L-arabinitol 4-dehydrogenase - Hypocrea jecorina

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Q96V44 (LAD_HYPJE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 56. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Gene names

Name:

lad1

Organism

Hypocrea jecorina (Trichoderma reesei)

Taxonomic identifier

51453 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea › mitosporic Hypocrea › Trichoderma

Protein attributes

Sequence length	377 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. Can partially compensate for xylitol dehydrogenase in xdh1 mutants. Also oxidizes galactitol to L-xylo-3-hexulose as an alternative to the standard Leloir pathway for D-galactose metabolism. NAPD cannot act as a cosubstrate. Ref.1 Ref.2 Ref.3 Ref.4
Catalytic activity	L-arabinitol + NAD⁺ = L-xylulose + NADH. Ref.1
Cofactor	Binds 2 zinc ions per subunit. Ref.4
Pathway	Carbohydrate degradation; L-arabinose degradation via L-arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route): step 2/5.
Subunit structure	Homotetramer. Ref.4
Induction	Only expressed when grown on L-arabinose. Ref.1
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: K_M=18 mM for L-arabinitol (at pH 7) Ref.1 Ref.3 Ref.4 K_M=200 mM for xylitol (at pH 7) K_M=4.5 mM for L-arabinitol (at pH 8.6) K_M=25 mM for D-talitol (at pH 8.6) K_M=60 mM for galactitol (at pH 8.6) K_M=46 mM for D-sorbitol (at pH 8.6) K_M=11.3 mM for D-allitol (at pH 8.6) K_M=37 mM for L-mannitol (at pH 8.6) K_M=191 mM for L-iditol (at pH 8.6) K_M=580 mM for D-arabino-3-hexulose (at pH 8.6) K_M=81 mM for L-xylo-3-hexulose (at pH 8.6) K_M=96 mM for D-fructose (at pH 8.6) K_M=81 mM for D-psicose (at pH 8.6) K_M=19 mM for L-sorbitol (at pH 8.6) K_M=28 mM for L-tagatose (at pH 8.6) K_M=115 mM for D-sorbose (at pH 8.6) K_M=180 µM for NAD (at pH 7) V_max=27 nmol/sec/mg enzyme with L-arabinitol as substrate (at pH 9 and 10) V_max=10 nmol/sec/mg enzyme with L-arabinitol as substrate (at pH 7) V_max=6 nmol/sec/mg enzyme with xylitol as substrate (at pH 7) V_max=0.213 nmol/sec/mg enzyme with L-arabinitol as substrate (at pH 8.6) V_max=0.146 nmol/sec/mg enzyme with D-talitol as substrate (at pH 8.6) V_max=0.012 nmol/sec/mg enzyme with galactitol as substrate (at pH 8.6) V_max=0.034 nmol/sec/mg enzyme with D-sorbitol as substrate (at pH 8.6) V_max=0.008 nmol/sec/mg enzyme with D-allitol as substrate (at pH 8.6) V_max=0.027 nmol/sec/mg enzyme with L-mannitol as substrate (at pH 8.6) V_max=0.021 nmol/sec/mg enzyme with L-iditol as substrate (at pH 8.6) V_max=0.969 nmol/sec/mg enzyme with D-arabino-3-hexulose as substrate (at pH 8.6) V_max=0.197 nmol/sec/mg enzyme with L-xylo-3-hexulose as substrate (at pH 8.6) V_max=0.008 nmol/sec/mg enzyme with D-fructose as substrate (at pH 8.6) V_max=0.011 nmol/sec/mg enzyme with D-psicose as substrate (at pH 8.6) V_max=0.001 nmol/sec/mg enzyme with L-sorbitol as substrate (at pH 8.6) V_max=0.003 nmol/sec/mg enzyme with L-tagatose as substrate (at pH 8.6) V_max=0.001 nmol/sec/mg enzyme with D-sorbose as substrate (at pH 8.6) pH dependence: Optimum pH is 9.4. Active from pH 7 to pH 11. Temperature dependence: Optimum temperature is 55-65 degrees Celsius.

