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Protein

L-arabinitol 4-dehydrogenase

Gene

ard-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD-dependent oxidation of L-arabinitol to L-xylulose in the fungal L-arabinose catabolic pathway. L-arabinose catabolism is important for using plant material as a carbon source. Not active on D-arabinitol, D-sorbitol and D-mannitol.1 Publication

Catalytic activityi

L-arabinitol + NAD+ = L-xylulose + NADH.1 Publication

Cofactori

Zn2+2 PublicationsNote: Binds 2 Zn2+ ions per subunit.2 Publications

Kineticsi

  1. KM=16 mM for L-arabinitol (at pH 8)1 Publication
  2. KM=290 mM for xylitol (at pH 8)1 Publication
  3. KM=35 mM for adonitol (at pH 8)1 Publication
  4. KM=174 µM for NAD (at pH 8)1 Publication

    pH dependencei

    Optimum pH is 9.5. Active from pH 8 to pH 10.5.1 Publication

    Temperature dependencei

    Optimum temperature is 45-55 degrees Celsius.1 Publication

    Pathwayi: L-arabinose degradation via L-arabinitol

    This protein is involved in step 2 of the subpathway that synthesizes D-xylulose 5-phosphate from L-arabinose (fungal route).
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. L-arabinitol 4-dehydrogenase (ard-1)
    3. no protein annotated in this organism
    4. no protein annotated in this organism
    5. no protein annotated in this organism
    This subpathway is part of the pathway L-arabinose degradation via L-arabinitol, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-xylulose 5-phosphate from L-arabinose (fungal route), the pathway L-arabinose degradation via L-arabinitol and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi53 – 531Zinc; catalytic1 Publication
    Metal bindingi78 – 781Zinc; catalytic1 Publication
    Metal bindingi79 – 791Zinc; catalytic1 Publication
    Metal bindingi108 – 1081Zinc; structural1 Publication
    Metal bindingi111 – 1111Zinc; structural1 Publication
    Metal bindingi114 – 1141Zinc; structural1 Publication
    Metal bindingi122 – 1221Zinc; structural1 Publication
    Metal bindingi163 – 1631Zinc; catalytic1 Publication
    Binding sitei211 – 2111NAD1 Publication
    Binding sitei216 – 2161NAD1 Publication
    Binding sitei282 – 2821NAD; via carbonyl oxygen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi190 – 1912NAD1 Publication
    Nucleotide bindingi306 – 3083NAD1 Publication

    GO - Molecular functioni

    • L-arabinitol 4-dehydrogenase activity Source: UniProtKB
    • nucleotide binding Source: UniProtKB-KW
    • zinc ion binding Source: InterPro

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Arabinose catabolism, Carbohydrate metabolism

    Keywords - Ligandi

    Metal-binding, NAD, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BRENDAi1.1.1.12. 3627.
    UniPathwayiUPA00146; UER00575.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-arabinitol 4-dehydrogenase (EC:1.1.1.12)
    Short name:
    LAD
    Gene namesi
    Name:ard-1
    ORF Names:NCU00643
    OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
    Taxonomic identifieri367110 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
    Proteomesi
    • UP000001805 Componenti: Chromosome 1, Linkage Group I

    Organism-specific databases

    EuPathDBiFungiDB:NCU00643.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi59 – 591F → A, S or Y: No effect. 1 Publication
    Mutagenesisi211 – 2122DI → SR: Alters cofactor specificity from NAD to NADP; when associated with T-348. 1 Publication
    Mutagenesisi348 – 3481S → T: Alters cofactor specificity from NAD to NADP; when associated with 211-SR-212. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 363363L-arabinitol 4-dehydrogenasePRO_0000418405Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Structurei

