XACC_HALVD
ID XACC_HALVD Reviewed; 291 AA.
AC D4GP31; L9VI99;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Pentonolactonase XacC {ECO:0000305};
DE EC=3.1.1.15 {ECO:0000269|PubMed:28854683};
DE EC=3.1.1.68 {ECO:0000269|PubMed:28854683};
DE AltName: Full=L-arabinonolactonase {ECO:0000305};
DE AltName: Full=Xylono-1,4-lactonase {ECO:0000305};
GN Name=xacC {ECO:0000303|PubMed:28854683};
GN OrderedLocusNames=HVO_B0030 {ECO:0000312|EMBL:ADE01475.1};
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, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
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: Pentonolactonase involved in D-arabinose and D-xylose
CC catabolism. Catalyzes the hydrolysis of both L-arabino-gamma-lactone
CC and D-xylono-gamma-lactone to the corresponding acids. Can also
CC hydrolyze D-galactono-gamma-lactone and D-glucono-delta-lactone.
CC {ECO:0000269|PubMed:28854683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arabinono-1,4-lactone = H(+) + L-arabinonate;
CC Xref=Rhea:RHEA:16217, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16501, ChEBI:CHEBI:17100; EC=3.1.1.15;
CC Evidence={ECO:0000269|PubMed:28854683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylono-1,4-lactone + H2O = D-xylonate + H(+);
CC Xref=Rhea:RHEA:18341, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16392, ChEBI:CHEBI:17746; EC=3.1.1.68;
CC Evidence={ECO:0000269|PubMed:28854683};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:28854683};
CC Note=Binds 1 divalent metal cation per subunit (By similarity). Most
CC active with Co(2+), Mg(2+) or Mn(2+). Has weaker activity with Fe(2+),
CC Ni(2+) or Zn(2+) (PubMed:28854683). {ECO:0000250|UniProtKB:Q15493,
CC ECO:0000269|PubMed:28854683};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37.1 mM for L-arabino-gamma-lactone {ECO:0000269|PubMed:28854683};
CC KM=10.9 mM for D-xylono-gamma-lactone {ECO:0000269|PubMed:28854683};
CC Vmax=761 umol/min/mg enzyme with L-arabino-gamma-lactone as substrate
CC {ECO:0000269|PubMed:28854683};
CC Vmax=437 umol/min/mg enzyme with D-xylono-gamma-lactone as substrate
CC {ECO:0000269|PubMed:28854683};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000269|PubMed:28854683}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:28854683}.
CC -!- INDUCTION: Transcriptionally up-regulated by both L-arabinose and D-
CC xylose via the pentose-specific regulator XacR.
CC {ECO:0000269|PubMed:28854683}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant shows restricted growth on L-
CC arabinose but grows on D-xylose as the wild type.
CC {ECO:0000269|PubMed:28854683}.
CC -!- SIMILARITY: Belongs to the SMP-30/CGR1 family. {ECO:0000305}.
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DR EMBL; CP001953; ADE01475.1; -; Genomic_DNA.
DR RefSeq; WP_004041124.1; NZ_AOHU01000021.1.
DR AlphaFoldDB; D4GP31; -.
DR SMR; D4GP31; -.
DR STRING; 309800.C498_01605; -.
DR EnsemblBacteria; ADE01475; ADE01475; HVO_B0030.
DR GeneID; 8919047; -.
DR KEGG; hvo:HVO_B0030; -.
DR PATRIC; fig|309800.29.peg.307; -.
DR eggNOG; arCOG05370; Archaea.
DR HOGENOM; CLU_036110_3_1_2; -.
DR OMA; AGTMRYD; -.
DR OrthoDB; 52063at2157; -.
DR BioCyc; MetaCyc:MON-20630; -.
DR BRENDA; 3.1.1.15; 2561.
DR BRENDA; 3.1.1.68; 2561.
DR Proteomes; UP000008243; Plasmid pHV3.
DR GO; GO:0050021; F:L-arabinonolactonase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050402; F:xylono-1,4-lactonase activity; IEA:UniProtKB-EC.
DR GO; GO:0019568; P:arabinose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR013658; SGL.
DR InterPro; IPR005511; SMP-30.
DR Pfam; PF08450; SGL; 1.
DR PRINTS; PR01790; SMP30FAMILY.
PE 1: Evidence at protein level;
KW Arabinose catabolism; Carbohydrate metabolism; Cobalt; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Plasmid; Reference proteome;
KW Xylose metabolism.
FT CHAIN 1..291
FT /note="Pentonolactonase XacC"
FT /id="PRO_0000449387"
FT ACT_SITE 191
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q15493"
FT BINDING 15
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q15493"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q15493"
FT BINDING 191
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q15493"
SQ SEQUENCE 291 AA; 31454 MW; 6E481BD06D0B538E CRC64;
MTVTRVVDTS CRLGEGPVWH PDEKRLYWVD IESGRLHRYD PETGAHDCPV ETSVIAGVTI
QRDGSLLAFM DRGRVGRVVD GDRRESARIV DSPTRFNDVI ADPAGRVFCG TMPSDTAGGR
LFRLDTDGTV TTVETGVGIP NGMGFTRDRE RFYFTETEAR TVYRYAYDEE TGAVSARERF
VESPETPGLP DGMTVDSAGH IWSARWEGGC VVEYDADGTE LGRFDVPTEK VTSVAFGGPD
LDSLYVTTAG GDGDGSAGEG DESTGDAAGA LFRLDVAATG RPEFRSDVRL G
