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Database: UniProt
Entry: A0A166RP19_9EURY
LinkDB: A0A166RP19_9EURY
Original site: A0A166RP19_9EURY 
ID   A0A166RP19_9EURY        Unreviewed;       391 AA.
AC   A0A166RP19;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE            EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN   ORFNames=A4G99_13990 {ECO:0000313|EMBL:KZN23182.1};
OS   Haladaptatus sp. R4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haladaptataceae; Haladaptatus.
OX   NCBI_TaxID=1679489 {ECO:0000313|EMBL:KZN23182.1, ECO:0000313|Proteomes:UP000076599};
RN   [1] {ECO:0000313|EMBL:KZN23182.1, ECO:0000313|Proteomes:UP000076599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R4 {ECO:0000313|EMBL:KZN23182.1,
RC   ECO:0000313|Proteomes:UP000076599};
RA   Mukhopadhyay S.K.;
RT   "Genome sequence of halophilic archaea.";
RL   Submitted (APR-2016) 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   -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-
CC       dioxopentanoate from D-glucarate: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005183}.
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:KZN23182.1}.
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DR   EMBL; LWHG01000029; KZN23182.1; -; Genomic_DNA.
DR   RefSeq; WP_066146798.1; NZ_LWHG01000029.1.
DR   AlphaFoldDB; A0A166RP19; -.
DR   STRING; 1679489.A4G99_13990; -.
DR   OrthoDB; 42605at2157; -.
DR   Proteomes; UP000076599; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03329; MR_like_4; 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; 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; SFLDG00179; mandelate_racemase; 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          149..254
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   391 AA;  43364 MW;  2880ED7FF551B78B CRC64;
     MGPEITKIVS TEFAYPLEDV GTDEHGFNLV YEPGTTTERK LFAVEVQTDT GISGEYIGGN
     SPGAAQYNTV ADYLVGKNPL EREKHWSEVK RALRKYDRMG IGPIDIALWD FAGKYYDAPI
     HELLGTYRER IPAYASTYHG DENGGLDSPE AFADFAEECR ERGFPGYKIH GWGGGDTSRD
     LSREIDAVHA VGERVGDEMD LMHDPACELE TFADALKLGR ALDEEGFFWY EDPFRDGGIS
     QHAHRKLRQS LDTPILQTEH VRGLEPAADF VANEATDFVR ADPEYDGGIT GAMKRARMAE
     SFGLDVEFHA PGPAQRHCIA ATRNSNYYEM ALVHPNCQNT QPPVYLGEYS DMIDAVDDDG
     TVPVPDGPGL GVEYDWDYVE SNATGSVHVY E
//
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