RHAD_THEAC
ID RHAD_THEAC Reviewed; 254 AA.
AC Q9HK58; G3LGQ3;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=L-rhamnose 1-dehydrogenase (NADP(+)) {ECO:0000303|PubMed:22481639};
DE Short=RHAD {ECO:0000303|PubMed:22481639};
DE EC=1.1.1.377 {ECO:0000269|PubMed:22481639};
GN Name=rhaD {ECO:0000303|PubMed:22481639}; OrderedLocusNames=Ta0747;
GN ORFNames=Ta0747P;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RA Kim S.M., Paek K.H., Lee S.B.;
RT "Characterization of NADP-specific L-rhamnose dehydrogenase from the
RT hyperthermophilic archaeon Thermoplasma acidophilum.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=22481639; DOI=10.1007/s00792-012-0444-1;
RA Kim S.M., Paek K.H., Lee S.B.;
RT "Characterization of NADP+-specific L-rhamnose dehydrogenase from the
RT thermoacidophilic Archaeon Thermoplasma acidophilum.";
RL Extremophiles 16:447-454(2012).
CC -!- FUNCTION: Involved in the non-phosphorylated metabolic pathway of L-
CC rhamnose catabolism. Catalyzes the oxidation of L-rhamnose to yield L-
CC rhamnono-1,4-lactone. It can also oxidize L-lyxose and L-mannose, and
CC uses only NADP. {ECO:0000269|PubMed:22481639}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-rhamnofuranose + NADP(+) = H(+) + L-rhamnono-1,4-lactone +
CC NADPH; Xref=Rhea:RHEA:42668, ChEBI:CHEBI:15378, ChEBI:CHEBI:16935,
CC ChEBI:CHEBI:17937, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.377; Evidence={ECO:0000269|PubMed:22481639};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.10 mM for NADP (at pH 7 and 60 degrees Celsius)
CC {ECO:0000269|PubMed:22481639};
CC KM=0.46 mM for L-rhamnose (at pH 7 and 60 degrees Celsius)
CC {ECO:0000269|PubMed:22481639};
CC KM=1.37 mM for L-lyxose (at pH 7 and 60 degrees Celsius)
CC {ECO:0000269|PubMed:22481639};
CC KM=6.74 mM for L-mannose (at pH 7 and 60 degrees Celsius)
CC {ECO:0000269|PubMed:22481639};
CC Note=kcat is 1.341 min(-1) for dehydrogenase activity with L-rhamnose
CC as substrate (at pH 7 and 60 degrees Celsius). kcat is 1.426 min(-1)
CC for dehydrogenase activity with L-lyxose as substrate (at pH 7 and 60
CC degrees Celsius). kcat is 892.9 min(-1) for dehydrogenase activity
CC with L-mannose as substrate (at pH 7 and 60 degrees Celsius).
CC {ECO:0000269|PubMed:22481639};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:22481639};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:22481639};
CC -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC11881.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; JN375693; AEN94562.1; -; Genomic_DNA.
DR EMBL; AL445065; CAC11881.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048161762.1; NC_002578.1.
DR AlphaFoldDB; Q9HK58; -.
DR SMR; Q9HK58; -.
DR STRING; 273075.Ta0747; -.
DR PRIDE; Q9HK58; -.
DR EnsemblBacteria; CAC11881; CAC11881; CAC11881.
DR GeneID; 1456306; -.
DR KEGG; tac:Ta0747; -.
DR eggNOG; arCOG01259; Archaea.
DR HOGENOM; CLU_010194_1_1_2; -.
DR OrthoDB; 62124at2157; -.
DR BRENDA; 1.1.1.377; 6324.
DR UniPathway; UPA00541; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0019301; P:rhamnose catabolic process; IDA:UniProtKB.
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 PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome; Rhamnose metabolism.
FT CHAIN 1..254
FT /note="L-rhamnose 1-dehydrogenase (NADP(+))"
FT /id="PRO_0000431250"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 10..18
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 37..38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 63..65
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 190..192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 16
FT /note="Important for NADP specificity"
FT /evidence="ECO:0000303|PubMed:22481639"
SQ SEQUENCE 254 AA; 27939 MW; 6AB2FB5D37583E69 CRC64;
MLDFKGKNAV ITGGSRGIGR AIALGLAKQG ANILISYASH DSEADEVLET ASKYGVKAHK
VKVDQSDPYE SIRFAEKAIE TFGKVHILVD NAGICPFEDF FRISVDLFEK VWKVNVESHY
FITQRIAKNM IENKINGRIL LISSISAHVG GEFQTHYTTT KSALNGFMHS IAIVLGKYGI
LVNSLEPGTI LTDINKEDLS NQEKRAYMER RTVVGRLGLP EDMVAPALFL LSDDNTYVTG
TELLADGGML INLQ
