RM1DH_PICST
ID RM1DH_PICST Reviewed; 258 AA.
AC A3LZU7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=L-rhamnose-1-dehydrogenase;
DE EC=1.1.1.173;
GN Name=DHG2; Synonyms=RHA1; ORFNames=PICST_50944;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18400031; DOI=10.1111/j.1742-4658.2008.06392.x;
RA Koivistoinen O.M., Hilditch S., Voutilainen S.P., Boer H., Penttila M.,
RA Richard P.;
RT "Identification in the yeast Pichia stipitis of the first L-rhamnose-1-
RT dehydrogenase gene.";
RL FEBS J. 275:2482-2488(2008).
RN [3]
RP CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION
RP OF GENE CLUSTER, INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18505728; DOI=10.1074/jbc.m801065200;
RA Watanabe S., Saimura M., Makino K.;
RT "Eukaryotic and bacterial gene clusters related to an alternative pathway
RT of nonphosphorylated L-rhamnose metabolism.";
RL J. Biol. Chem. 283:20372-20382(2008).
CC -!- FUNCTION: NAD-dependent dehydrogenase that has high activity with L-
CC rhamnose and L-lyxose, and shows only low activity with L-mannose. Has
CC no activity with NADP. Catalyzes the first step in an alternative
CC pathway for rhamnose utilization that does not involve phosphorylated
CC intermediates. {ECO:0000269|PubMed:18400031}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-rhamnofuranose + NAD(+) = H(+) + L-rhamnono-1,4-lactone +
CC NADH; Xref=Rhea:RHEA:12649, ChEBI:CHEBI:15378, ChEBI:CHEBI:16935,
CC ChEBI:CHEBI:17937, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.173; Evidence={ECO:0000269|PubMed:18400031,
CC ECO:0000269|PubMed:18505728};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for NAD {ECO:0000269|PubMed:18400031,
CC ECO:0000269|PubMed:18505728};
CC KM=1.7 mM for L-rhamnose {ECO:0000269|PubMed:18400031,
CC ECO:0000269|PubMed:18505728};
CC KM=4.7 mM for L-lyxose {ECO:0000269|PubMed:18400031,
CC ECO:0000269|PubMed:18505728};
CC KM=41 mM for L-mannose {ECO:0000269|PubMed:18400031,
CC ECO:0000269|PubMed:18505728};
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:18400031,
CC ECO:0000269|PubMed:18505728};
CC -!- INDUCTION: Up-regulated by growth on rhamnose.
CC {ECO:0000269|PubMed:18400031, ECO:0000269|PubMed:18505728}.
CC -!- MISCELLANEOUS: Part of gene cluster that contains the genes for this
CC rhamnose catabolic pathway.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; CP000502; ABN68405.2; -; Genomic_DNA.
DR RefSeq; XP_001386434.2; XM_001386397.1.
DR AlphaFoldDB; A3LZU7; -.
DR SMR; A3LZU7; -.
DR STRING; 4924.XP_001386434.2; -.
DR EnsemblFungi; ABN68405; ABN68405; PICST_50944.
DR GeneID; 4840981; -.
DR KEGG; pic:PICST_50944; -.
DR eggNOG; KOG1200; Eukaryota.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; A3LZU7; -.
DR OMA; GICEFKE; -.
DR OrthoDB; 1134303at2759; -.
DR BioCyc; MetaCyc:MON-16227; -.
DR Proteomes; UP000002258; Chromosome 8.
DR GO; GO:0050034; F:L-rhamnose 1-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0019301; P:rhamnose catabolic process; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome; Rhamnose metabolism.
FT CHAIN 1..258
FT /note="L-rhamnose-1-dehydrogenase"
FT /id="PRO_0000418398"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 11..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 38..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 67..69
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 161..165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 194..196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 258 AA; 27207 MW; C2A879B244359A72 CRC64;
MTGLLNGKVV AITGGVTGIG RAIAIEMARN GAKVVVNHLP SEEQAQLAKE LKEEISDGEN
NVLTIPGDIS LPETGRRIVE LAVEKFGEIN VFVSNAGVCG FREFLEITPE TLFQTVNINL
NGAFFAIQAA AQQMVKQGKG GSIIGISSIS ALVGGAHQTH YTPTKAGILS LMQSTACALG
KYGIRCNAIL PGTISTALNE EDLKDPEKRK YMEGRIPLGR VGDPKDIAGP AIFLASDMSN
YVNGAQLLVD GGLFVNLQ
