ID A0A240A540_SERFI Unreviewed; 382 AA.
AC A0A240A540;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:SNV78270.1};
GN ORFNames=SAMEA4384070_00012 {ECO:0000313|EMBL:SNV78270.1};
OS Serratia ficaria.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=61651 {ECO:0000313|EMBL:SNV78270.1, ECO:0000313|Proteomes:UP000215134};
RN [1] {ECO:0000313|EMBL:SNV78270.1, ECO:0000313|Proteomes:UP000215134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12148 {ECO:0000313|EMBL:SNV78270.1,
RC ECO:0000313|Proteomes:UP000215134};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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; LT906479; SNV78270.1; -; Genomic_DNA.
DR RefSeq; WP_061797832.1; NZ_QTUE01000001.1.
DR AlphaFoldDB; A0A240A540; -.
DR STRING; 1411141.GCA_001590885_02809; -.
DR GeneID; 75025208; -.
DR KEGG; sfj:SAMEA4384070_0012; -.
DR OrthoDB; 103536at2; -.
DR UniPathway; UPA00081; UER00518.
DR Proteomes; UP000215134; Chromosome 1.
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; SFLDG00179; mandelate_racemase; 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:SNV78270.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01289};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01289};
KW Reference proteome {ECO:0000313|Proteomes:UP000215134}.
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; 42334 MW; 24D7CAC9EB2718E8 CRC64;
MKITKLTTYR LPPRWMFLKI ETDEGVVGWG EPVIEGRARS VEAAVHELAE YVVGQDPARI
NDIWQTLYRG GFYRGGPILM SAIAGIDQAL WDIKGKALGV PVYQLLGGLV RDKIKAYSWV
GGDRPADVIS GINTLTEIGF DTFKLNGCEE MGIIDSARKV DAAVAVVAQI REAFGNRIEF
GLDFHGRVDA PMAKILIKEL EPYRPLFIEE PVLAEQAEYY PRLAAQTHIP IAAGERMYSR
FDFKRVLADG GLAIIQPDLS HAGGITECFK IAAMAESYDV ALAPHCPLGP IALAACLHVD
FVARNAVFQE QSMGIHYNQG AELLDYVVNK DDFKMTDGHF YPLTKPGLGV EIDEELVIAR
SKQAPDWRNP VWRYPDGAVA EW
//
