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Database: UniProt
Entry: H5Y9L7_9BRAD
LinkDB: H5Y9L7_9BRAD
Original site: H5Y9L7_9BRAD 
ID   H5Y9L7_9BRAD            Unreviewed;       447 AA.
AC   H5Y9L7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE            EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN   ORFNames=Bra471DRAFT_05314 {ECO:0000313|EMBL:EHR04512.1};
OS   Bradyrhizobium sp. WSM471.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR04512.1};
RN   [1] {ECO:0000313|EMBL:EHR04512.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM471 {ECO:0000313|EMBL:EHR04512.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA   Howieson J., Reeve W., Woyke T.;
RT   "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001426};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRSR:PIRSR617653-3};
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-
CC       dioxopentanoate from D-glucarate: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005183}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. GlucD subfamily. {ECO:0000256|ARBA:ARBA00009938}.
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DR   EMBL; CM001442; EHR04512.1; -; Genomic_DNA.
DR   RefSeq; WP_007612380.1; NZ_CM001442.1.
DR   AlphaFoldDB; H5Y9L7; -.
DR   HOGENOM; CLU_030273_9_0_5; -.
DR   OrthoDB; 9775913at2; -.
DR   UniPathway; UPA00564; UER00627.
DR   Proteomes; UP000005774; 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; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   InterPro; IPR034593; DgoD-like.
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   NCBIfam; TIGR03247; glucar-dehydr; 1.
DR   PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR   PANTHER; PTHR48080:SF4; GLUCARATE DEHYDRATASE; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   SFLD; SFLDS00001; Enolase; 1.
DR   SFLD; SFLDF00005; glucarate_dehydratase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR617653-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR617653-3}.
FT   DOMAIN          187..287
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        209
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-1"
FT   ACT_SITE        341
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-1"
FT   BINDING         34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         237..239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT   BINDING         291
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         341..343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         370
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         423
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
SQ   SEQUENCE   447 AA;  48501 MW;  F8EF67179DD38BEB CRC64;
     MAKTEITGAP VVTAMQVIPV AGRDSMLLNL SGAHAPFFTR NIVILTDNAG HTGVGEVPGG
     QKIWQTLQDA RDLVIGKTVG AMNNILADIR TAFADRDAAG RGKQTFDLRV MIHAVTAVES
     ALLDLLGQHL NLPVAALLGE GQQRNSVETL GYLFFVGDIS KSKLDYVTGE TGKPEWFNLR
     HQQAMTPETV VRLAEATHDH YGFADFKLKG GVLRGEQEIE AVTAIARRFP DARVTLDPNG
     AWSLDEAVSL CKDMHGILAY AEDPCGAEGG FSGREIMAEF RRATGLPTAT NMIATDWRQL
     SHALRLGAVD IPLADPHFWT MQGSVRVAQT CRDNGLTWGS HSNNHFDISL AMFTHVGAAA
     PGKVTAIDTH WIWQDGQALT KEPLQIRAGK IAVPDRPGLG IEIDRAAIEA AHDLYKQHGL
     GARDDAIAMQ DLIPGWTFDD KRPCLVR
//
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