    Secondary structure

    1
    363
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 145Combined sources
    Beta strandi20 – 245Combined sources
    Helixi29 – 346Combined sources
    Beta strandi42 – 5110Combined sources
    Helixi54 – 629Combined sources
    Beta strandi63 – 675Combined sources
    Beta strandi79 – 879Combined sources
    Beta strandi99 – 1024Combined sources
    Helixi112 – 1154Combined sources
    Helixi119 – 1213Combined sources
    Beta strandi138 – 1447Combined sources
    Helixi145 – 1473Combined sources
    Beta strandi148 – 1503Combined sources
    Helixi156 – 17520Combined sources
    Beta strandi183 – 1864Combined sources
    Helixi190 – 20112Combined sources
    Beta strandi206 – 2127Combined sources
    Helixi214 – 22310Combined sources
    Beta strandi228 – 2314Combined sources
    Helixi237 – 24711Combined sources
    Beta strandi254 – 2585Combined sources
    Helixi263 – 27210Combined sources
    Beta strandi278 – 2814Combined sources
    Helixi293 – 2997Combined sources
    Beta strandi302 – 3054Combined sources
    Helixi313 – 3219Combined sources
    Helixi328 – 3303Combined sources
    Beta strandi331 – 3366Combined sources
    Helixi337 – 3393Combined sources
    Helixi340 – 3489Combined sources
    Helixi350 – 3523Combined sources
    Beta strandi355 – 3606Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3M6IX-ray2.60A/B1-363[»]
    ProteinModelPortaliQ7SI09.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    HOGENOMiHOG000294670.
    InParanoidiQ7SI09.
    KOiK00008.
    OrthoDBiEOG79CZ8G.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q7SI09-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MASSASKTNI GVFTNPQHDL WISEASPSLE SVQKGEELKE GEVTVAVRST
    60 70 80 90 100
    GICGSDVHFW KHGCIGPMIV ECDHVLGHES AGEVIAVHPS VKSIKVGDRV
    110 120 130 140 150
    AIEPQVICNA CEPCLTGRYN GCERVDFLST PPVPGLLRRY VNHPAVWCHK
    160 170 180 190 200
    IGNMSYENGA MLEPLSVALA GLQRAGVRLG DPVLICGAGP IGLITMLCAK
    210 220 230 240 250
    AAGACPLVIT DIDEGRLKFA KEICPEVVTH KVERLSAEES AKKIVESFGG
    260 270 280 290 300
    IEPAVALECT GVESSIAAAI WAVKFGGKVF VIGVGKNEIQ IPFMRASVRE
    310 320 330 340 350
    VDLQFQYRYC NTWPRAIRLV ENGLVDLTRL VTHRFPLEDA LKAFETASDP
    360
    KTGAIKVQIQ SLE
    Length:363
    Mass (Da):39,136
    Last modified:December 15, 2003 - v1
    Checksum:i6A1CDDDB24D2AE40
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CM002236 Genomic DNA. Translation: EAA36547.1.
    RefSeqiXP_965783.1. XM_960690.2.

    Genome annotation databases

    EnsemblFungiiEFNCRT00000000635; EFNCRP00000000635; EFNCRG00000000635.
    GeneIDi3881980.
    KEGGincr:NCU00643.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CM002236 Genomic DNA. Translation: EAA36547.1.
    RefSeqiXP_965783.1. XM_960690.2.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3M6IX-ray2.60A/B1-363[»]
    ProteinModelPortaliQ7SI09.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiEFNCRT00000000635; EFNCRP00000000635; EFNCRG00000000635.
    GeneIDi3881980.
    KEGGincr:NCU00643.

    Organism-specific databases

    EuPathDBiFungiDB:NCU00643.

    Phylogenomic databases

    HOGENOMiHOG000294670.
    InParanoidiQ7SI09.
    KOiK00008.
    OrthoDBiEOG79CZ8G.

    Enzyme and pathway databases

    UniPathwayiUPA00146; UER00575.
    BRENDAi1.1.1.12. 3627.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The genome sequence of the filamentous fungus Neurospora crassa."
      Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
      , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
      Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
    2. "Cloning, characterization, and mutational analysis of a highly active and stable L-arabinitol 4-dehydrogenase from Neurospora crassa."
      Sullivan R., Zhao H.
      Appl. Microbiol. Biotechnol. 77:845-852(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, MUTAGENESIS OF PHE-59, BIOPHYSICOCHEMICAL PROPERTIES.
    3. "Structure and engineering of L-arabinitol 4-dehydrogenase from Neurospora crassa."
      Bae B., Sullivan R.P., Zhao H., Nair S.K.
      J. Mol. Biol. 402:230-240(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC, MUTAGENESIS OF 211-ASP-ILE-212 AND SER-348, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiLAD_NEUCR
    AccessioniPrimary (citable) accession number: Q7SI09
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: December 15, 2003
    Last modified: December 9, 2015
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    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.