GFO6_HALMA
ID GFO6_HALMA Reviewed; 360 AA.
AC Q5UY95; Q5EC62;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=D-xylose 1-dehydrogenase [NADP(+)];
DE Short=XDH;
DE EC=1.1.1.424 {ECO:0000269|PubMed:15342590};
GN Name=gfo6; Synonyms=xdh; OrderedLocusNames=rrnAC3034;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19, SUBUNIT,
RP INDUCTION, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15342590; DOI=10.1128/jb.186.18.6198-6207.2004;
RA Johnsen U., Schonheit P.;
RT "Novel xylose dehydrogenase in the halophilic archaeon Haloarcula
RT marismortui.";
RL J. Bacteriol. 186:6198-6207(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
CC -!- FUNCTION: NADP-dependent D-xylose dehydrogenase involved in the
CC degradation of D-xylose, a major component of hemicelluloses such as
CC xylan. In addition to D-xylose, oxidizes D-ribose at similar kinetic
CC constants, whereas D-glucose is oxidized with about 70-fold lower
CC catalytic efficiency. {ECO:0000269|PubMed:15342590}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylofuranose + NADP(+) = D-xylono-1,4-lactone + H(+) +
CC NADPH; Xref=Rhea:RHEA:64416, ChEBI:CHEBI:15378, ChEBI:CHEBI:16392,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:146758;
CC EC=1.1.1.424; Evidence={ECO:0000269|PubMed:15342590};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for D-xylose {ECO:0000269|PubMed:15342590};
CC KM=2.3 mM for D-ribose {ECO:0000269|PubMed:15342590};
CC KM=64 mM for D-glucose {ECO:0000269|PubMed:15342590};
CC KM=0.15 mM for NADP(+) {ECO:0000269|PubMed:15342590};
CC KM=0.9 mM for NAD(+) {ECO:0000269|PubMed:15342590};
CC Vmax=100 umol/min/mg enzyme toward D-xylose
CC {ECO:0000269|PubMed:15342590};
CC Vmax=82 umol/min/mg enzyme toward D-ribose
CC {ECO:0000269|PubMed:15342590};
CC Vmax=39 umol/min/mg enzyme toward D-glucose
CC {ECO:0000269|PubMed:15342590};
CC Vmax=2 umol/min/mg enzyme toward D-fructose
CC {ECO:0000269|PubMed:15342590};
CC Vmax=1 umol/min/mg enzyme toward D-arabinose
CC {ECO:0000269|PubMed:15342590};
CC Vmax=92 umol/min/mg enzyme toward NADP(+)
CC {ECO:0000269|PubMed:15342590};
CC Vmax=80 umol/min/mg enzyme toward NAD(+)
CC {ECO:0000269|PubMed:15342590};
CC pH dependence:
CC Optimum pH is 8.3. {ECO:0000269|PubMed:15342590};
CC -!- SUBUNIT: Homotretramer. {ECO:0000269|PubMed:15342590}.
CC -!- INDUCTION: Expression is induced during growth on D-xylose.
CC {ECO:0000269|PubMed:15342590}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; AY911409; AAW78223.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV47758.1; -; Genomic_DNA.
DR RefSeq; WP_004964872.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5UY95; -.
DR SMR; Q5UY95; -.
DR STRING; 272569.rrnAC3034; -.
DR DNASU; 3130318; -.
DR EnsemblBacteria; AAV47758; AAV47758; rrnAC3034.
DR GeneID; 40153860; -.
DR GeneID; 64823732; -.
DR KEGG; hma:rrnAC3034; -.
DR PATRIC; fig|272569.17.peg.3586; -.
DR eggNOG; arCOG01622; Archaea.
DR HOGENOM; CLU_023194_5_1_2; -.
DR OMA; LMVHENF; -.
DR BioCyc; MetaCyc:MON-16385; -.
DR BRENDA; 1.1.1.179; 2549.
DR BRENDA; 1.1.1.424; 2549.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..360
FT /note="D-xylose 1-dehydrogenase [NADP(+)]"
FT /id="PRO_0000428910"
SQ SEQUENCE 360 AA; 39937 MW; B28C3F3EA5642B0B CRC64;
MNVDALTGGF DRRDWQEQTA TDNPVRFAMI GVGWWTTEQA MPAVDAGDLC ETTVLVSSDR
EKAADVAADS ETVEHAITYE EFHDGAASDA YDAVYIVTPN ALHLPYVETA AELDKAILCE
KPMEATIERA ERMVEVCDEH DATLMIAYRM HTEPAVRRAK DLIDEGYIGE PLFVHGNMTE
PILELVPDPD QWRLDGELSG GCAVMDIGIY PLNTSRFLLD ADPVAVRGTV ASVQEEFADV
PDEHGAFQLD FPGHVYAVCT ASQNAHLDSH ISVLGTEGKV RVEPAFYPWD DRALQLSHEG
TTVEIDFEQI DQMEEEFEYF AHCLLTDTEP YADGEHGLVD INTIKSVYEA SETESTVRLD
