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Database: UniProt
Entry: A1HSE9_9FIRM
LinkDB: A1HSE9_9FIRM
Original site: A1HSE9_9FIRM 
ID   A1HSE9_9FIRM            Unreviewed;       452 AA.
AC   A1HSE9;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE            EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN   ORFNames=TcarDRAFT_0709 {ECO:0000313|EMBL:EAX47014.1};
OS   Thermosinus carboxydivorans Nor1.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Thermosinus.
OX   NCBI_TaxID=401526 {ECO:0000313|EMBL:EAX47014.1, ECO:0000313|Proteomes:UP000005139};
RN   [1] {ECO:0000313|EMBL:EAX47014.1, ECO:0000313|Proteomes:UP000005139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nor1 {ECO:0000313|EMBL:EAX47014.1,
RC   ECO:0000313|Proteomes:UP000005139};
RG   US DOE Joint Genome Institute (JGI-ORNL);
RA   Larimer F., Land M., Hauser L.;
RT   "Annotation of the draft genome assembly of Thermosinus carboxydivorans
RT   Nor1.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAX47014.1, ECO:0000313|Proteomes:UP000005139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nor1 {ECO:0000313|EMBL:EAX47014.1,
RC   ECO:0000313|Proteomes:UP000005139};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Pitluck S., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Thermosinus carboxydivorans
RT   Nor1.";
RL   Submitted (JAN-2007) 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         ECO:0000256|PIRSR:PIRSR617653-3};
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}.
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:EAX47014.1}.
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DR   EMBL; AAWL01000016; EAX47014.1; -; Genomic_DNA.
DR   RefSeq; WP_007289955.1; NZ_AAWL01000016.1.
DR   AlphaFoldDB; A1HSE9; -.
DR   eggNOG; COG4948; Bacteria.
DR   OrthoDB; 193563at2; -.
DR   UniPathway; UPA00564; UER00627.
DR   Proteomes; UP000005139; Unassembled WGS sequence.
DR   GO; GO:0008872; F:glucarate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0042838; P:D-glucarate catabolic process; IEA:UniProtKB-UniPathway.
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; IPR017653; Glucarate_dehydratase.
DR   InterPro; IPR034598; GlucD-like.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   NCBIfam; TIGR03247; glucar-dehydr; 1.
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; SFLDF00005; glucarate_dehydratase; 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   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR617653-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR617653-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005139}.
FT   DOMAIN          191..291
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        213
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-1"
FT   ACT_SITE        345
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-1"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         241..243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         241
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT   BINDING         272
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-3"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         345..347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         374
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
FT   BINDING         428
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617653-2"
SQ   SEQUENCE   452 AA;  50052 MW;  FB46E308080DD5C8 CRC64;
     MNNETTKNGI SGSPVVTELH VIPVAGRDSM LLNLSGAHGP FFTRNIVILK DSAGHTGVGE
     VPGGEKIRQT IEDARPLVVG QPIGKYNNIL TTVRQRFADR DAGGRGLQTF DLRITIHAVT
     ALEAALLDLL GQFLGVPVAA LLGEGQQRDE VEMLGYLFYI GDRKKTDLPY YSAPEAKDNW
     LRIRHEEAMT PQAIVELAEA AYERYGFNDF KLKGGVLRGE EEMEAVIALA KRFSKARITI
     DPNGAWSLEE AIKLCRGKHD VLAYAEDPCG AENGYSGREI MAEFRRATGI PTATNMIATD
     WRQMGHAIQL HSIDIPLADP HFWTMQGSVR VAQMCHEWGL TWGSHSNNHF DISLAMFTHV
     GAAAPGKITA LDTHWIWQEG IERLTKEPLK IVNGKVTVPD KPGLGIEVDM EQIEKAHQIY
     KKLGLGARDD TVAMQYLIPG WKFDNKRPCL VR
//
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