Wagener N., Pierik A.J., Ibdah A., Hille R., Dobbek H.
Proc. Natl. Acad. Sci. U.S.A. 106:11055-11060(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH COFACTOR; NDHM; NDHS AND NDHF, SUBUNIT.
Strain: ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 10623.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ310789 Genomic DNA. Translation: ABC88398.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HRDX-ray2.20A/E1-425[»]
ProteinModelPortalQ0QLF2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48913N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11705.
UniPathwayUPA01010; UER01011.

Family and domain databases

Gene3D3.30.365.10. 4 hits.
3.90.1170.50. 1 hit.
InterProIPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
[Graphical view]
PfamPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view]
SMARTSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMSSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ0QLF2.

Entry information

Entry nameNDLMS_EUBBA
AccessionPrimary (citable) accession number: Q0QLF2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: September 5, 2006
Last modified: October 16, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways