ID A0A1R1BHK1_9BACL Unreviewed; 382 AA.
AC A0A1R1BHK1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Galactonate dehydratase {ECO:0000313|EMBL:OMF07248.1};
GN ORFNames=BK127_29580 {ECO:0000313|EMBL:OMF07248.1};
OS Paenibacillus sp. FSL H7-0331.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1920421 {ECO:0000313|EMBL:OMF07248.1, ECO:0000313|Proteomes:UP000187480};
RN [1] {ECO:0000313|EMBL:OMF07248.1, ECO:0000313|Proteomes:UP000187480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0331 {ECO:0000313|EMBL:OMF07248.1,
RC ECO:0000313|Proteomes:UP000187480};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. GalD subfamily. {ECO:0000256|ARBA:ARBA00010339}.
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:OMF07248.1}.
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DR EMBL; MRTH01000028; OMF07248.1; -; Genomic_DNA.
DR RefSeq; WP_076235701.1; NZ_MRTH01000028.1.
DR AlphaFoldDB; A0A1R1BHK1; -.
DR STRING; 1920421.BK127_29580; -.
DR OrthoDB; 9775391at2; -.
DR Proteomes; UP000187480; Unassembled WGS sequence.
DR GO; GO:0008869; F:galactonate dehydratase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR GO; GO:0034194; P:D-galactonate catabolic process; IEA:InterPro.
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 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000187480}.
FT DOMAIN 125..230
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 382 AA; 42290 MW; 1E9034B56CAAFBA2 CRC64;
MKIKSMELFK VPPRWLFLKI TTDDGIVGWG EPVVEGKADT VRTAVEEMSE YLIGKDPGNI
EDLWQVLYRG GFYRGGPILS SAISGIEQAL WDIKGKKLGV PVYDLLGGPV RDKMRVYAWI
GGDKPSDVAE AAKEKIAQGY TAIKMNGTSE MEWIDSPAKI EEAVERLAAV RSAIGNSNGI
GVDLHGRVHK TMAKVLIKEM EPFKPMFIEE PVLAENYEVI HEITKGSSVP IATGERMYTR
WDFKRLLTHG GVDIIQPDLS HAGGIWEVRK IAAMAEAFDV AVAPHCPLGP IALASSLQLD
FCTPNAFIQE QSLGIHYNQG SDLLDYLVDP GVFDYEGGFV KRLTKPGLGI EIDEAKVREM
AAIGHQWRNP VWRNEDGVVT EW
//
