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Protein

Nicotinate dehydrogenase large molybdopterin subunit

Gene

ndhL

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

Se-Mo-molybdopterin cytosine dinucleotide1 PublicationNote: Binds 1 Se-Mo-molybdopterin cytosine dinucleotide (Se-Mo-MCD) cofactor per heterotetramer. The cofactor is bound between the NdhL and NdhM subunits.1 Publication

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 sitei208Se-Mo-molybdopterin cytosine dinucleotide1 Publication1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • nicotinate dehydrogenase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, Molybdenum, NADP, Selenium

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11705.
BRENDAi1.17.1.5. 1459.
UniPathwayiUPA01010; UER01011.

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00004042432 – 425Nicotinate dehydrogenase large molybdopterin subunit1 PublicationAdd BLAST424

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-48913N.

Structurei

Secondary structure

1425
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 21Combined sources5
Helixi28 – 30Combined sources3
Beta strandi37 – 43Combined sources7
Beta strandi45 – 55Combined sources11
Helixi57 – 60Combined sources4
Beta strandi65 – 69Combined sources5
Helixi71 – 73Combined sources3
Beta strandi82 – 84Combined sources3
Beta strandi101 – 109Combined sources9
Helixi110 – 119Combined sources10
Beta strandi121 – 126Combined sources6
Helixi133 – 137Combined sources5
Beta strandi149 – 159Combined sources11
Helixi161 – 166Combined sources6
Beta strandi169 – 178Combined sources10
Beta strandi190 – 195Combined sources6
Beta strandi201 – 205Combined sources5
Helixi210 – 220Combined sources11
Helixi225 – 227Combined sources3
Beta strandi228 – 232Combined sources5
Turni239 – 242Combined sources4
Helixi248 – 258Combined sources11
Beta strandi262 – 265Combined sources4
Helixi268 – 274Combined sources7
Beta strandi281 – 289Combined sources9
Beta strandi295 – 309Combined sources15
Helixi313 – 323Combined sources11
Beta strandi333 – 341Combined sources9
Beta strandi343 – 345Combined sources3
Turni351 – 354Combined sources4
Helixi355 – 372Combined sources18
Helixi377 – 384Combined sources8
Helixi404 – 419Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HRDX-ray2.20A/E1-425[»]
ProteinModelPortaliQ0QLF2.
SMRiQ0QLF2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ0QLF2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni238 – 240Se-Mo-molybdopterin cytosine dinucleotide binding1 Publication3

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Sequence analysis

Phylogenomic databases

KOiK20447.

Family and domain databases

Gene3Di3.30.365.10. 4 hits.
3.90.1170.50. 1 hit.
InterProiIPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view]
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q0QLF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKDYQVLGK NKVKVDSLEK VMGTAKFAAD YSFPDMLYAG VFRSTVPHAR
60 70 80 90 100
IVSLDLSKAR AIDGVEAVLD YHAIPGKNRF GIIIKDEPCL VDDKVRRYGD
110 120 130 140 150
AIAVVAAQTP DLVQEALDAI TIEYEELEGI FTMERALEED SPAIHGDTNI
160 170 180 190 200
HQVKHLEYGD VDAAFKQCDI VVEDTYSTHR LTHMFIEPDA GVSYYDNEGM
210 220 230 240 250
LTVVVSTQNP HYDRGEVAGM LALPNSKVRI IQATTGGGFG GKLDLSVQCH
260 270 280 290 300
CALLTYHTKK PVKMVRSREE STTVSSKRHP MTMHCKTGAT KDGRLQAVQV
310 320 330 340 350
EMFGDTGAYA SYGPAVITRA TVHCMGPYVV PNVRVDAKFV YTNNPMSGAF
360 370 380 390 400
RGFGVPQASV CHEGQMNALA KALGMDPIDI RILNAHQVGA KLATGQVLEN
410 420
SVGLIETLEK AREKAVEVMG YEKTR
Length:425
Mass (Da):46,488
Last modified:September 5, 2006 - v1
Checksum:iF8270B4ABECD71A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ310789 Genomic DNA. Translation: ABC88398.1.

Genome annotation databases

KEGGiag:ABC88398.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ310789 Genomic DNA. Translation: ABC88398.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HRDX-ray2.20A/E1-425[»]
ProteinModelPortaliQ0QLF2.
SMRiQ0QLF2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48913N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:ABC88398.

Phylogenomic databases

KOiK20447.

Enzyme and pathway databases

UniPathwayiUPA01010; UER01011.
BioCyciMetaCyc:MONOMER-11705.
BRENDAi1.17.1.5. 1459.

Miscellaneous databases

EvolutionaryTraceiQ0QLF2.

Family and domain databases

Gene3Di3.30.365.10. 4 hits.
3.90.1170.50. 1 hit.
InterProiIPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view]
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNDLMS_EUBBA
AccessioniPrimary (citable) accession number: Q0QLF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: September 5, 2006
Last modified: November 30, 2016
This is version 46 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.