ID E6BMF8_ECOLX Unreviewed; 382 AA.
AC E6BMF8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=D-galactonate dehydratase {ECO:0000256|HAMAP-Rule:MF_01289};
DE Short=GalD {ECO:0000256|HAMAP-Rule:MF_01289};
DE EC=4.2.1.6 {ECO:0000256|HAMAP-Rule:MF_01289};
GN Name=dgoD {ECO:0000256|HAMAP-Rule:MF_01289,
GN ECO:0000313|EMBL:EFU34590.1};
GN ORFNames=HMPREF9350_03576 {ECO:0000313|EMBL:EFU34590.1};
OS Escherichia coli MS 85-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679202 {ECO:0000313|EMBL:EFU34590.1, ECO:0000313|Proteomes:UP000005056};
RN [1] {ECO:0000313|EMBL:EFU34590.1, ECO:0000313|Proteomes:UP000005056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 85-1 {ECO:0000313|EMBL:EFU34590.1,
RC ECO:0000313|Proteomes:UP000005056};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dehydration of D-galactonate to 2-keto-3-deoxy-
CC D-galactonate. {ECO:0000256|HAMAP-Rule:MF_01289}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactonate = 2-dehydro-3-deoxy-D-galactonate + H2O;
CC Xref=Rhea:RHEA:18649, ChEBI:CHEBI:12931, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57989; EC=4.2.1.6; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01289};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01289};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01289};
CC -!- PATHWAY: Carbohydrate acid metabolism; D-galactonate degradation; D-
CC glyceraldehyde 3-phosphate and pyruvate from D-galactonate: step 1/3.
CC {ECO:0000256|HAMAP-Rule:MF_01289}.
CC -!- MISCELLANEOUS: Reaction proceeds via an anti dehydration.
CC {ECO:0000256|HAMAP-Rule:MF_01289}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. GalD subfamily. {ECO:0000256|HAMAP-Rule:MF_01289}.
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:EFU34590.1}.
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DR EMBL; ADWQ01000016; EFU34590.1; -; Genomic_DNA.
DR RefSeq; WP_000705001.1; NZ_ADWQ01000016.1.
DR AlphaFoldDB; E6BMF8; -.
DR SMR; E6BMF8; -.
DR GeneID; 75205406; -.
DR PATRIC; fig|679202.3.peg.3307; -.
DR UniPathway; UPA00081; UER00518.
DR Proteomes; UP000005056; Unassembled WGS sequence.
DR GO; GO:0008869; F:galactonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR GO; GO:0034194; P:D-galactonate catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd03325; D-galactonate_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 HAMAP; MF_01289; Galacton_dehydrat; 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; IPR023592; Galactonate_deHydtase.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR PANTHER; PTHR48080:SF2; D-GALACTONATE DEHYDRATASE; 1.
DR PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDF00003; D-galactonate_dehydratase; 1.
DR SFLD; SFLDS00001; Enolase; 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.
DR PROSITE; PS00908; MR_MLE_1; 1.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01289, ECO:0000313|EMBL:EFU34590.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01289};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01289}.
FT DOMAIN 125..230
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 185
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01289"
FT ACT_SITE 285
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01289"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01289"
FT BINDING 209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01289"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01289"
FT SITE 258
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01289"
FT SITE 310
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01289"
SQ SEQUENCE 382 AA; 42523 MW; B38D4E0B95FD7041 CRC64;
MKITKITTYR LPPRWMFLKI ETDEGVVGWG EPVIEGRART VEAAVHELGD YLIGQDPSRI
NDLWQVMYRA GFYRGGPILM SAIAGIDQAL WDIKGKVLNA PVWQLMGGLV RDKIKAYSWV
GGDRPADVID GIKTLREIGF DTFKLNGCEE LGLIDNSRAV DAAVNTVAQI REAFGNQIEF
GLDFHGRVSA PMAKVLIKEL EPYRPLFIEE PVLAEQAEYY PKLAAQTHIP LAAGERMFSR
FDFKRVLEAG GISILQPDLS HAGGITECYK IAGMAEAYDV TLAPHCPLGP IALAACLHID
FVSYNAVLQE QSMGIHYNKG AELLDFVKNK EDFSMVGGFF KPLTKPGLGV EIDEAKVIEF
SKNAPDWRNP LWRHEDNSVA EW
//