ID A0A0D0SBQ1_9FIRM Unreviewed; 441 AA.
AC A0A0D0SBQ1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN ORFNames=P261_02387 {ECO:0000313|EMBL:KIR03572.1};
OS Lachnospiraceae bacterium TWA4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1392836 {ECO:0000313|EMBL:KIR03572.1, ECO:0000313|Proteomes:UP000032079};
RN [1] {ECO:0000313|EMBL:KIR03572.1, ECO:0000313|Proteomes:UP000032079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TWA4 {ECO:0000313|EMBL:KIR03572.1,
RC ECO:0000313|Proteomes:UP000032079};
RX PubMed=25495654;
RA Gagen E.J., Wang J., Padmanabha J., Liu J., de Carvalho I., Liu J.,
RA Webb R.I., Al Jassim R., Morrison M., Denman S.E., McSweeney C.S.;
RT "Investigation of a new acetogen isolated from an enrichment of the tammar
RT wallaby forestomach.";
RL BMC Microbiol. 14:314-314(2014).
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:PIRSR634598-3};
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:KIR03572.1}.
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DR EMBL; JPZU01000001; KIR03572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0SBQ1; -.
DR STRING; 1392836.P261_02387; -.
DR PATRIC; fig|1392836.3.peg.2693; -.
DR OrthoDB; 193563at2; -.
DR Proteomes; UP000032079; Unassembled WGS sequence.
DR GO; GO:0008872; F:glucarate dehydratase activity; IEA:UniProtKB-EC.
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 PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR PANTHER; PTHR48080:SF4; GLUCARATE DEHYDRATASE; 1.
DR Pfam; PF13378; MR_MLE_C; 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:0000313|EMBL:KIR03572.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR634598-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634598-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000032079}.
FT DOMAIN 180..280
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT ACT_SITE 334
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 230..232
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 334..336
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-2"
SQ SEQUENCE 441 AA; 49393 MW; 429DFA9DDE3D21B5 CRC64;
MSKIVKMEVF PVAGRDCMEL NLSGAHAPYF TRNIVILTDE NGVEGIGEVP GGEKITKALE
EVTSLVVGKN TEEYRNILLD VQAHFDAKGE EDVRGNQTFD LRTGVHVKTA IEAPCLDLLG
KQLNVPVCKL LGDGQQRDKV RMLGYLFFVG DPNKTDLEYA HELDSDCDWY RLRHEEALDA
ETIVAHARAT QEKYGFKDFK LKGGVLPGNE EMEVIKALKK AFPDARIDLD PNGGWLLEQA
VEYVKDMQGI LTYCEDPCGA EGVYSGREIM SEFRRRTGFP TATNMIATDW RQVCHSLETQ
AVDIILADPH FWTMNGSVRV AQMCHDFGLT WGSHSNNHFD ISLAMFTQVG AAVPGKYNAL
DTHWIWQEGL ERLTKEPLQI VDGCVAVPDK PGLGVEIDRE QVEKAHKLYM DKCLGGRDDS
VGMQYLIPGW KFDPKKPCLV R
//
