ID A0A158JC73_9BURK Unreviewed; 387 AA.
AC A0A158JC73;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Mandelate racemase/muconate lactonizing protein {ECO:0000313|EMBL:SAL66019.1};
GN ORFNames=AWB65_06275 {ECO:0000313|EMBL:SAL66019.1};
OS Caballeronia humi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=326474 {ECO:0000313|EMBL:SAL66019.1, ECO:0000313|Proteomes:UP000054977};
RN [1] {ECO:0000313|EMBL:SAL66019.1, ECO:0000313|Proteomes:UP000054977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22934 {ECO:0000313|EMBL:SAL66019.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR633978-3};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR633978-3};
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DR EMBL; FCNW02000072; SAL66019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158JC73; -.
DR STRING; 326474.AWB65_06275; -.
DR OrthoDB; 8609034at2; -.
DR Proteomes; UP000054977; Unassembled WGS sequence.
DR GO; GO:0008867; F:galactarate dehydratase activity; IEA:InterPro.
DR GO; GO:1990594; F:L-altrarate 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 CDD; cd03316; MR_like; 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; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR033978; L-talarate_dehydratase.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR InterPro; IPR046945; RHMD-like.
DR PANTHER; PTHR13794; ENOLASE SUPERFAMILY, MANDELATE RACEMASE; 1.
DR PANTHER; PTHR13794:SF58; MITOCHONDRIAL ENOLASE SUPERFAMILY MEMBER 1; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDF00134; L-talarate/galactarate_dehydra; 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; PS00909; MR_MLE_2; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|PIRSR:PIRSR633978-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR633978-3}.
FT DOMAIN 165..262
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT ACT_SITE 317
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT BINDING 35..37
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 71..72
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT SITE 290
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-4"
SQ SEQUENCE 387 AA; 42490 MW; AB68B421734A4B00 CRC64;
MNAIDTRIAD TATVDRITWI RIASTFLPLA NPISDAKVLT GRQKPMTEIA ILFVEIETTD
GHRGLGFSYS KRAGGPGQFA HAKEIAPTLI GEDPSDIAKL WNKLAWAGAS VGRSGMAVQA
IGAFDVALWD LKAKRANLSL AKLLGSQRDS VRCYNTSGGF LHTPLDQLPT NTDASREKGI
GGIKLKVGQP DCALDIHRVE TVRKHLGDAF PLMVDANQQW DRPTAQRMCR TFEQFNLVWI
EEPLDCYDAE GHAALAAQFD TPIATGEMLT SVAEHWEFIK LRGADYLMPD APRVGGITPF
LKIAGLAEHA GLMLGPHFAM ELHVHLAACY PTEPWVEHFE WLEPLFNERL ETHGGRMIVP
TRPGLGLTLS ERVAGWTAQE VEIGNRA
//
