ARAD_SACS2
ID ARAD_SACS2 Reviewed; 373 AA.
AC Q97U96;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Arabinonate dehydratase;
DE EC=4.2.1.5 {ECO:0000269|PubMed:16849334};
GN Name=araD; OrderedLocusNames=SSO3124 {ECO:0000312|EMBL:AAK43225.1};
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057 {ECO:0000312|EMBL:AAK43225.1};
RN [1] {ECO:0000312|Proteomes:UP000001974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2
RC {ECO:0000312|Proteomes:UP000001974};
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, INDUCTION BY
RP D-ARABINOSE, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=16849334; DOI=10.1074/jbc.m605549200;
RA Brouns S.J., Walther J., Snijders A.P., van de Werken H.J., Willemen H.L.,
RA Worm P., de Vos M.G., Andersson A., Lundgren M., Mazon H.F.,
RA van den Heuvel R.H., Nilsson P., Salmon L., de Vos W.M., Wright P.C.,
RA Bernander R., van der Oost J.;
RT "Identification of the missing links in prokaryotic pentose oxidation
RT pathways: evidence for enzyme recruitment.";
RL J. Biol. Chem. 281:27378-27388(2006).
CC -!- FUNCTION: Catalyzes the dehydration of D-arabinonate to 2-keto-3-deoxy-
CC D-arabinonate. Participates in a pentose oxidation pathway that
CC converts D-arabinonate to 2-oxoglutarate.
CC {ECO:0000269|PubMed:16849334}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinonate = 2-dehydro-3-deoxy-D-arabinonate + H2O;
CC Xref=Rhea:RHEA:21836, ChEBI:CHEBI:15377, ChEBI:CHEBI:16157,
CC ChEBI:CHEBI:16699; EC=4.2.1.5;
CC Evidence={ECO:0000269|PubMed:16849334};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16849334};
CC -!- ACTIVITY REGULATION: Inhibited by substrate levels above 8 mM.
CC {ECO:0000269|PubMed:16849334}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.7. {ECO:0000269|PubMed:16849334};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius.
CC {ECO:0000269|PubMed:16849334};
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:16849334}.
CC -!- INDUCTION: Expression is strongly increased by growth on D-arabinose,
CC both at the mRNA and at the protein level.
CC {ECO:0000269|PubMed:16849334}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. {ECO:0000305}.
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DR EMBL; AE006641; AAK43225.1; -; Genomic_DNA.
DR PIR; B90496; B90496.
DR RefSeq; WP_009989946.1; NC_002754.1.
DR AlphaFoldDB; Q97U96; -.
DR SMR; Q97U96; -.
DR STRING; 273057.SSO3124; -.
DR DNASU; 1453144; -.
DR EnsemblBacteria; AAK43225; AAK43225; SSO3124.
DR GeneID; 44128843; -.
DR KEGG; sso:SSO3124; -.
DR PATRIC; fig|273057.12.peg.3230; -.
DR eggNOG; arCOG01168; Archaea.
DR HOGENOM; CLU_030273_3_0_2; -.
DR InParanoid; Q97U96; -.
DR OMA; WVEHFDW; -.
DR PhylomeDB; Q97U96; -.
DR BioCyc; MetaCyc:MON-13205; -.
DR BRENDA; 4.2.1.5; 6163.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0047675; F:arabinonate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
DR GO; GO:0019571; P:D-arabinose catabolic process; IDA:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
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; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Lyase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..373
FT /note="Arabinonate dehydratase"
FT /id="PRO_0000430860"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11444"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11444"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11444"
SQ SEQUENCE 373 AA; 42437 MW; 5060B5D2ACAF238B CRC64;
MIKDIRTYKL CYEGINDERD ALAIKGLAEH PMEIVATEIE TSDGYVGYGE SLAYGCSDAV
QVTIEKILKP LLLKEDEELI EYLWDKMYKA TLRFGRRGIA IAGISGVDTA LWDIMGKKAK
KPIYKLLGGS KRKVRAYITG GYYSEKKDLE KLRDEEAYYV KMGFKGIKVK IGAKSMEEDI
ERLKAIREVV GEDVKIAVDA NNVYTFEEAL EMGRRLEKLG IWFFEEPIQT DYLDLSARLA
EELEVPIAGY ETAYTRWEFY EIMRKRAVDI VQTDVMWTGG ISEMMKIGNM AKVMGYPLIP
HYSAGGISLI GNLHVAAALN SPWIEMHLRK NDLRDKIFKE SIEIDNGHLV VPDRPGLGYT
IRDGVFEEYK CKS
