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Database: UniProt
Entry: A0A0U2XXA7_9BURK
LinkDB: A0A0U2XXA7_9BURK
Original site: A0A0U2XXA7_9BURK 
ID   A0A0U2XXA7_9BURK        Unreviewed;       424 AA.
AC   A0A0U2XXA7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE            EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN   ORFNames=AT302_03485 {ECO:0000313|EMBL:ALS58980.1};
OS   Pandoraea norimbergensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Pandoraea.
OX   NCBI_TaxID=93219 {ECO:0000313|EMBL:ALS58980.1, ECO:0000313|Proteomes:UP000060277};
RN   [1] {ECO:0000313|Proteomes:UP000060277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11628 {ECO:0000313|Proteomes:UP000060277};
RA   Ee R., Lim Y.-L., Yong D., Yin W.-F., Chan K.-G.;
RT   "Complete genome sequence of Pandoraea norimbergensis DSM 11628.";
RL   Submitted (DEC-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   -!- 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; CP013480; ALS58980.1; -; Genomic_DNA.
DR   RefSeq; WP_058375923.1; NZ_CP013480.3.
DR   AlphaFoldDB; A0A0U2XXA7; -.
DR   STRING; 93219.AT302_03485; -.
DR   KEGG; pnr:AT302_03485; -.
DR   OrthoDB; 193563at2; -.
DR   Proteomes; UP000060277; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR034598; GlucD-like.
DR   InterPro; IPR013342; Mandelate_racemase_C.
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; SFLDG00055; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          171..265
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT   ACT_SITE        320
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
SQ   SEQUENCE   424 AA;  47053 MW;  3C93F55ECC5475E7 CRC64;
     MKIQRITITP IAFRDPPLLN AAGIHEPYAL RTIIEIETDN GHVGLGETYG DAPVLTLLQN
     TREHLIGMDP FDTNGLRARV AAVVARGVGG ERVEYELAPG TDPRKDAEKI YSAFEVPFLD
     LQARHLGIPL VELLGGAVRN EVQYSAYLFF KYAQHIDNPY APDPWGETLD ATQLVAQART
     MIDTYGFGSI KLKAGALDPN EEVKCLKALK RAFPDKPLRI DPNGNWSLAT AIRMGRELEG
     DLEYYEDPTP TLEGMAELHR ATGMPLATNM VVTDLRQFRE NVRVNGAQII LSDHHYWGGL
     RDTQVLARMC ETFDLGLSMH SNSHLGISLM AMTHLAASVP RLSYACDTHY PWQAADEEVV
     RGGKIAIRNG AVALTKAPGL GLEIDQDQLA KLHEQYLRCG VRTRNDAVQM RKYQPGWSGK
     APRF
//
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