ID   W0JWA0_9EURY            Unreviewed;       401 AA.
AC   W0JWA0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   18-JUN-2025, entry version 45.
DE   RecName: Full=gluconate dehydratase {ECO:0000256|ARBA:ARBA00066770};
DE            EC=4.2.1.39 {ECO:0000256|ARBA:ARBA00066770};
GN   ORFNames=HALLA_02800 {ECO:0000313|EMBL:AHG01328.1};
OS   Halostagnicola larsenii XH-48.
OG   Plasmid unnamed {ECO:0000313|EMBL:AHG01328.1}.
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Halobacteria; Halobacteriales; Natrialbaceae; Halostagnicola.
OX   NCBI_TaxID=797299 {ECO:0000313|EMBL:AHG01328.1, ECO:0000313|Proteomes:UP000019024};
RN   [1] {ECO:0000313|EMBL:AHG01328.1, ECO:0000313|Proteomes:UP000019024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH-48 {ECO:0000313|EMBL:AHG01328.1,
RC   ECO:0000313|Proteomes:UP000019024};
RC   PLASMID=1 {ECO:0000313|Proteomes:UP000019024};
RG   DOE Joint Genome Institute;
RA   Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-gluconate = 2-dehydro-3-deoxy-D-gluconate + H2O;
CC         Xref=Rhea:RHEA:21612, ChEBI:CHEBI:15377, ChEBI:CHEBI:18391,
CC         ChEBI:CHEBI:57990; EC=4.2.1.39;
CC         Evidence={ECO:0000256|ARBA:ARBA00050848};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. GaD subfamily. {ECO:0000256|ARBA:ARBA00061582}.
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DR   EMBL; CP007056; AHG01328.1; -; Genomic_DNA.
DR   RefSeq; WP_049954259.1; NZ_CP007056.1.
DR   AlphaFoldDB; W0JWA0; -.
DR   GeneID; 25146746; -.
DR   KEGG; hlr:HALLA_02800; -.
DR   PATRIC; fig|797299.3.peg.3075; -.
DR   eggNOG; arCOG01168; Archaea.
DR   HOGENOM; CLU_030273_1_0_2; -.
DR   OrthoDB; 42605at2157; -.
DR   Proteomes; UP000019024; Plasmid 1.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:TreeGrafter.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:TreeGrafter.
DR   GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:TreeGrafter.
DR   FunFam; 3.20.20.120:FF:000005; Putative L-rhamnonate 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; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   InterPro; IPR046945; RHMD-like.
DR   PANTHER; PTHR13794; ENOLASE SUPERFAMILY, MANDELATE RACEMASE; 1.
DR   PANTHER; PTHR13794:SF58; MITOCHONDRIAL ENOLASE SUPERFAMILY MEMBER 1; 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.
DR   PROSITE; PS00908; MR_MLE_1; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Plasmid {ECO:0000313|EMBL:AHG01328.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019024}.
FT   DOMAIN          165..268
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   401 AA;  44691 MW;  3F183BEDB9D87308 CRC64;
     MEITDITVTK VSTDSWGEFV EFPLVTVMSK FDEYNNADGD NPQARRKWMG PVGDVVVEVE
     TDAGITGVGV GNWATGSIET IVDETLSKLI VGEDPHQRER LWDMMYRATI PFGRKGAAIE
     AISAVDLALW DIAGKEAEKP VYELLGGPVT DEIPCYASNL HPVDHDKLER EAQEYAEAGF
     DTMKLRFLHG PEAGREGMKE NEKIVETVRD AVGDEIGIAG DAYMGWTVRY AKKMLKRLER
     YDMEWVEEPV IPDDIDGYAE VREASNVPIS GGEHEFTRWG HKELLEREAV DILQPDVHRC
     GGLTELLKID SMASARDVPV IPHSGTNPHL HFIAASTNAP MAEYFPIPEW YQERQGEQES
     TYADAIYANP PNAENGSIAL PETVGLSSEV NRDALEHYRV E
//