LAD_TALEM
ID LAD_TALEM Reviewed; 388 AA.
AC C5J3R8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=L-arabinitol 4-dehydrogenase;
DE Short=LAD;
DE EC=1.1.1.12;
GN Name=lad;
OS Talaromyces emersonii (Thermophilic fungus) (Rasamsonia emersonii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=68825;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=20111899; DOI=10.1007/s10528-010-9332-5;
RA Fernandes S., Tuohy M.G., Murray P.G.;
RT "Cloning, heterologous expression, and characterization of the xylitol and
RT L-arabitol dehydrogenase genes, Texdh and Telad, from the thermophilic
RT fungus Talaromyces emersonii.";
RL Biochem. Genet. 48:480-495(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:20111899}.
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:20111899};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.4 mM for L-arabinitol {ECO:0000269|PubMed:20111899};
CC KM=23.3 mM for D-xylitol {ECO:0000269|PubMed:20111899};
CC KM=483.5 mM for D-sorbitol {ECO:0000269|PubMed:20111899};
CC KM=60 uM for NAD {ECO:0000269|PubMed:20111899};
CC pH dependence:
CC Optimum pH is 9. Active from pH 7 to pH 11.
CC {ECO:0000269|PubMed:20111899};
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:0000250}.
CC -!- INDUCTION: Induced by L-arabinose, D-xylose, xylitol, L-arabinitol, and
CC galactitol. {ECO:0000269|PubMed:20111899}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; FJ985742; ACR78270.1; -; Genomic_DNA.
DR AlphaFoldDB; C5J3R8; -.
DR SMR; C5J3R8; -.
DR BRENDA; 1.1.1.12; 6211.
DR UniPathway; UPA00146; UER00575.
DR GO; GO:0050019; F:L-arabinitol 4-dehydrogenase activity; IEA:UniProtKB-EC.
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; Zinc.
FT CHAIN 1..388
FT /note="L-arabinitol 4-dehydrogenase"
FT /id="PRO_0000418408"
FT BINDING 55
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 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 192..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 317..319
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 388 AA; 41389 MW; 47FA6ACFAC615468 CRC64;
MAAGISLTKP NIGVYTNPNH DLWVADAKPT LEEVKSGSDL KPGQVTVEIR STGICGSDVH
FWHAGCIGPM IVTGDHILGH ESAGVVIAVA PDVKTLKPGD RVAIEPNIIC NKCEPCLTGR
YNGCEAVEFL STPPVDGLLR RYVNHPAIWC HKIGDMSFED GALLEPLSVA LAGMDRAGVR
LGDPVLVAGA GPIGLVTLLC VRAAGATPIV ITDIDEGRLR FAKELVPEVR TYRVQTGLSA
EENAAGILDA LNDGNGSAPD AIRPRVAMEC TGVESSVASA IWSVKFGGKV FVIGVGKNEM
KVPFMRLSTW EIDLQYQYRY CNTWPKAIRL VKNGVINLKK LVTHRFPLED AVKAFETAAN
PKTGAIKVQI MSSEEDIKAA SGVNGASN
