ID   XDH2_HALVD              Reviewed;         325 AA.
AC   D4GP30;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=D-xylose 1-dehydrogenase (NADP(+)) 2;
DE            Short=XDH 2;
DE            EC=1.1.1.179;
DE   Flags: Precursor;
GN   OrderedLocusNames=HVO_B0029; ORFNames=C498_01610;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG   Plasmid pHV3.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=DS2 / DS70;
RX   PubMed=19584053; DOI=10.1074/jbc.m109.003814;
RA   Johnsen U., Dambeck M., Zaiss H., Fuhrer T., Soppa J., Sauer U.,
RA   Schonheit P.;
RT   "D-xylose degradation pathway in the halophilic archaeon Haloferax
RT   volcanii.";
RL   J. Biol. Chem. 284:27290-27303(2009).
CC   -!- FUNCTION: NADP-dependent D-xylose dehydrogenase involved in the
CC       degradation of D-xylose, a major component of hemicelluloses such as
CC       xylan. Even if it shows D-xylose dehydrogenase activity, it is not
CC       essential for D-xylose degradation. {ECO:0000269|PubMed:19584053}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-xylose + NADP(+) = D-xylono-1,5-lactone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:22000, ChEBI:CHEBI:15378, ChEBI:CHEBI:15867,
CC         ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.179; Evidence={ECO:0000269|PubMed:19584053};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=89 mM for D-xylose {ECO:0000269|PubMed:19584053};
CC         KM=0.75 mM for NADP {ECO:0000269|PubMed:19584053};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- INDUCTION: Expression is highly induced during growth on D-xylose.
CC       {ECO:0000269|PubMed:19584053}.
CC   -!- DISRUPTION PHENOTYPE: Does not affect growth on D-xylose as sole energy
CC       and carbon substrate. {ECO:0000269|PubMed:19584053}.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR   EMBL; CP001953; ADE01305.1; -; Genomic_DNA.
DR   EMBL; AOHU01000021; ELY36802.1; -; Genomic_DNA.
DR   RefSeq; WP_004041125.1; NZ_AOHU01000021.1.
DR   AlphaFoldDB; D4GP30; -.
DR   SMR; D4GP30; -.
DR   STRING; 309800.C498_01610; -.
DR   EnsemblBacteria; ADE01305; ADE01305; HVO_B0029.
DR   EnsemblBacteria; ELY36802; ELY36802; C498_01610.
DR   GeneID; 8919277; -.
DR   KEGG; hvo:HVO_B0029; -.
DR   PATRIC; fig|309800.29.peg.308; -.
DR   eggNOG; arCOG01622; Archaea.
DR   HOGENOM; CLU_023194_5_0_2; -.
DR   OMA; FINYCQY; -.
DR   OrthoDB; 39139at2157; -.
DR   BRENDA; 1.1.1.179; 2561.
DR   SABIO-RK; D4GP30; -.
DR   Proteomes; UP000008243; Plasmid pHV3.
DR   Proteomes; UP000011532; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0047837; F:D-xylose 1-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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   NADP; Oxidoreductase; Plasmid; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..325
FT                   /note="D-xylose 1-dehydrogenase (NADP(+)) 2"
FT                   /id="PRO_0000428798"
SQ   SEQUENCE   325 AA;  34719 MW;  7A65AFF0D7580401 CRC64;
     MMFGILGTAG IGVKSVIPAV QASEHEAAAI ASRDEARASA VADELGIPTA YGSYEALLAD
     DSLDAVYIPL PNGLHADWVR AAADRGLHVL CEKPLTASAD ETAAVFDYCE DAGVTLMEAF
     MYRFHPLTER AAELVASELG AVVSVTSNFS FRLPDGADDI RIDPDLAGGS VMDVGCYAVS
     AARLFLGTPD RVYATTTDTR DCGVDTRMSG VLEYDSGATA RVESSFDTPE TQYYRVQTTD
     GRLEANPAFN VDPTAAAELT YATDGRVVTE TFDPTDSYRR EVEAFARAVE TGETPRVDRE
     ESVSVMRTID AIYESAETGA AVELD