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
//