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Database: UniProt
Entry: XDH1_HALVD
LinkDB: XDH1_HALVD
Original site: XDH1_HALVD 
ID   XDH1_HALVD              Reviewed;         390 AA.
AC   D4GP29;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=D-xylose 1-dehydrogenase [NADP(+)] 1;
DE            Short=XDH 1;
DE            EC=1.1.1.424 {ECO:0000269|PubMed:28854683, ECO:0000305|PubMed:19584053};
DE   Flags: Precursor;
GN   Name=xacA {ECO:0000303|PubMed:25141768}; OrderedLocusNames=HVO_B0028;
GN   ORFNames=C498_01615;
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, SUBUNIT,
RP   INDUCTION, AND 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).
RN   [4]
RP   INDUCTION.
RX   PubMed=25141768; DOI=10.1111/1462-2920.12603;
RA   Johnsen U., Sutter J.M., Schulz A.C., Taestensen J.B., Schoenheit P.;
RT   "XacR - a novel transcriptional regulator of D-xylose and L-arabinose
RT   catabolism in the haloarchaeon Haloferax volcanii.";
RL   Environ. Microbiol. 17:1663-1676(2015).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DS2 / DS70 / H26;
RX   PubMed=28854683; DOI=10.1093/femsle/fnx140;
RA   Sutter J.M., Johnsen U., Schoenheit P.;
RT   "Characterization of a pentonolactonase involved in D-xylose and L-
RT   arabinose catabolism in the haloarchaeon Haloferax volcanii.";
RL   FEMS Microbiol. Lett. 364:0-0(2017).
CC   -!- FUNCTION: NADP-dependent D-xylose dehydrogenase involved in the
CC       degradation of D-xylose, a major component of hemicelluloses such as
CC       xylan. Catalyzes the initial reaction in the xylose utilization pathway
CC       by oxydizing D-xylose into D-xylonolactone.
CC       {ECO:0000269|PubMed:19584053, ECO:0000269|PubMed:28854683}.
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:28854683,
CC         ECO:0000305|PubMed:19584053};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.7 mM for D-xylose {ECO:0000269|PubMed:19584053};
CC         KM=198 mM for D-glucose {ECO:0000269|PubMed:19584053};
CC         KM=0.36 mM for NAD(+) {ECO:0000269|PubMed:19584053};
CC         KM=0.031 mM for NADP(+) {ECO:0000269|PubMed:19584053};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19584053}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- INDUCTION: Transcriptionally up-regulated by both L-arabinose and D-
CC       xylose via the pentose-specific regulator XacR.
CC       {ECO:0000269|PubMed:19584053, ECO:0000269|PubMed:25141768}.
CC   -!- DISRUPTION PHENOTYPE: Impairs growth on D-xylose as sole energy and
CC       carbon substrate. {ECO:0000269|PubMed:19584053}.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR   EMBL; CP001953; ADE01534.1; -; Genomic_DNA.
DR   EMBL; AOHU01000021; ELY36803.1; -; Genomic_DNA.
DR   RefSeq; WP_004041126.1; NZ_AOHU01000021.1.
DR   AlphaFoldDB; D4GP29; -.
DR   SMR; D4GP29; -.
DR   PaxDb; 309800-C498_01615; -.
DR   EnsemblBacteria; ADE01534; ADE01534; HVO_B0028.
DR   GeneID; 8919161; -.
DR   KEGG; hvo:HVO_B0028; -.
DR   PATRIC; fig|309800.29.peg.309; -.
DR   eggNOG; arCOG01622; Archaea.
DR   HOGENOM; CLU_023194_5_1_2; -.
DR   OMA; INMNYLQ; -.
DR   OrthoDB; 195534at2157; -.
DR   BioCyc; MetaCyc:MONOMER-16373; -.
DR   BRENDA; 1.1.1.179; 2561.
DR   BRENDA; 1.1.1.424; 2561.
DR   SABIO-RK; D4GP29; -.
DR   Proteomes; UP000008243; Plasmid pHV3.
DR   Proteomes; UP000011532; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   NCBIfam; NF041392; XylDh_Gfo6_Halo; 1.
DR   PANTHER; PTHR22604; OXIDOREDUCTASES; 1.
DR   PANTHER; PTHR22604:SF105; TRANS-1,2-DIHYDROBENZENE-1,2-DIOL DEHYDROGENASE; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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..390
FT                   /note="D-xylose 1-dehydrogenase [NADP(+)] 1"
FT                   /id="PRO_0000428797"
FT   REGION          361..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  42307 MW;  64AC8E2E5479700F CRC64;
     MSPAPTDIVE EFTRRDWQGD DVTGTVRVAM IGLGWWTRDE AIPAVEASEF CETTVVVSSS
     KEKAEGATAL TESITHGLTY DEFHEGVAAD AYDAVYVVTP NGLHLPYVET AAELGKAVLC
     EKPLEASVER AEKLVAACDR ADVPLMVAYR MQTEPAVRRA RELVEAGVIG EPVFVHGHMS
     QRLLDEVVPD PDQWRLDPEL SGGATVMDIG LYPLNTARFV LDADPVRVRA TARVDDEAFE
     AVGDEHVSFG VDFDDGTLAV CTASQSAYQL SHLRVTGTEG ELEIEPAFYN RQKRGFRLSW
     GDQSADYDFE QVNQMTEEFD YFASRLLSDS DPAPDGDHAL VDMRAMDAIY AAAERGTDVA
     VDAADSDSAD SDSADAAAAN HDADPDSDGT
//
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