ARADH_HALVD
ID ARADH_HALVD Reviewed; 254 AA.
AC D4GP33;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=L-arabinose 1-dehydrogenase (NAD(P)(+)) {ECO:0000303|PubMed:23949136};
DE Short=L-AraDH {ECO:0000303|PubMed:23949136};
DE EC=1.1.1.376 {ECO:0000269|PubMed:23949136};
GN Name=xacB {ECO:0000303|PubMed:25141768}; OrderedLocusNames=HVO_B0032;
GN ORFNames=C498_01595;
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 1-17, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, DISRUPTION PHENOTYPE, SUBSTRATE SPECIFICITY, PATHWAY,
RP INDUCTION, AND SUBUNIT.
RX PubMed=23949136; DOI=10.1007/s00792-013-0572-2;
RA Johnsen U., Sutter J.M., Zaiss H., Schoenheit P.;
RT "L-Arabinose degradation pathway in the haloarchaeon Haloferax volcanii
RT involves a novel type of L-arabinose dehydrogenase.";
RL Extremophiles 17:897-909(2013).
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: L-AraDH initiates the degradation of L-arabinose. Catalyzes
CC the NAD(P)(+)-dependent conversion of L-arabinose to L-arabino-gamma-
CC lactone. It is highly specific for L-arabinose as substrate and can use
CC both NADP(+) and NAD(+) as electron acceptor, with a slight preference
CC for NADP(+). {ECO:0000269|PubMed:23949136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-L-arabinopyanose + NAD(+) = H(+) + L-arabinono-1,4-
CC lactone + NADH; Xref=Rhea:RHEA:17925, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17100, ChEBI:CHEBI:46987, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.376;
CC Evidence={ECO:0000269|PubMed:23949136};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-L-arabinopyanose + NADP(+) = H(+) + L-arabinono-1,4-
CC lactone + NADPH; Xref=Rhea:RHEA:42664, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17100, ChEBI:CHEBI:46987, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.376;
CC Evidence={ECO:0000269|PubMed:23949136};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 mM for NADP(+) {ECO:0000269|PubMed:23949136};
CC KM=2 mM for NAD(+) {ECO:0000269|PubMed:23949136};
CC KM=2.1 mM for L-arabinose {ECO:0000269|PubMed:23949136};
CC pH dependence:
CC Optimum pH is 8.5. It shows 50% activity at pH values of 6 and 10.
CC {ECO:0000269|PubMed:23949136};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:23949136};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC arabinono-1,4-lactone pathway. {ECO:0000305|PubMed:23949136}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:23949136}.
CC -!- INDUCTION: Transcriptionally up-regulated by both L-arabinose and D-
CC xylose via the pentose-specific regulator XacR.
CC {ECO:0000269|PubMed:23949136, ECO:0000269|PubMed:25141768}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to grow
CC on L-arabinose but not on D-xylose. {ECO:0000269|PubMed:23949136}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; CP001953; ADE01542.1; -; Genomic_DNA.
DR EMBL; AOHU01000021; ELY36799.1; -; Genomic_DNA.
DR RefSeq; WP_004041122.1; NZ_AOHU01000021.1.
DR AlphaFoldDB; D4GP33; -.
DR SMR; D4GP33; -.
DR STRING; 309800.C498_01595; -.
DR PRIDE; D4GP33; -.
DR EnsemblBacteria; ADE01542; ADE01542; HVO_B0032.
DR EnsemblBacteria; ELY36799; ELY36799; C498_01595.
DR GeneID; 8919002; -.
DR KEGG; hvo:HVO_B0032; -.
DR PATRIC; fig|309800.29.peg.305; -.
DR eggNOG; arCOG04704; Archaea.
DR HOGENOM; CLU_079334_1_0_2; -.
DR OMA; NLRIGWL; -.
DR OrthoDB; 43299at2157; -.
DR BioCyc; MetaCyc:MON-21251; -.
DR BRENDA; 1.1.1.376; 2561.
DR BRENDA; 1.1.1.46; 2561.
DR UniPathway; UPA00141; -.
DR Proteomes; UP000008243; Plasmid pHV3.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0050022; F:L-arabinose 1-dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0044103; F:L-arabinose 1-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0019572; P:L-arabinose catabolic process; IMP:UniProtKB.
DR GO; GO:0019570; P:L-arabinose catabolic process to 2-oxoglutarate; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Arabinose catabolism; Carbohydrate metabolism; Direct protein sequencing;
KW NAD; NADP; Oxidoreductase; Plasmid; Reference proteome.
FT CHAIN 1..254
FT /note="L-arabinose 1-dehydrogenase (NAD(P)(+))"
FT /id="PRO_0000435667"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P09147, ECO:0000255|HAMAP-
FT Rule:MF_02046"
FT BINDING 142
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147, ECO:0000255|HAMAP-
FT Rule:MF_02046"
FT BINDING 146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147, ECO:0000255|HAMAP-
FT Rule:MF_02046"
SQ SEQUENCE 254 AA; 27775 MW; 6297BED3664F5FC6 CRC64;
MARIAVTGAA GNVGRVTVEA LASDHDVTPI THREREGLDS VILDVRDEDA LTEAFEGHDI
VVHLAANPNP DAAWDSVYEV NIGGTYNVYE AALAADIDRL VFASTNHVHQ MYNIADATRP
ETLAADAEAV GVSDPPRPDS YYGVSKVFGE ALGNYYADRH GLEVLNLRIG WLLTADEVRE
KMDEEESVAR YVRAMWLSPG DCEQGMRRAV EASLPDSPLA VNLISANDDR YLSLTETMRA
IGYRPRDNSA TVVE
