GUDD_ACIAD
ID GUDD_ACIAD Reviewed; 444 AA.
AC Q6FFQ2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Glucarate dehydratase;
DE Short=GDH;
DE Short=GlucD;
DE EC=4.2.1.40;
GN Name=gudD; OrderedLocusNames=ACIAD0128;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [2]
RP FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=18364348; DOI=10.1074/jbc.m800487200;
RA Aghaie A., Lechaplais C., Sirven P., Tricot S., Besnard-Gonnet M.,
RA Muselet D., de Berardinis V., Kreimeyer A., Gyapay G., Salanoubat M.,
RA Perret A.;
RT "New insights into the alternative D-glucarate degradation pathway.";
RL J. Biol. Chem. 283:15638-15646(2008).
CC -!- FUNCTION: Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D-
CC glucarate (5-kdGluc). {ECO:0000269|PubMed:18364348}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H2O;
CC Xref=Rhea:RHEA:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:30612,
CC ChEBI:CHEBI:42819; EC=4.2.1.40;
CC Evidence={ECO:0000269|PubMed:18364348};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-
CC dioxopentanoate from D-glucarate: step 1/2.
CC {ECO:0000269|PubMed:18364348}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. GlucD subfamily. {ECO:0000305}.
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DR EMBL; CR543861; CAG67105.1; -; Genomic_DNA.
DR RefSeq; WP_004930680.1; NC_005966.1.
DR AlphaFoldDB; Q6FFQ2; -.
DR SMR; Q6FFQ2; -.
DR STRING; 62977.ACIAD0128; -.
DR EnsemblBacteria; CAG67105; CAG67105; ACIAD0128.
DR GeneID; 45232650; -.
DR KEGG; aci:ACIAD0128; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_9_0_6; -.
DR OMA; MQYLIPN; -.
DR OrthoDB; 951991at2; -.
DR BioCyc; ASP62977:ACIAD_RS00600-MON; -.
DR BioCyc; MetaCyc:MON-15624; -.
DR BRENDA; 4.2.1.40; 8909.
DR SABIO-RK; Q6FFQ2; -.
DR UniPathway; UPA00564; UER00627.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0008872; F:glucarate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042838; P:D-glucarate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03323; D-glucarate_dehydratase; 1.
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; IPR017653; Glucarate_dehydratase.
DR InterPro; IPR034598; GlucD-like.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR034593; Mandelate_racemase_DgoD-like.
DR PANTHER; PTHR48080; PTHR48080; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR SFLD; SFLDF00005; glucarate_dehydratase; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR03247; glucar-dehydr; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..444
FT /note="Glucarate dehydratase"
FT /id="PRO_0000424017"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233..235
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 337..339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 444 AA; 49027 MW; 51EBDF3601CE576C CRC64;
MAASTPIIQS VRAIPVAGHD SMLLNLSGAH APYFTRNLLV IEDNSGNIGV GEIPGGEKIL
ATLNDAKSLI LGQPIGEYKN LLKKIHQTFA DRDSGGRGNQ TFDLRTTVHV VTAYESALLD
LLGKHLNVNV ASLLGDGQQR DEVEVLGYLF FIGDRKQTSL DYATSTHLNH DWYQVRHEKA
LTPEAIQRLA EASYDRYGFK DFKLKGGVLH GEQEAEAVTA IARRFPDARV TLDPNGAWYL
DEAIGLGKHL KGVLAYAEDP CGAEQGYSSR EIMAEFKRAT GLPTATNMIA TDWREMSHSI
QLQAVDIPLA DPHFWTLEGS VRVSQLCNMY NLTWGSHSNN HFDVSLAMFT HVAAAAVGNV
TAIDTHWIWQ EGTDHLTKQP LEIKGGKIQV PSVPGLGVEL DWDNINRAHE LYKAKGLGAR
NDADAMQFMV PNWKFDHKKP CLVR
