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 03-AUG-2022, entry version 67.
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 STRING; 309800.C498_01615; -.
DR EnsemblBacteria; ADE01534; ADE01534; HVO_B0028.
DR EnsemblBacteria; ELY36803; ELY36803; C498_01615.
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; 39139at2157; -.
DR BioCyc; MetaCyc:MON-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 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..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
