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UniProtKB - A2QAC0 (LAD_ASPNC)
Protein
L-arabinitol 4-dehydrogenase
Gene
ladA
Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
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 with NADP as cosubstrate.
2 PublicationsCatalytic activityi
- EC:1.1.1.121 Publication
Cofactori
Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication
Kineticsi
- KM=89 mM for L-arabinitol (at pH 9.6)3 Publications
- KM=5 mM for L-xylulose (at pH 9.6)3 Publications
- KM=50 µM for NAD (at pH 9.6)3 Publications
- KM=8 µM for NADH (at pH 9.6)3 Publications
- Vmax=96 µmol/min/mg enzyme for the forward reaction3 Publications
- Vmax=805 µmol/min/mg enzyme for the reverse reaction3 Publications
pH dependencei
Optimum pH is 9.4. Active from pH 7 to pH 11.3 Publications
Temperature dependencei
Optimum temperature is 40-50 degrees Celsius.3 Publications
: 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).1 Publication 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 | 55 | Zinc; catalyticBy similarity | 1 | |
Metal bindingi | 80 | Zinc; catalyticBy similarity | 1 | |
Metal bindingi | 81 | Zinc; catalyticBy similarity | 1 | |
Metal bindingi | 110 | Zinc; structuralBy similarity | 1 | |
Metal bindingi | 113 | Zinc; structuralBy similarity | 1 | |
Metal bindingi | 116 | Zinc; structuralBy similarity | 1 | |
Metal bindingi | 124 | Zinc; structuralBy similarity | 1 | |
Metal bindingi | 165 | Zinc; catalyticBy similarity | 1 | |
Binding sitei | 213 | NADBy similarity | 1 | |
Binding sitei | 218 | NADBy similarity | 1 | |
Binding sitei | 293 | NAD; via carbonyl oxygenBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 192 – 193 | NADBy similarity | 2 | |
Nucleotide bindingi | 317 – 319 | NADBy similarity | 3 |
GO - Molecular functioni
- L-arabinitol 4-dehydrogenase activity Source: UniProtKB
- zinc ion binding Source: InterPro
GO - Biological processi
- L-arabinose catabolic process to xylulose 5-phosphate Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Arabinose catabolism, Carbohydrate metabolism |
Ligand | Metal-binding, NAD, Zinc |
Enzyme and pathway databases
BRENDAi | 1.1.1.12, 518 |
UniPathwayi | UPA00146;UER00575 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:ladA ORF Names:An01g10920 |
Organismi | Aspergillus niger (strain CBS 513.88 / FGSC A1513) |
Taxonomic identifieri | 425011 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Circumdati › |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | FungiDB:An01g10920 |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 70 | M → F: Abolishes enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 213 – 214 | DI → SR: Alters cofactor specificity from NAD to NADP; when associated with T-359. 1 Publication | 2 | |
Mutagenesisi | 318 | Y → F: Increases affinity for D-sorbitol. 1 Publication | 1 | |
Mutagenesisi | 359 | A → T: Alters cofactor specificity from NAD to NADP; when associated with 213-SR-214. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000418404 | 1 – 386 | L-arabinitol 4-dehydrogenaseAdd BLAST | 386 |
Proteomic databases
PaxDbi | A2QAC0 |
Interactioni
Subunit structurei
Homotetramer.
1 PublicationFamily & Domainsi
Sequence similaritiesi
Belongs to the zinc-containing alcohol dehydrogenase family.Curated
Phylogenomic databases
HOGENOMi | CLU_026673_11_5_1 |
Family and domain databases
CDDi | cd05285, sorbitol_DH, 1 hit |
InterProi | View protein in InterPro IPR013149, ADH_C IPR013154, ADH_N IPR002328, ADH_Zn_CS 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 |
PROSITEi | View protein in PROSITE PS00059, ADH_ZINC, 1 hit |
i Sequence
Sequence statusi: Complete.
A2QAC0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MATATVLEKA NIGVFTNTKH DLWVADAKPT LEEVKNGQGL QPGEVTIEVR
60 70 80 90 100
STGICGSDVH FWHAGCIGPM IVTGDHILGH ESAGQVVAVA PDVTSLKPGD
110 120 130 140 150
RVAVEPNIIC NACEPCLTGR YNGCENVQFL STPPVDGLLR RYVNHPAIWC
160 170 180 190 200
HKIGDMSYED GALLEPLSVS LAGIERSGLR LGDPCLVTGA GPIGLITLLS
210 220 230 240 250
ARAAGASPIV ITDIDEGRLE FAKSLVPDVR TYKVQIGLSA EQNAEGIINV
260 270 280 290 300
FNDGQGSGPG ALRPRIAMEC TGVESSVASA IWSVKFGGKV FVIGVGKNEM
310 320 330 340 350
TVPFMRLSTW EIDLQYQYRY CNTWPRAIRL VRNGVIDLKK LVTHRFLLED
360 370 380
AIKAFETAAN PKTGAIKVQI MSSEDDVKAA SAGQKI
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ854040 Genomic DNA Translation: CAH69383.1 AM269980 Genomic DNA Translation: CAK37272.1 |
RefSeqi | XP_001389509.1, XM_001389472.2 |
Genome annotation databases
EnsemblFungii | CAK37272; CAK37272; An01g10920 |
GeneIDi | 4977395 |
KEGGi | ang:ANI_1_1474014 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ854040 Genomic DNA Translation: CAH69383.1 AM269980 Genomic DNA Translation: CAK37272.1 |
RefSeqi | XP_001389509.1, XM_001389472.2 |
3D structure databases
SMRi | A2QAC0 |
ModBasei | Search... |
Proteomic databases
PaxDbi | A2QAC0 |
Genome annotation databases
EnsemblFungii | CAK37272; CAK37272; An01g10920 |
GeneIDi | 4977395 |
KEGGi | ang:ANI_1_1474014 |
Organism-specific databases
VEuPathDBi | FungiDB:An01g10920 |
Phylogenomic databases
HOGENOMi | CLU_026673_11_5_1 |
Enzyme and pathway databases
UniPathwayi | UPA00146;UER00575 |
BRENDAi | 1.1.1.12, 518 |
Family and domain databases
CDDi | cd05285, sorbitol_DH, 1 hit |
InterProi | View protein in InterPro IPR013149, ADH_C IPR013154, ADH_N IPR002328, ADH_Zn_CS 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 |
PROSITEi | View protein in PROSITE PS00059, ADH_ZINC, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | LAD_ASPNC | |
Accessioni | A2QAC0Primary (citable) accession number: A2QAC0 Secondary accession number(s): Q5GN52 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 5, 2012 |
Last sequence update: | September 23, 2008 | |
Last modified: | February 23, 2022 | |
This is version 73 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
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families