XAD_HALVD
ID XAD_HALVD Reviewed; 412 AA.
AC D4GP40;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=D-xylonate dehydratase;
DE Short=XAD;
DE EC=4.2.1.82;
GN Name=xacD {ECO:0000303|PubMed:25141768}; Synonyms=xad;
GN OrderedLocusNames=HVO_B0038A; ORFNames=C498_01565;
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 PROTEIN SEQUENCE OF 2-20, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, 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).
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 third reaction in the xylose utilization pathway
CC through dehydratation of D-xylonate into 2-dehydro-3-deoxy-D-xylonate.
CC {ECO:0000269|PubMed:19584053}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylonate = 2-dehydro-3-deoxy-D-arabinonate + H2O;
CC Xref=Rhea:RHEA:19157, ChEBI:CHEBI:15377, ChEBI:CHEBI:16699,
CC ChEBI:CHEBI:17746; EC=4.2.1.82;
CC Evidence={ECO:0000269|PubMed:19584053};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.55 mM for xylonate {ECO:0000269|PubMed:19584053};
CC KM=0.4 mM for gluconate {ECO:0000269|PubMed:19584053};
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:19584053}.
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}.
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DR EMBL; CP001953; ADE01444.1; -; Genomic_DNA.
DR EMBL; AOHU01000021; ELY36793.1; -; Genomic_DNA.
DR RefSeq; WP_004041116.1; NZ_AOHU01000021.1.
DR AlphaFoldDB; D4GP40; -.
DR SMR; D4GP40; -.
DR STRING; 309800.C498_01565; -.
DR DNASU; 8919180; -.
DR EnsemblBacteria; ADE01444; ADE01444; HVO_B0038A.
DR EnsemblBacteria; ELY36793; ELY36793; C498_01565.
DR GeneID; 8919180; -.
DR KEGG; hvo:HVO_B0038A; -.
DR PATRIC; fig|309800.29.peg.298; -.
DR eggNOG; arCOG01168; Archaea.
DR HOGENOM; CLU_030273_3_2_2; -.
DR OMA; WDYEYLW; -.
DR OrthoDB; 18921at2157; -.
DR BioCyc; MetaCyc:MON-16374; -.
DR BRENDA; 4.2.1.82; 2561.
DR SABIO-RK; D4GP40; -.
DR Proteomes; UP000008243; Plasmid pHV3.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0050401; F:xylonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR034593; Mandelate_racemase_DgoD-like.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR InterPro; IPR034624; Xylonate_dehydratase_2.
DR PANTHER; PTHR48080; PTHR48080; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDF00564; xylonate_dehydratase_2; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; Plasmid; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:19584053"
FT CHAIN 2..412
FT /note="D-xylonate dehydratase"
FT /id="PRO_0000428801"
SQ SEQUENCE 412 AA; 45529 MW; 63AD3C0162EF7A47 CRC64;
MVEQAKLSDP NAEYTMRDLS AETIDITNPR GGVRDAEITD VQTTMVDGNY PWILVRVYTD
AGVVGTGEAY WGGGDTAIIE RMKPFLVGEN PLDIDRLYEH LVQKMSGEGS VSGKVISAIS
GIEIALHDVA GKLLDVPAYQ LVGGKYRDEV RVYCDLHTED EANPQACAEE GVRVVEELGY
DAIKFDLDVP SGHEKDRANR HLRNPEIDHK VEIVEAVTEA VGDRADVAFD CHWSFTGGSA
KRLASELEDY DVWWLEDPVP PENHDVQKLV TQSTTTPIAV GENVYRKFGQ RTLLEPQAVD
IIAPDLPRVG GMRETRKIAD LADMYYIPVA MHNVSSPIGT MASAQVAAAI PNSLALEYHS
YQLGWWEDLV EEDDLIQNGH MEIPEKPGLG LTLDLDAVEA HMVEGETLFD EE
