ALX1_AMBMO
ID ALX1_AMBMO Reviewed; 272 AA.
AC Q70FD1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=NADH-dependent L-xylulose reductase {ECO:0000303|PubMed:14736891};
DE EC=1.1.1.15 {ECO:0000269|PubMed:14736891};
DE EC=1.1.1.250 {ECO:0000269|PubMed:14736891};
GN Name=ALX1 {ECO:0000303|PubMed:14736891};
OS Ambrosiozyma monospora (Yeast) (Endomycopsis monosporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Ambrosiozyma.
OX NCBI_TaxID=43982;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND INDUCTION.
RC STRAIN=ATCC 56618 / CBS 2554 / JCM 7599 / NRRL Y-1484 / Goto TH-2;
RX PubMed=14736891; DOI=10.1074/jbc.m312533200;
RA Verho R., Putkonen M., Londesborough J., Penttila M., Richard P.;
RT "A novel NADH-linked l-xylulose reductase in the l-arabinose catabolic
RT pathway of yeast.";
RL J. Biol. Chem. 279:14746-14751(2004).
CC -!- FUNCTION: NADH-dependent L-xylulose reductase; part of the yeast
CC pathway for L-arabinose catabolism (PubMed:14736891). Reversibly
CC converts L-xylulose to xylitol and D-ribulose to D-arabinitol
CC (PubMed:14736891). It has a much lower activity with D-xylulose
CC (PubMed:14736891). Sugar alcohols can serve as a substrate when the
CC hydroxyl group of C-2 is in the L- and the hydroxyl group of the C-3 is
CC in the D-configuration (PubMed:14736891). Seems also to be specific for
CC sugar alcohols that have not more than 5 carbons since no activity is
CC observed with dulcitol (galactitol), which has the hydroxyl group of C-
CC 2 in L- and of C-3 in D-configuration, but is a six-carbon sugar
CC alcohol (PubMed:14736891). {ECO:0000269|PubMed:14736891}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + xylitol = H(+) + L-xylulose + NADH;
CC Xref=Rhea:RHEA:68100, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC ChEBI:CHEBI:17399, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.15;
CC Evidence={ECO:0000269|PubMed:14736891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68101;
CC Evidence={ECO:0000269|PubMed:14736891};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68102;
CC Evidence={ECO:0000269|PubMed:14736891};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinitol + NAD(+) = D-ribulose + H(+) + NADH;
CC Xref=Rhea:RHEA:17389, ChEBI:CHEBI:15378, ChEBI:CHEBI:17173,
CC ChEBI:CHEBI:18333, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.250; Evidence={ECO:0000269|PubMed:14736891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17390;
CC Evidence={ECO:0000269|PubMed:14736891};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17391;
CC Evidence={ECO:0000269|PubMed:14736891};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.6 mM for L-xylulose {ECO:0000269|PubMed:14736891};
CC KM=7.4 mM for D-ribulose {ECO:0000269|PubMed:14736891};
CC KM=0.3 mM for D-arabinitol {ECO:0000269|PubMed:14736891};
CC KM=7.2 mM for xylitol {ECO:0000269|PubMed:14736891};
CC Vmax=1.7 umol/sec/mg enzyme with L-xylulose as substrate
CC {ECO:0000269|PubMed:14736891};
CC Vmax=2.7 umol/sec/mg enzyme with D-ribulose as substrate
CC {ECO:0000269|PubMed:14736891};
CC Vmax=0.6 umol/sec/mg enzyme with D-arabinitol as substrate
CC {ECO:0000269|PubMed:14736891};
CC Vmax=0.63 umol/sec/mg enzyme with xylitol as substrate
CC {ECO:0000269|PubMed:14736891};
CC -!- INDUCTION: Strongly expressed during growth on L-arabinose.
CC {ECO:0000269|PubMed:14736891}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ583159; CAE47547.1; -; mRNA.
DR BRENDA; 1.1.1.10; 7272.
DR GO; GO:0047038; F:D-arabinitol 2-dehydrogenase activity; IDA:GO_Central.
DR GO; GO:0044105; F:L-xylulose reductase (NAD+) activity; IDA:GO_Central.
DR GO; GO:0019572; P:L-arabinose catabolic process; IDA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase.
FT CHAIN 1..272
FT /note="NADH-dependent L-xylulose reductase"
FT /id="PRO_0000454240"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 16..24
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 66..79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 175..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 208..210
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 272 AA; 29636 MW; 3338DEB95ECC473D CRC64;
MTDYIPTFRF DGHLTIVTGA CGGLAEALIK GLLAYGSDIA LLDIDQEKTA AKQAEYHKYA
TEELKLKEVP KMGSYACDIS DSDTVHKVFA QVAKDFGKLP LHLVNTAGYC ENFPCEDYPA
KNAEKMVKVN LLGSLYVSQA FAKPLIKEGI KGASVVLIGS MSGAIVNDPQ NQVVYNMSKA
GVIHLAKTLA CEWAKYNIRV NSLNPGYIYG PLTKNVINGN EELYNRWISG IPQQRMSEPK
EYIGAVLYLL SESAASYTTG ASLLVDGGFT SW
