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Database: UniProt
Entry: C3N467_SULIA
LinkDB: C3N467_SULIA
Original site: C3N467_SULIA 
ID   C3N467_SULIA            Unreviewed;       400 AA.
AC   C3N467;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE            EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN   OrderedLocusNames=M1627_0863 {ECO:0000313|EMBL:ACP54799.1};
OS   Sulfolobus islandicus (strain M.16.27).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=427318 {ECO:0000313|EMBL:ACP54799.1, ECO:0000313|Proteomes:UP000002307};
RN   [1] {ECO:0000313|EMBL:ACP54799.1, ECO:0000313|Proteomes:UP000002307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.27 {ECO:0000313|EMBL:ACP54799.1,
RC   ECO:0000313|Proteomes:UP000002307};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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   -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-
CC       dioxopentanoate from D-glucarate: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005183}.
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DR   EMBL; CP001401; ACP54799.1; -; Genomic_DNA.
DR   RefSeq; WP_012718611.1; NC_012632.1.
DR   AlphaFoldDB; C3N467; -.
DR   GeneID; 84055448; -.
DR   KEGG; sim:M1627_0863; -.
DR   HOGENOM; CLU_030273_3_1_2; -.
DR   Proteomes; UP000002307; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR   PANTHER; PTHR48080:SF4; GLUCARATE DEHYDRATASE; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 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   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          144..239
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   400 AA;  44876 MW;  F0808F531BA35983 CRC64;
     MKIKNLETKT IAIPLKDKLL HGVGEHPGRL IFTIVKIETD EGVIGYGETG GGGYSLSPMI
     EKLKTSLIGE DLNIRRLRWK VASPISATYY NQLLPQIWFP IETALLDIKG KALGISISDQ
     IGGKVKDEIE VSAYIFPTPN TLTVQELVNK VEKIVKEGGF RVVKLKTGVF SPKHEIDVVK
     ELAERLPYIK FRLDPNGAWS LSEALYVARS LEGVNIEYFE DPVWTTNGLK AFRELSKYPV
     ATNTVAIKFE DLPNVFLRDA VDIVLGDPHW WYGIYGFLEL SASLWSLGLE LGMHSPTETG
     IALAAMLHAA SASPNLAYAI DTHYVHLSDD IIKRPFKISE GKIKVPTEPG LGVDVDENKI
     DKYQQLYEEE GEYTYHQVEL TKEIVMIPRR SFINCKCHPY
//
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