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UniProtKB - Q7SI09 (LAD_NEUCR)
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
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 PublicationCatalytic activityi
- EC:1.1.1.121 Publication
Cofactori
Zn2+2 PublicationsNote: Binds 2 Zn2+ ions per subunit.2 Publications
Kineticsi
- KM=16 mM for L-arabinitol (at pH 8)1 Publication
- KM=290 mM for xylitol (at pH 8)1 Publication
- KM=35 mM for adonitol (at pH 8)1 Publication
- 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
: L-arabinose degradation via L-arabinitol Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes D-xylulose 5-phosphate from L-arabinose (fungal route). 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 53 | Zinc; catalytic1 Publication | 1 | |
Metal bindingi | 78 | Zinc; catalytic1 Publication | 1 | |
Metal bindingi | 79 | Zinc; catalytic1 Publication | 1 | |
Metal bindingi | 108 | Zinc; structural1 Publication | 1 | |
Metal bindingi | 111 | Zinc; structural1 Publication | 1 | |
Metal bindingi | 114 | Zinc; structural1 Publication | 1 | |
Metal bindingi | 122 | Zinc; structural1 Publication | 1 | |
Metal bindingi | 163 | Zinc; catalytic1 Publication | 1 | |
Binding sitei | 211 | NAD1 Publication | 1 | |
Binding sitei | 216 | NAD1 Publication | 1 | |
Binding sitei | 282 | NAD; via carbonyl oxygen1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 190 – 191 | NAD1 Publication | 2 | |
Nucleotide bindingi | 306 – 308 | NAD1 Publication | 3 |
GO - Molecular functioni
- L-arabinitol 4-dehydrogenase activity Source: UniProtKB
- L-iditol 2-dehydrogenase activity Source: GO_Central
- metal ion binding Source: UniProtKB-KW
- nucleotide binding Source: UniProtKB-KW
GO - Biological processi
- L-arabinose catabolic process to xylulose 5-phosphate Source: UniProtKB-UniPathway
- sorbitol catabolic process Source: GO_Central
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Arabinose catabolism, Carbohydrate metabolism |
Ligand | Metal-binding, NAD, Nucleotide-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 1.1.1.12, 3627 |
UniPathwayi | UPA00146;UER00575 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:ard-1 ORF Names:NCU00643 |
Organismi | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
Taxonomic identifieri | 367110 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora › |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | FungiDB:NCU00643 |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 59 | F → A, S or Y: No effect. 1 Publication | 1 | |
Mutagenesisi | 211 – 212 | DI → SR: Alters cofactor specificity from NAD to NADP; when associated with T-348. 1 Publication | 2 | |
Mutagenesisi | 348 | S → T: Alters cofactor specificity from NAD to NADP; when associated with 211-SR-212. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000418405 | 1 – 363 | L-arabinitol 4-dehydrogenaseAdd BLAST | 363 |
Interactioni
Subunit structurei
Homotetramer.
2 PublicationsProtein-protein interaction databases
STRINGi | 5141.EFNCRP00000000635 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q7SI09 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the zinc-containing alcohol dehydrogenase family.Curated
Phylogenomic databases
HOGENOMi | CLU_026673_11_5_1 |
InParanoidi | Q7SI09 |
Family and domain databases
CDDi | cd05285, sorbitol_DH, 1 hit |
InterProi | View protein in InterPro IPR013149, ADH_C IPR013154, ADH_N IPR011032, GroES-like_sf IPR036291, NAD(P)-bd_dom_sf IPR045306, SDH-like |
Pfami | View protein in Pfam PF08240, ADH_N, 1 hit PF00107, ADH_zinc_N, 1 hit |
SUPFAMi | SSF50129, SSF50129, 1 hit SSF51735, SSF51735, 1 hit |
i Sequence
Sequence statusi: Complete.
Q7SI09-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CM002236 Genomic DNA Translation: EAA36547.1 |
RefSeqi | XP_965783.1, XM_960690.2 |
Genome annotation databases
EnsemblFungii | EAA36547; EAA36547; NCU00643 |
GeneIDi | 3881980 |
KEGGi | ncr:NCU00643 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CM002236 Genomic DNA Translation: EAA36547.1 |
RefSeqi | XP_965783.1, XM_960690.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3M6I | X-ray | 2.60 | A/B | 1-363 | [»] | |
SMRi | Q7SI09 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 5141.EFNCRP00000000635 |
Genome annotation databases
EnsemblFungii | EAA36547; EAA36547; NCU00643 |
GeneIDi | 3881980 |
KEGGi | ncr:NCU00643 |
Organism-specific databases
VEuPathDBi | FungiDB:NCU00643 |
Phylogenomic databases
HOGENOMi | CLU_026673_11_5_1 |
InParanoidi | Q7SI09 |
Enzyme and pathway databases
UniPathwayi | UPA00146;UER00575 |
BRENDAi | 1.1.1.12, 3627 |
Family and domain databases
CDDi | cd05285, sorbitol_DH, 1 hit |
InterProi | View protein in InterPro IPR013149, ADH_C IPR013154, ADH_N IPR011032, GroES-like_sf IPR036291, NAD(P)-bd_dom_sf IPR045306, SDH-like |
Pfami | View protein in Pfam PF08240, ADH_N, 1 hit PF00107, ADH_zinc_N, 1 hit |
SUPFAMi | SSF50129, SSF50129, 1 hit SSF51735, SSF51735, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | LAD_NEUCR | |
Accessioni | Q7SI09Primary (citable) accession number: Q7SI09 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 5, 2012 |
Last sequence update: | December 15, 2003 | |
Last modified: | February 23, 2022 | |
This is version 106 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families