ID A1HSF1_9FIRM Unreviewed; 463 AA.
AC A1HSF1;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN ORFNames=TcarDRAFT_0711 {ECO:0000313|EMBL:EAX47016.1};
OS Thermosinus carboxydivorans Nor1.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Thermosinus.
OX NCBI_TaxID=401526 {ECO:0000313|EMBL:EAX47016.1, ECO:0000313|Proteomes:UP000005139};
RN [1] {ECO:0000313|EMBL:EAX47016.1, ECO:0000313|Proteomes:UP000005139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nor1 {ECO:0000313|EMBL:EAX47016.1,
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:EAX47016.1, ECO:0000313|Proteomes:UP000005139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nor1 {ECO:0000313|EMBL:EAX47016.1,
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: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:EAX47016.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAWL01000016; EAX47016.1; -; Genomic_DNA.
DR RefSeq; WP_007289957.1; NZ_AAWL01000016.1.
DR AlphaFoldDB; A1HSF1; -.
DR eggNOG; COG4948; Bacteria.
DR OrthoDB; 193563at2; -.
DR Proteomes; UP000005139; 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:EAX47016.1};
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:UP000005139}.
FT DOMAIN 202..302
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT ACT_SITE 356
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-3"
SQ SEQUENCE 463 AA; 50894 MW; C53D469365C990B4 CRC64;
MSDSVYTGVP IVTDMQVIPV AGHDSMLLNL CGAHAPFFIR NIIILKDNSG RTGVGEVPGG
EGIRKALENA RPLVIGQSIG AYNKVLNSVR QQLFNRQAGR QATVYQVTSA AEAAILTQPH
EINLRADNVI TAIEAAMLDL LGQFLNVPVA ALLGNGQQRD TVRMLGYLFY IGDRKKTDLP
YLSNPTAKDG WLRLRHEEAL TPAAIVALAE AAAERYGFQD FKLKGGVMSG EEEMEAVTAL
AKRFPQARIT IDPNGAWSLD EAIRLCRNKQ DVLAYAEDPC GPENGYSGRE IMAEFRRATG
IPTATNMIAT DWRQMGHAIQ LHAVDIPLAD PHFWTMQGSV RVAQMCHEFG LTWGSHSNNH
FDISLAMFTH VAAAAPGNIT AIDTHWIWQE NQERLTKEPF KIVGGLVEVP QKPGLGIEID
MAQVEKANAL YNKLGQGARD DAMAMQYLIP GWKYNPKRPS MVR
//
