KDXD_HALVD
ID KDXD_HALVD Reviewed; 289 AA.
AC D4GP28;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Probable 2-keto-3-deoxyxylonate dehydratase {ECO:0000303|PubMed:19584053};
DE Short=KDXD {ECO:0000303|PubMed:19584053};
DE EC=4.2.1.141 {ECO:0000305|PubMed:19584053};
GN Name=xacE {ECO:0000303|PubMed:25141768}; OrderedLocusNames=HVO_B0027;
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 FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
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 [3]
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: Probable 2-keto-3-deoxyxylonate dehydratase involved in the
CC degradation of D-xylose, a major component of hemicelluloses such as
CC xylan. Catalyzes the fourth reaction in the xylose utilization pathway
CC through dehydratation of 2-dehydro-3-deoxy-D-xylonate into alpha-
CC ketoglutarate semialdehyde (2,5-dioxopentanoate).
CC {ECO:0000269|PubMed:19584053}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-D-arabinonate = 2,5-dioxopentanoate + H2O;
CC Xref=Rhea:RHEA:35807, ChEBI:CHEBI:15377, ChEBI:CHEBI:16699,
CC ChEBI:CHEBI:58136; EC=4.2.1.141;
CC Evidence={ECO:0000305|PubMed:19584053};
CC -!- PATHWAY: Carbohydrate metabolism; D-xylose degradation.
CC {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}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR EMBL; CP001953; ADE01418.1; -; Genomic_DNA.
DR RefSeq; WP_004061785.1; NZ_AOHU01000021.1.
DR AlphaFoldDB; D4GP28; -.
DR SMR; D4GP28; -.
DR STRING; 309800.C498_01620; -.
DR EnsemblBacteria; ADE01418; ADE01418; HVO_B0027.
DR GeneID; 8919100; -.
DR KEGG; hvo:HVO_B0027; -.
DR eggNOG; arCOG00236; Archaea.
DR HOGENOM; CLU_078481_0_0_2; -.
DR OMA; WQIPEPE; -.
DR OrthoDB; 35713at2157; -.
DR BioCyc; MetaCyc:MON-16376; -.
DR UniPathway; UPA00810; -.
DR Proteomes; UP000008243; Plasmid pHV3.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042843; P:D-xylose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.850.10; -; 1.
DR InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR SUPFAM; SSF56529; SSF56529; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Lyase; Magnesium; Metal-binding; Plasmid;
KW Reference proteome.
FT CHAIN 1..289
FT /note="Probable 2-keto-3-deoxyxylonate dehydratase"
FT /id="PRO_0000428800"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q97UA0"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q97UA0"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q97UA0"
SQ SEQUENCE 289 AA; 31862 MW; 009D64A921BD3176 CRC64;
MHYHQLAVSG ERRLTASRDS TTYDLTSADA DLRTFGDLAR VASIARTSVD RLAAELTEDA
DVVDDAFVDR HATVPVDAEE IWAAGVTYQI SEQAREEESS MPDMYFDVYD ADRPEVFFKA
TPSRTVEPGD AIGVRGDSEW DVPEPELGIV LRRGEIVGYT VGNDVSSRSI EGENPLYLPQ
AKVYDRCCSI GPCVVTPEDV EDPHELEMSM TIERDGEVIY DDATNTSEMV RSCDELVSYF
TRHNTVPELA VILTGTSLVP EQPFDLQEGD HVDITIEGIG TLSNSVTTV