ID A0A1I3N015_9GAMM Unreviewed; 382 AA.
AC A0A1I3N015;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 ORFNames=SAMN05421680_10546 {ECO:0000313|EMBL:SFJ02579.1};
OS Xenorhabdus mauleonii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351675 {ECO:0000313|EMBL:SFJ02579.1, ECO:0000313|Proteomes:UP000198919};
RN [1] {ECO:0000313|Proteomes:UP000198919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17908 {ECO:0000313|Proteomes:UP000198919};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FORG01000005; SFJ02579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3N015; -.
DR STRING; 351675.SAMN05421680_10546; -.
DR OrthoDB; 103536at2; -.
DR UniPathway; UPA00081; UER00518.
DR Proteomes; UP000198919; 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};
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; 42758 MW; EC2DAE915AF8FAB5 CRC64;
MKITKLTTYR LPPRWMFLKM ETDDGVVGWG EPTIEGRART VEMAVHELGE YLIGQDPARI
NDLWQVMYRG GFYRGGPVLM SAIAGIDQAL WDIKGKVLKA PVWQLLGGLV RDKIKAYSWV
GGDRPAEVIA GIENLCKIGF DTFKLNGCEE LEIIDTARKV DAAVSVVAQI REAFGHQIEF
GLDFHGRVSA PMAKVLIHEL EPYRPLFIEE PVLAEQAEYY PRLAAQTHIP IAAGERMFSR
FEFKRVLENG GVSILQPDLS HAGGITECHK IASMAEAYDV ALAPHCPLGP IALAACLHID
FVSRNAIFQE QSMGIHYNQG AELLDFVRNK NDFDMTGGHF YPLTKPGLGV EIDEEQVIFR
SQNVADWRNP LWRHDDGSVA EW
//
