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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)DescriptionActionsGraphical viewLength
    Metal bindingi53Zinc; catalytic1 Publication1
    Metal bindingi78Zinc; catalytic1 Publication1
    Metal bindingi79Zinc; catalytic1 Publication1
    Metal bindingi108Zinc; structural1 Publication1
    Metal bindingi111Zinc; structural1 Publication1
    Metal bindingi114Zinc; structural1 Publication1
    Metal bindingi122Zinc; structural1 Publication1
    Metal bindingi163Zinc; catalytic1 Publication1
    Binding sitei211NAD1 Publication1
    Binding sitei216NAD1 Publication1
    Binding sitei282NAD; via carbonyl oxygen1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi190 – 191NAD1 Publication2
    Nucleotide bindingi306 – 308NAD1 Publication3

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi59F → A, S or Y: No effect. 1 Publication1
    Mutagenesisi211 – 212DI → SR: Alters cofactor specificity from NAD to NADP; when associated with T-348. 1 Publication2
    Mutagenesisi348S → T: Alters cofactor specificity from NAD to NADP; when associated with 211-SR-212. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004184051 – 363L-arabinitol 4-dehydrogenaseAdd BLAST363

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Structurei

    Secondary structure

    1363
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi10 – 14Combined sources5
    Beta strandi20 – 24Combined sources5
    Helixi29 – 34Combined sources6
    Beta strandi42 – 51Combined sources10
    Helixi54 – 62Combined sources9
    Beta strandi63 – 67Combined sources5
    Beta strandi79 – 87Combined sources9
    Beta strandi99 – 102Combined sources4
    Helixi112 – 115Combined sources4
    Helixi119 – 121Combined sources3
    Beta strandi138 – 144Combined sources7
    Helixi145 – 147Combined sources3
    Beta strandi148 – 150Combined sources3
    Helixi156 – 175Combined sources20
    Beta strandi183 – 186Combined sources4
    Helixi190 – 201Combined sources12
    Beta strandi206 – 212Combined sources7
    Helixi214 – 223Combined sources10
    Beta strandi228 – 231Combined sources4
    Helixi237 – 247Combined sources11
    Beta strandi254 – 258Combined sources5
    Helixi263 – 272Combined sources10
    Beta strandi278 – 281Combined sources4
    Helixi293 – 299Combined sources7
    Beta strandi302 – 305Combined sources4
    Helixi313 – 321Combined sources9
    Helixi328 – 330Combined sources3
    Beta strandi331 – 336Combined sources6
    Helixi337 – 339Combined sources3
    Helixi340 – 348Combined sources9
    Helixi350 – 352Combined sources3
    Beta strandi355 – 360Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3M6IX-ray2.60A/B1-363[»]
    ProteinModelPortaliQ7SI09.
    SMRiQ7SI09.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    HOGENOMiHOG000294670.
    InParanoidiQ7SI09.
    KOiK00008.
    OrthoDBiEOG092C2LBV.

    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

    EnsemblFungiiEAA36547; EAA36547; NCU00643.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3M6IX-ray2.60A/B1-363[»]
    ProteinModelPortaliQ7SI09.
    SMRiQ7SI09.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiEAA36547; EAA36547; NCU00643.
    GeneIDi3881980.
    KEGGincr:NCU00643.

    Organism-specific databases

    EuPathDBiFungiDB:NCU00643.

    Phylogenomic databases

    HOGENOMiHOG000294670.
    InParanoidiQ7SI09.
    KOiK00008.
    OrthoDBiEOG092C2LBV.

    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...

    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: November 2, 2016
    This is version 89 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.