A2QAC0 (LAD_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-arabinitol 4-dehydrogenase
Short name=LAD
EC=1.1.1.12

Gene names

Name:	ladA
ORF Names:	An01g10920

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus niger

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 NAPD as cosubstrate. Ref.4 Ref.5
Catalytic activity	L-arabinitol + NAD+ = L-xylulose + NADH. Ref.3
Cofactor	Binds 2 zinc ions per subunit. Ref.5
Pathway	Carbohydrate degradation; L-arabinose degradation via L-arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route): step 2/5. Ref.3
Subunit structure	Homotetramer. Ref.5
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: KM=89 mM for L-arabinitol (at pH 9.6) Ref.3 Ref.4 Ref.5 KM=5 mM for L-xylulose (at pH 9.6) KM=50 µM for NAD (at pH 9.6) KM=8 µM for NADH (at pH 9.6) Vmax=96 µmol/min/mg enzyme for the forward reaction Vmax=805 µmol/min/mg enzyme for the reverse reaction pH dependence: Optimum pH is 9.4. Active from pH 7 to pH 11. Temperature dependence: Optimum temperature is 40-50 degrees Celsius.

Ontologies

Keywords
Biological process	Arabinose catabolism Carbohydrate metabolism
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	L-arabinose catabolic process to xylulose 5-phosphate Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	L-arabinitol 4-dehydrogenase activity Inferred from direct assay Ref.5. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 386	386	L-arabinitol 4-dehydrogenase		PRO_0000418404
Regions
	Nucleotide binding	192 – 193	2	NAD By similarity
	Nucleotide binding	317 – 319	3	NAD By similarity
Sites
	Metal binding	55	1	Zinc; catalytic By similarity
	Metal binding	80	1	Zinc; catalytic By similarity
	Metal binding	81	1	Zinc; catalytic By similarity
	Metal binding	110	1	Zinc; structural By similarity
	Metal binding	113	1	Zinc; structural By similarity
	Metal binding	116	1	Zinc; structural By similarity
	Metal binding	124	1	Zinc; structural By similarity
	Metal binding	165	1	Zinc; catalytic By similarity
	Binding site	213	1	NAD By similarity
	Binding site	218	1	NAD By similarity
	Binding site	293	1	NAD; via carbonyl oxygen By similarity
Experimental info
	Mutagenesis	70	1	M → F: Abolishes enzyme activity. Ref.4
	Mutagenesis	213 – 214	2	DI → SR: Alters cofactor specificity from NAD to NADP; when associated with T-359.
	Mutagenesis	318	1	Y → F: Increases affinity for D-sorbitol. Ref.4
	Mutagenesis	359	1	A → T: Alters cofactor specificity from NAD to NADP; when associated with 213-SR-214. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	A2QAC0 [UniParc]. Last modified September 23, 2008. Version 1. Checksum: CCC018D7E5CF75C6	FASTA	386	41,345
	10 20 30 40 50 60 MATATVLEKA NIGVFTNTKH DLWVADAKPT LEEVKNGQGL QPGEVTIEVR STGICGSDVH 70 80 90 100 110 120 FWHAGCIGPM IVTGDHILGH ESAGQVVAVA PDVTSLKPGD RVAVEPNIIC NACEPCLTGR 130 140 150 160 170 180 YNGCENVQFL STPPVDGLLR RYVNHPAIWC HKIGDMSYED GALLEPLSVS LAGIERSGLR 190 200 210 220 230 240 LGDPCLVTGA GPIGLITLLS ARAAGASPIV ITDIDEGRLE FAKSLVPDVR TYKVQIGLSA 250 260 270 280 290 300 EQNAEGIINV FNDGQGSGPG ALRPRIAMEC TGVESSVASA IWSVKFGGKV FVIGVGKNEM 310 320 330 340 350 360 TVPFMRLSTW EIDLQYQYRY CNTWPRAIRL VRNGVIDLKK LVTHRFLLED AIKAFETAAN 370 380 PKTGAIKVQI MSSEDDVKAA SAGQKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Diversity in regulation and substrate specificity of the pentose catabolic pathway genes/enzymes of Aspergillus niger." de Groot M.J.L., Vandeputte-Rutten L., van den Dool C., Woesten H.A.B., Levisson M., vanKuyk P.A., Ruijter G.J.G., de Vries R.P. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513.
[2]	"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513.
[3]	"Metabolic control analysis of Aspergillus niger L-arabinose catabolism." de Groot M.J., Prathumpai W., Visser J., Ruijter G.J. Biotechnol. Prog. 21:1610-1616(2005) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY.
[4]	"A single amino acid change (Y318F) in the L-arabitol dehydrogenase (LadA) from Aspergillus niger results in a significant increase in affinity for D-sorbitol." Rutten L., Ribot C., Trejo-Aguilar B., Wosten H.A., de Vries R.P. BMC Microbiol. 9:166-166(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF MET-70 AND TYR-318, BIOPHYSICOCHEMICAL PROPERTIES.
[5]	"Cloning, characterization, and engineering of fungal L-arabinitol dehydrogenases." Kim B., Sullivan R.P., Zhao H. Appl. Microbiol. Biotechnol. 87:1407-1414(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF 213-ASP-ILE-214 AND ALA-359, ZINC-BINDING.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ854040 Genomic DNA. Translation: CAH69383.1. AM269980 Genomic DNA. Translation: CAK37272.1.
RefSeq	XP_001389509.1. XM_001389472.2.
3D structure databases
ProteinModelPortal	A2QAC0.
ModBase	Search...
Protein-protein interaction databases
STRING	5061.CADANGAP00001060.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANGAT00001091; CADANGAP00001060; CADANGAG00001091.
GeneID	4977395.
KEGG	ang:ANI_1_1474014.
Phylogenomic databases
eggNOG	COG1063.
HOGENOM	HOG000294670.
KO	K00008.
OrthoDB	EOG479JGK.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13195.
UniPathway	UPA00146; UER00575.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR013149. ADH_C. IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn-type. IPR002328. ADH_Zn_CS. IPR011032. GroES-like. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR11695. PTHR11695. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
SUPFAM	SSF50129. GroES_like. 1 hit.
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LAD_ASPNC

Accession

Primary (citable) accession number: A2QAC0
Secondary accession number(s): Q5GN52

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2012
Last sequence update:	September 23, 2008
Last modified:	April 3, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program