ARADA_AZOBR
ID ARADA_AZOBR Reviewed; 583 AA.
AC Q1JUQ1;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=L-arabonate dehydratase;
DE EC=4.2.1.25;
DE AltName: Full=L-arabinonate dehydratase;
GN Name=araC;
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-17, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION,
RP PATHWAY, SUBUNIT, METAL-BINDING SITES, AND MUTAGENESIS OF CYS-47; CYS-56;
RP CYS-124; CYS-197 AND CYS-441.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=16950779; DOI=10.1074/jbc.m606727200;
RA Watanabe S., Shimada N., Tajima K., Kodaki T., Makino K.;
RT "Identification and characterization of L-arabonate dehydratase, L-2-keto-
RT 3-deoxyarabonate dehydratase and L-arabinolactonase involved in an
RT alternative pathway of L-arabinose metabolism: novel evolutionary insight
RT into sugar metabolism.";
RL J. Biol. Chem. 281:33521-33536(2006).
RN [2]
RP PATHWAY.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=6798025; DOI=10.1128/jb.149.1.364-367.1982;
RA Novick N.J., Tyler M.E.;
RT "L-arabinose metabolism in Azospirillum brasiliense.";
RL J. Bacteriol. 149:364-367(1982).
CC -!- FUNCTION: Catalyzes the dehydration of L-arabonate to L-2-keto-3-
CC deoxyarabonate (L-KDA). Is involved in a degradation pathway of L-
CC arabinose that allows A.brasilense to grow on L-arabinose as a sole
CC carbon source. To a lesser extent, can also use D-xylonate as
CC substrate, but not D-galactonate, D-arabonate, and D-gluconate.
CC {ECO:0000269|PubMed:16950779}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arabinonate = 2-dehydro-3-deoxy-L-arabinonate + H2O;
CC Xref=Rhea:RHEA:20968, ChEBI:CHEBI:15377, ChEBI:CHEBI:16501,
CC ChEBI:CHEBI:35173; EC=4.2.1.25;
CC Evidence={ECO:0000269|PubMed:16950779};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:16950779};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:16950779};
CC -!- ACTIVITY REGULATION: Activity is enhanced by Mg(2+), being optimal with
CC a concentration of 1-10 mM Mg(2+). {ECO:0000269|PubMed:16950779}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16950779}.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000305}.
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DR EMBL; AB241136; BAE94269.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1JUQ1; -.
DR SMR; Q1JUQ1; -.
DR BRENDA; 4.2.1.25; 611.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0050020; F:L-arabinonate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019570; P:L-arabinose catabolic process to 2-oxoglutarate; IDA:UniProtKB.
DR Gene3D; 3.50.30.80; -; 1.
DR InterPro; IPR042096; Dihydro-acid_dehy_C.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR InterPro; IPR037237; IlvD/EDD_N.
DR Pfam; PF00920; ILVD_EDD; 1.
DR SUPFAM; SSF143975; SSF143975; 1.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Arabinose catabolism; Carbohydrate metabolism;
KW Direct protein sequencing; Iron; Iron-sulfur; Lyase; Metal-binding.
FT CHAIN 1..583
FT /note="L-arabonate dehydratase"
FT /id="PRO_0000418506"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305|PubMed:16950779"
FT BINDING 124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:16950779"
FT BINDING 197
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:16950779"
FT MUTAGEN 47
FT /note="C->A: 2-fold reduction in activity and still binds a
FT 4Fe-4S cluster."
FT /evidence="ECO:0000269|PubMed:16950779"
FT MUTAGEN 56
FT /note="C->A: Loss of activity but seems to be able to bind
FT a Fe-S cluster."
FT /evidence="ECO:0000269|PubMed:16950779"
FT MUTAGEN 124
FT /note="C->A: Loss of activity and no 4Fe-4S cluster
FT binding."
FT /evidence="ECO:0000269|PubMed:16950779"
FT MUTAGEN 197
FT /note="C->A: Loss of activity and no 4Fe-4S cluster
FT binding."
FT /evidence="ECO:0000269|PubMed:16950779"
FT MUTAGEN 441
FT /note="C->A: Increase in activity and still binds a 4Fe-4S
FT cluster."
FT /evidence="ECO:0000269|PubMed:16950779"
SQ SEQUENCE 583 AA; 62252 MW; 8AAEC32CA3094D5C CRC64;
MSATKPRLRS TQWFGTNDKN GFMYRSWMKN QGIPDHEFDG RPIIGICNTW SELTPCNAHF
RKLAEHVKRG ISEAGGFPVE FPVFSNGESN LRPSAMLTRN LASMDVEEAI RGNPIDAVVL
LAGCDKTTPA LLMGAASCDV PAIVVSGGPM LNGKLEGKNI GSGTAVWQLH EALKAGEIDV
HHFLSAEAGM SRSAGTCNTM GTASTMACMA EALGVALPHN AAIPAVDSRR YVLAHMSGIR
IVEMALEGLV LSKILTRAAF ENAIRANAAI GGSTNAVIHL KAIAGRIGVP LELEDWMRIG
RDTPTIVDLM PSGRFPMEEF YYAGGLPAVL RRLGEGGLLP NPDALTVNGK SLWDNVREAP
NYDEEVIRPL DRPLIADGGI RILRGNLAPR GAVLKPSAAS PELLKHRGRA VVFENLDHYK
ATINDEALDI DASSVMVLKN CGPRGYPGMA EVGNMGLPPK LLRQGVKDMV RISDARMSGT
AYGTVVLHVA PEAAAGGPLA AVRNGDWIEL DCEAGTLHLD ITDDELHRRL SDVDPTAAPG
VAGQLGKGGY ARLYIDHVLQ ADEGCDLDFL VGTRGAEVPS HSH
