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Database: UniProt
Entry: A0A0L8LQR8_9ACTN
LinkDB: A0A0L8LQR8_9ACTN
Original site: A0A0L8LQR8_9ACTN 
ID   A0A0L8LQR8_9ACTN        Unreviewed;       377 AA.
AC   A0A0L8LQR8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Mandelate racemase/muconate lactonizing protein {ECO:0000313|EMBL:KOG40543.1};
GN   ORFNames=ADK74_23915 {ECO:0000313|EMBL:KOG40543.1};
OS   Streptomyces decoyicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=249567 {ECO:0000313|EMBL:KOG40543.1, ECO:0000313|Proteomes:UP000037606};
RN   [1] {ECO:0000313|Proteomes:UP000037606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2666 {ECO:0000313|Proteomes:UP000037606};
RG   Consortium for Microbial Forensics and Genomics (microFORGE);
RA   Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA   Blagden T., Winegar R.A.;
RL   Submitted (JUL-2015) 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};
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:KOG40543.1}.
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DR   EMBL; LGUU01000244; KOG40543.1; -; Genomic_DNA.
DR   RefSeq; WP_053209776.1; NZ_LGUU01000244.1.
DR   AlphaFoldDB; A0A0L8LQR8; -.
DR   PATRIC; fig|249567.6.peg.5311; -.
DR   Proteomes; UP000037606; 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   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; 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; SFLDS00001; Enolase; 1.
DR   SFLD; SFLDF00134; L-talarate/galactarate_dehydra; 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.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR633978-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR633978-3}.
FT   DOMAIN          156..253
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT   ACT_SITE        308
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT   BINDING         26..28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         62..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         206
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT   BINDING         258
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT   BINDING         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   SITE            281
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-4"
SQ   SEQUENCE   377 AA;  40502 MW;  B364D7D0AD08D346 CRC64;
     MTLTTDRIVT VSVSFVRLPL PEPVSDAKVL TGRQKPLVEV ALVFARIVTE AGLTGLGFGY
     AKRAGGPGLY AHAREIAPEL IGEDPSDIGR LWRKLVWAGA SMGRSGLAVQ AVAAFDIALW
     DLKARRAGLP LAKLLGAHRS AVPCYNTSGG FLSLPVEQVL ENADTALARG IGGIKIKVGQ
     PDPAADLRRV ETVRGHLGDG VPMMVDANQQ WDRATAQRIG RTLEQFQLAW IEEPLDAYDA
     EGHAALAASL DTPVATGEML TGAEEHTRLI EAGAADFVQP DAPRVGGITP FLRVMALADH
     KGLSLAPHFV MEVHLHLAAA YPGTAWVEHF DWLEPLFQER LELRDGRMCV PDRPGLGLSL
     SDRAMAWTVE RCEASAG
//
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