XDH_PAENI
ID XDH_PAENI Reviewed; 388 AA.
AC Q8GAK6;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=D-xylose dehydrogenase;
DE EC=1.1.1.179 {ECO:0000269|PubMed:23063486};
DE AltName: Full=NADP-dependent D-xylose dehydrogenase;
GN Name=xdh; ORFNames=ORF40;
OS Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans).
OG Plasmid pAO1.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=29320;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49919 / DSM 420 / JCM 3874 / NBRC 15511; PLASMID=pAO1;
RX PubMed=12618462; DOI=10.1128/jb.185.6.1976-1986.2003;
RA Igloi G.L., Brandsch R.;
RT "Sequence of the 165-kilobase catabolic plasmid pAO1 from Arthrobacter
RT nicotinovorans and identification of a pAO1-dependent nicotine uptake
RT system.";
RL J. Bacteriol. 185:1976-1986(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, KINETIC
RP PARAMETERS, SUBUNIT, PATHWAY, AND INDUCTION.
RC STRAIN=ATCC 49919 / DSM 420 / JCM 3874 / NBRC 15511; PLASMID=pAO1;
RX PubMed=23063486; DOI=10.1016/j.resmic.2012.10.003;
RA Mihasan M., Stefan M., Hritcu L., Artenie V., Brandsch R.;
RT "Evidence of a plasmid-encoded oxidative xylose-catabolic pathway in
RT Arthrobacter nicotinovorans pAO1.";
RL Res. Microbiol. 164:22-30(2013).
CC -!- FUNCTION: Catalyzes the NADP(+)-dependent oxidation of D-xylose. Is
CC able to use both NADP(+) and NAD(+); however, the enzyme shows a very
CC strong preference for NADP(+). Is likely involved in the first step of
CC the oxidative D-xylose degradation pathway.
CC {ECO:0000269|PubMed:23063486}.
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:23063486};
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 Evidence={ECO:0000269|PubMed:23063486};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:23063486};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:23063486};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.2 mM for D-xylose {ECO:0000269|PubMed:23063486};
CC KM=0.32 mM for NADP(+) {ECO:0000269|PubMed:23063486};
CC KM=5.03 mM for NAD(+) {ECO:0000269|PubMed:23063486};
CC Note=kcat is 14.9 sec(-1).;
CC -!- PATHWAY: Carbohydrate metabolism; D-xylose degradation.
CC {ECO:0000269|PubMed:23063486}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:23063486}.
CC -!- INDUCTION: Is induced by D-xylose. No significant levels of expression
CC can detected when the cells are grown on various other sugars such as
CC L-xylose, L-arabinose, D-galactose, D-tagatose and D-glucose.
CC {ECO:0000269|PubMed:23063486}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; AJ507836; CAD47898.1; -; Genomic_DNA.
DR RefSeq; WP_016359409.1; NC_021229.1.
DR RefSeq; YP_007988724.1; NC_021229.1.
DR AlphaFoldDB; Q8GAK6; -.
DR SMR; Q8GAK6; -.
DR STRING; 1304876.AZVC01000007_gene81; -.
DR eggNOG; COG0673; Bacteria.
DR SABIO-RK; Q8GAK6; -.
DR UniPathway; UPA00810; -.
DR GO; GO:0047838; F:D-xylose 1-dehydrogenase (NAD) activity; IEA:RHEA.
DR GO; GO:0047837; F:D-xylose 1-dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0042843; P:D-xylose catabolic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
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 Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Plasmid.
FT CHAIN 1..388
FT /note="D-xylose dehydrogenase"
FT /id="PRO_0000429428"
SQ SEQUENCE 388 AA; 43189 MW; 622407EE3EFE4871 CRC64;
MTKTAIVRVA MNGITGRMGY RQHLLRSILP IRDAGGFTLE DGTKVQIEPI LVGRNEAKIR
ELAEKHKVAE WSTDLDSVVN DPTVDIIFDA SMTSLRAATL KKAMLAGKHI FTEKPTAETL
EEAIELARIG KQAGVTAGVV HDKLYLPGLV KLRRLVDEGF FGRILSIRGE FGYWVFEGDV
QAAQRPSWNY RKEDGGGMTT DMFCHWNYVL EGIIGKVKSV NAKTATHIPT RWDEAGKEYK
ATADDASYGI FELETPGGDD VIGQINSSWA VRVYRDELVE FQVDGTHGSA VAGLNKCVAQ
QRAHTPKPVW NPDLPVTESF RDQWQEVPAN AELDNGFKLQ WEEFLRDVVA GREHRFGLLS
AARGVQLAEL GLQSNDERRT IDIPEITL
