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Database: UniProt
Entry: D6K065_9ACTN
LinkDB: D6K065_9ACTN
Original site: D6K065_9ACTN 
ID   D6K065_9ACTN            Unreviewed;       447 AA.
AC   D6K065;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE            EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN   ORFNames=SSTG_01277 {ECO:0000313|EMBL:EFF90959.2};
OS   Streptomyces sp. e14.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=645465 {ECO:0000313|EMBL:EFF90959.2, ECO:0000313|Proteomes:UP000004704};
RN   [1] {ECO:0000313|EMBL:EFF90959.2, ECO:0000313|Proteomes:UP000004704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=e14 {ECO:0000313|Proteomes:UP000004704};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Streptomyces sp. strain e14.";
RL   Submitted (OCT-2009) 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; GG753626; EFF90959.2; -; Genomic_DNA.
DR   AlphaFoldDB; D6K065; -.
DR   STRING; 645465.SSTG_01277; -.
DR   eggNOG; COG4948; Bacteria.
DR   Proteomes; UP000004704; Unassembled WGS sequence.
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   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   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004704}.
FT   DOMAIN          194..288
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        216
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT   ACT_SITE        343
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT   BINDING         47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         244..246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         343..345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         372
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT   BINDING         426
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
SQ   SEQUENCE   447 AA;  48132 MW;  9D46D2C47C307AEE CRC64;
     MAAVGHRARP PPTRRSRPVT RDLAIAEVRL TPILVADPPL LNTQGVHQPY TPRLIVEVVT
     ADGITGLGET YGDTKYLELA RPLADRLVGH RVSELNALHA LDVAVAADRV VDAVDVGGLR
     GVQTADKLRL SVVSAFEVAC LDALGKALGL PVHALLGGKV RDSVEYSAYL FYKWAAHPEA
     AGGEKDDWGA ALDPAGVVEQ ARTFTERYGF TSFKLKGGVF PPDQEVAAVR ALAEAFPGHP
     LRLDPNGAWS VETSVRVARE LADVLEYLED PALGTPAMAE VAARTDVPLA TNMCVTTFGE
     IPEAFAEGAV QVVLSDHHYW GGLRNTQHLA ALCAAFGVGV SMHSNTHLGI SLAAMTHVAS
     TVPNLRHACD SHYPWQSEDV LTERLVFDGG RVAVGDAPGL GIALDRDELE RLHRRWLDDD
     RPLRERDDAA AMRVAEPGWA TPATPRW
//
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