Ontologies

Keywords
Biological process	Arabinose catabolism Carbohydrate metabolism Galactose metabolism Xylose metabolism
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	D-xylose catabolic process Inferred from mutant phenotype Ref.2. Source: UniProtKB L-arabinose catabolic process to xylulose 5-phosphate Inferred from electronic annotation. Source: UniProtKB-UniPathway arabinose catabolic process Inferred from mutant phenotype Ref.3. Source: UniProtKB galactose catabolic process Inferred from mutant phenotype Ref.3. Source: UniProtKB
Molecular_function	L-arabinitol 4-dehydrogenase activity Inferred from direct assay Ref.1. 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 – 377

377

L-arabinitol 4-dehydrogenase

PRO_0000418403

Regions

Nucleotide binding

203 – 204

NAD By similarity

Nucleotide binding

320 – 322

NAD By similarity

Sites

Metal binding

Zinc; catalytic By similarity

Metal binding

Zinc; catalytic By similarity

Metal binding

Zinc; catalytic By similarity

Metal binding

121

Zinc; structural By similarity

Metal binding

124

Zinc; structural By similarity

Metal binding

127

Zinc; structural By similarity

Metal binding

135

Zinc; structural By similarity

Metal binding

176

Zinc; catalytic By similarity

Binding site

224

NAD By similarity

Binding site

229

NAD By similarity

Binding site

296

NAD; via carbonyl oxygen By similarity

Experimental info

Mutagenesis

224 – 225

DI → SR: Alters cofactor specificity from NAD to NADP; when associated with T-362.

Mutagenesis

362

A → T: Alters cofactor specificity from NAD to NADP; when associated with 224-SR-225. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

Q96V44 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 5015D4A61D948D1D
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FASTA

377

39,886

        10         20         30         40         50         60 
MSPSAVDDAP KATGAAISVK PNIGVFTNPK HDLWISEAEP SADAVKSGAD LKPGEVTIAV 

        70         80         90        100        110        120 
RSTGICGSDV HFWHAGCIGP MIVEGDHILG HESAGEVIAV HPTVSSLQIG DRVAIEPNII 

       130        140        150        160        170        180 
CNACEPCLTG RYNGCEKVEF LSTPPVPGLL RRYVNHPAVW CHKIGNMSWE NGALLEPLSV 

       190        200        210        220        230        240 
ALAGMQRAKV QLGDPVLVCG AGPIGLVSML CAAAAGACPL VITDISESRL AFAKEICPRV 

       250        260        270        280        290        300 
TTHRIEIGKS AEETAKSIVS SFGGVEPAVT LECTGVESSI AAAIWASKFG GKVFVIGVGK 

       310        320        330        340        350        360 
NEISIPFMRA SVREVDIQLQ YRYSNTWPRA IRLIESGVID LSKFVTHRFP LEDAVKAFET 

       370 
SADPKSGAIK VMIQSLD

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References

[1]	"Cloning and expression of a fungal L-arabinitol 4-dehydrogenase gene." Richard P., Londesborough J., Putkonen M., Kalkkinen N., Penttila M. J. Biol. Chem. 276:40631-40637(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 12-40; 323-329 AND 357-365, FUNCTION, CATALYTIC ACTIVITY, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: ATCC 56765 / Rut C-30.
[2]	"D-xylose metabolism in Hypocrea jecorina: loss of the xylitol dehydrogenase step can be partially compensated for by lad1-encoded L-arabinitol-4-dehydrogenase." Seiboth B., Hartl L., Pail M., Kubicek C.P. Eukaryot. Cell 2:867-875(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: ATCC 26921 / CBS 392.92 / QM9414.
[3]	"The metabolic role and evolution of L-arabinitol 4-dehydrogenase of Hypocrea jecorina." Pail M., Peterbauer T., Seiboth B., Hametner C., Druzhinina I., Kubicek C.P. Eur. J. Biochem. 271:1864-1872(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"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 224-ASP-ILE-225 AND ALA-362, ZINC-BINDING.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF355628 mRNA. Translation: AAL08944.1. AY225444 Genomic DNA. Translation: AAP57209.1.
3D structure databases
HSSP	HSSP built from PDB template 1PL7 based on UniProtKB Q00796.
ProteinModelPortal	Q96V44.
ModBase	Search...
Protein-protein interaction databases
STRING	51453.JGI49753.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG1063.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13196.
SABIO-RK	Q96V44.
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. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LAD_HYPJE

Accession

Primary (citable) accession number: Q96V44

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2012
Last sequence update:	December 1, 2001
Last modified:	April 3, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents