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Q0QLF2

- NDLMS_EUBBA

UniProt

Q0QLF2 - NDLMS_EUBBA

Protein

Nicotinate dehydrogenase large molybdopterin subunit

Gene

ndhL

Organism
Eubacterium barkeri (Clostridium barkeri)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 1 (05 Sep 2006)
      Previous versions | rss
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    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

    Binds 1 hydroxyoxoselanylmolybdenum molybdopterin cytosine dinucleotide 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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei208 – 2081Hydroxyoxoselanylmolybdenum molybdopterin cytosine dinucleotide1 Publication

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. nicotinate dehydrogenase activity Source: UniProtKB

    GO - Biological processi

    1. cofactor catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, Molybdenum, NADP, Selenium

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-11705.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 425424Nicotinate dehydrogenase large molybdopterin subunit1 PublicationPRO_0000404243Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    DIPiDIP-48913N.

    Structurei

    Secondary structure

    1
    425
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 215
    Helixi28 – 303
    Beta strandi37 – 437
    Beta strandi45 – 5511
    Helixi57 – 604
    Beta strandi65 – 695
    Helixi71 – 733
    Beta strandi82 – 843
    Beta strandi101 – 1099
    Helixi110 – 11910
    Beta strandi121 – 1266
    Helixi133 – 1375
    Beta strandi149 – 15911
    Helixi161 – 1666
    Beta strandi169 – 17810
    Beta strandi190 – 1956
    Beta strandi201 – 2055
    Helixi210 – 22011
    Helixi225 – 2273
    Beta strandi228 – 2325
    Turni239 – 2424
    Helixi248 – 25811
    Beta strandi262 – 2654
    Helixi268 – 2747
    Beta strandi281 – 2899
    Beta strandi295 – 30915
    Helixi313 – 32311
    Beta strandi333 – 3419
    Beta strandi343 – 3453
    Turni351 – 3544
    Helixi355 – 37218
    Helixi377 – 3848
    Helixi404 – 41916

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HRDX-ray2.20A/E1-425[»]
    ProteinModelPortaliQ0QLF2.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ0QLF2.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni238 – 2403Hydroxyoxoselanylmolybdenum molybdopterin cytosine dinucleotide binding1 Publication

    Sequence similaritiesi

    Belongs to the xanthine dehydrogenase family.Sequence Analysis

    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

    MGKDYQVLGK NKVKVDSLEK VMGTAKFAAD YSFPDMLYAG VFRSTVPHAR    50
    IVSLDLSKAR AIDGVEAVLD YHAIPGKNRF GIIIKDEPCL VDDKVRRYGD 100
    AIAVVAAQTP DLVQEALDAI TIEYEELEGI FTMERALEED SPAIHGDTNI 150
    HQVKHLEYGD VDAAFKQCDI VVEDTYSTHR LTHMFIEPDA GVSYYDNEGM 200
    LTVVVSTQNP HYDRGEVAGM LALPNSKVRI IQATTGGGFG GKLDLSVQCH 250
    CALLTYHTKK PVKMVRSREE STTVSSKRHP MTMHCKTGAT KDGRLQAVQV 300
    EMFGDTGAYA SYGPAVITRA TVHCMGPYVV PNVRVDAKFV YTNNPMSGAF 350
    RGFGVPQASV CHEGQMNALA KALGMDPIDI RILNAHQVGA KLATGQVLEN 400
    SVGLIETLEK AREKAVEVMG YEKTR 425
    Length:425
    Mass (Da):46,488
    Last modified:September 5, 2006 - v1
    Checksum:iF8270B4ABECD71A5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ310789 Genomic DNA. Translation: ABC88398.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ310789 Genomic DNA. Translation: ABC88398.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HRD X-ray 2.20 A/E 1-425 [» ]
    ProteinModelPortali Q0QLF2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48913N.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA01010 ; UER01011 .
    BioCyci MetaCyc:MONOMER-11705.

    Miscellaneous databases

    EvolutionaryTracei Q0QLF2.

    Family and domain databases

    Gene3Di 3.30.365.10. 4 hits.
    3.90.1170.50. 1 hit.
    InterProi IPR000674. Ald_Oxase/Xan_DH_a/b.
    IPR008274. AldOxase/xan_DH_Mopterin-bd.
    [Graphical view ]
    Pfami PF01315. Ald_Xan_dh_C. 1 hit.
    PF02738. Ald_Xan_dh_C2. 1 hit.
    [Graphical view ]
    SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54665. SSF54665. 1 hit.
    SSF56003. SSF56003. 1 hit.
    ProtoNeti Search...

    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 2-26, 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 COFACTOR; NDHM; NDHS AND NDHF, SUBUNIT.
      Strain: ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 106231 Publication.

    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: October 1, 2014
    This is version 38 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

    External Data

    Dasty 3