ID   XDH_CAUVN               Reviewed;         248 AA.
AC   B8H1Z0;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=D-xylose 1-dehydrogenase;
DE            Short=XDH;
DE            EC=1.1.1.175;
GN   Name=xylB; OrderedLocusNames=CCNA_00864;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=17172333; DOI=10.1128/jb.01438-06;
RA   Stephens C., Christen B., Fuchs T., Sundaram V., Watanabe K., Jenal U.;
RT   "Genetic analysis of a novel pathway for D-xylose metabolism in Caulobacter
RT   crescentus.";
RL   J. Bacteriol. 189:2181-2185(2007).
CC   -!- FUNCTION: D-xylose dehydrogenase involved in the degradation of D-
CC       xylose, a major component of hemicelluloses such as xylan. Catalyzes
CC       the initial reaction in the xylose utilization pathway by oxydizing D-
CC       xylose into D-xylonolactone. Shows some activity toward L-arabinose,
CC       but little to none toward D-arabinose, L-xylose, D-ribose, D-galactose,
CC       D-glucose or D-glucose-6-phosphate. {ECO:0000269|PubMed:17172333}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-xylose + NAD(+) = D-xylono-1,5-lactone + H(+) + NADH;
CC         Xref=Rhea:RHEA:13861, ChEBI:CHEBI:15378, ChEBI:CHEBI:15867,
CC         ChEBI:CHEBI:53455, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.175; Evidence={ECO:0000269|PubMed:17172333};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.76 mM for D-xylose {ECO:0000269|PubMed:17172333};
CC         KM=166 mM for L-arabinose {ECO:0000269|PubMed:17172333};
CC         Vmax=27.5 umol/min/mg enzyme with D-xylose as substrate
CC         {ECO:0000269|PubMed:17172333};
CC         Vmax=20.05 umol/min/mg enzyme with L-arabinose as substrate
CC         {ECO:0000269|PubMed:17172333};
CC   -!- DISRUPTION PHENOTYPE: Impairs growth on D-xylose as sole energy and
CC       carbon substrate. {ECO:0000269|PubMed:17172333}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; CP001340; ACL94329.1; -; Genomic_DNA.
DR   RefSeq; WP_010918706.1; NC_011916.1.
DR   RefSeq; YP_002516237.1; NC_011916.1.
DR   AlphaFoldDB; B8H1Z0; -.
DR   SMR; B8H1Z0; -.
DR   PRIDE; B8H1Z0; -.
DR   EnsemblBacteria; ACL94329; ACL94329; CCNA_00864.
DR   GeneID; 7329904; -.
DR   KEGG; ccs:CCNA_00864; -.
DR   PATRIC; fig|565050.3.peg.851; -.
DR   HOGENOM; CLU_010194_1_0_5; -.
DR   OMA; TGEMMRV; -.
DR   OrthoDB; 1601931at2; -.
DR   PhylomeDB; B8H1Z0; -.
DR   BRENDA; 1.1.1.175; 1218.
DR   SABIO-RK; B8H1Z0; -.
DR   Proteomes; UP000001364; Chromosome.
DR   GO; GO:0047838; F:D-xylose 1-dehydrogenase (NAD) activity; IEA:UniProtKB-EC.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..248
FT                   /note="D-xylose 1-dehydrogenase"
FT                   /id="PRO_0000428802"
FT   ACT_SITE        156
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         14..39
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   248 AA;  26641 MW;  45AEA26019C09AEA CRC64;
     MSSAIYPSLK GKRVVITGGG SGIGAGLTAG FARQGAEVIF LDIADEDSRA LEAELAGSPI
     PPVYKRCDLM NLEAIKAVFA EIGDVDVLVN NAGNDDRHKL ADVTGAYWDE RINVNLRHML
     FCTQAVAPGM KKRGGGAVIN FGSISWHLGL EDLVLYETAK AGIEGMTRAL ARELGPDDIR
     VTCVVPGNVK TKRQEKWYTP EGEAQIVAAQ CLKGRIVPEN VAALVLFLAS DDASLCTGHE
     YWIDAGWR