ID A0A150UKK6_9BRAD Unreviewed; 447 AA.
AC A0A150UKK6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN Name=gudD {ECO:0000313|EMBL:KYG24690.1};
GN ORFNames=SE92_34315 {ECO:0000313|EMBL:KYG24690.1};
OS Bradyrhizobium sp. AT1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=574934 {ECO:0000313|EMBL:KYG24690.1, ECO:0000313|Proteomes:UP000075342};
RN [1] {ECO:0000313|EMBL:KYG24690.1, ECO:0000313|Proteomes:UP000075342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT1 {ECO:0000313|EMBL:KYG24690.1,
RC ECO:0000313|Proteomes:UP000075342};
RA Okubo T., Minamisawa K.;
RT "Evolution of nitrogen fixation genes.";
RL Submitted (JAN-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYG24690.1}.
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DR EMBL; JXDL01000001; KYG24690.1; -; Genomic_DNA.
DR RefSeq; WP_063203212.1; NZ_JXDL01000001.1.
DR AlphaFoldDB; A0A150UKK6; -.
DR STRING; 574934.SE92_34315; -.
DR PATRIC; fig|574934.3.peg.7266; -.
DR OrthoDB; 9775913at2; -.
DR UniPathway; UPA00564; UER00627.
DR Proteomes; UP000075342; Unassembled WGS sequence.
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, ECO:0000313|EMBL:KYG24690.1};
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; 48552 MW; 1FEE13A007E9BAFC CRC64;
MAQTDISGAP IVTAMQVIPV AGRDSMLLNL SGAHAPFFTR NIVILTDNAG HTGVGEVPGG
QKIWQTLQDA RDLVIGKTVG AMNNILADVR TAFADRDAGG RGKQTFDLRV MIHAVTAIES
ALLDLLGQHL NLPVAALLGE GLQRSSVETL GYLFFVGDRR KSRLDYVAGE TGKPEWFNLR
HQEAMTPETV VRLAEATHDH YGFADFKLKG GVLRGEQEIE AVTAIAKRFP NARVTLDPNG
AWSLDEAIRL CKGMHGILAY AEDPCGAEAG FSGREIMAEF RRATGLPTAT NMIATDWRQL
SHALRLGAVD IPLADPHFWT MQGSVRVAQT CRDNGLTWGS HSNNHFDISL AMFTHVGAAA
PGKVTAIDTH WIWQDGQALT REPLQIKGGR IAVPDRPGLG IEIDRAAIDA AHDLYKQHGL
GARDDAIAMQ DLIPGWTFDD KRPCLVR
//
