LAD_PENRW
ID LAD_PENRW Reviewed; 385 AA.
AC B6HI95;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=L-arabinitol 4-dehydrogenase;
DE Short=LAD;
DE EC=1.1.1.12 {ECO:0000269|PubMed:20414651};
GN Name=lad1; ORFNames=Pc21g23190;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF
RP 212-ASP-ILE-213 AND SER-358, ZINC-BINDING, AND CATALYTIC ACTIVITY.
RX PubMed=20414651; DOI=10.1007/s00253-010-2593-4;
RA Kim B., Sullivan R.P., Zhao H.;
RT "Cloning, characterization, and engineering of fungal L-arabinitol
RT dehydrogenases.";
RL Appl. Microbiol. Biotechnol. 87:1407-1414(2010).
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation of L-arabinitol to L-
CC xylulose in the fungal L-arabinose catabolic pathway. L-arabinose
CC catabolism is important for using plant material as a carbon source.
CC NADP cannot act as a cosubstrate. {ECO:0000269|PubMed:20414651}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arabinitol + NAD(+) = H(+) + L-xylulose + NADH;
CC Xref=Rhea:RHEA:16381, ChEBI:CHEBI:15378, ChEBI:CHEBI:17399,
CC ChEBI:CHEBI:18403, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.12;
CC Evidence={ECO:0000269|PubMed:20414651};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:20414651};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:20414651};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37 mM for L-arabinitol (at pH 7) {ECO:0000269|PubMed:20414651};
CC KM=300 uM for NAD (at pH 7) {ECO:0000269|PubMed:20414651};
CC pH dependence:
CC Optimum pH is 9.4. Active from pH 7 to pH 11.
CC {ECO:0000269|PubMed:20414651};
CC Temperature dependence:
CC Optimum temperature is 40-50 degrees Celsius.
CC {ECO:0000269|PubMed:20414651};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route):
CC step 2/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20414651}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AM920436; CAP97216.1; -; Genomic_DNA.
DR RefSeq; XP_002569286.1; XM_002569240.1.
DR AlphaFoldDB; B6HI95; -.
DR SMR; B6HI95; -.
DR STRING; 1108849.XP_002569286.1; -.
DR EnsemblFungi; CAP97216; CAP97216; PCH_Pc21g23190.
DR GeneID; 8310191; -.
DR KEGG; pcs:Pc21g23190; -.
DR VEuPathDB; FungiDB:PCH_Pc21g23190; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_5_1; -.
DR OMA; VGKNEMT; -.
DR OrthoDB; 1019156at2759; -.
DR BioCyc; PCHR:PC21G23190-MON; -.
DR BRENDA; 1.1.1.12; 4606.
DR UniPathway; UPA00146; UER00575.
DR Proteomes; UP000000724; Contig Pc00c21.
DR GO; GO:0050019; F:L-arabinitol 4-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniPathway.
DR CDD; cd05285; sorbitol_DH; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR045306; SDH-like.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Arabinose catabolism; Carbohydrate metabolism; Metal-binding; NAD;
KW Nucleotide-binding; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..385
FT /note="L-arabinitol 4-dehydrogenase"
FT /id="PRO_0000418407"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 191..192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 316..318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MUTAGEN 212..213
FT /note="DI->SR: Alters cofactor specificity from NAD to
FT NADP; when associated with T-358."
FT /evidence="ECO:0000269|PubMed:20414651"
FT MUTAGEN 358
FT /note="S->T: Alters cofactor specificity from NAD to NADP;
FT when associated with 212-SR-213."
FT /evidence="ECO:0000269|PubMed:20414651"
SQ SEQUENCE 385 AA; 41030 MW; E1E063C41F883A00 CRC64;
MASATVTKTN IGVYTNPKHD LWIADSSPTA EDINAGKGLK AGEVTIEVRS TGICGSDVHF
WHAGCIGPMI VTGDHVLGHE SAGQVLAVAP DVTHLKVGDR VAVEPNVICN ACEPCLTGRY
NGCVNVAFLS TPPVDGLLRR YVNHPAVWCH KIGDMSYEDG AMLEPLSVTL AAIERSGLRL
GDPLLITGAG PIGLISLLSA RAAGACPIVI TDIDEGRLAF AKSLVPEVRT YKVEIGKSAE
ECADGIINAL NDGQGSGPDA LRPKLALECT GVESSVNSAI WSVKFGGKVF VIGVGKNEMT
IPFMRLSTQE IDLQYQYRYC NTWPRAIRLI QNGVIDLSKL VTHRYSLENA LQAFETASNP
KTGAIKVQIM SSEEDVKAAT AGQKY
