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Database: UniProt
Entry: A0A176Y9G6_9BRAD
LinkDB: A0A176Y9G6_9BRAD
Original site: A0A176Y9G6_9BRAD 
ID   A0A176Y9G6_9BRAD        Unreviewed;       389 AA.
AC   A0A176Y9G6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Mandelate racemase/muconate lactonizing protein {ECO:0000313|EMBL:OAE97724.1};
GN   ORFNames=AYJ54_34760 {ECO:0000313|EMBL:OAE97724.1};
OS   Bradyrhizobium centrolobii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1505087 {ECO:0000313|EMBL:OAE97724.1, ECO:0000313|Proteomes:UP000076959};
RN   [1] {ECO:0000313|EMBL:OAE97724.1, ECO:0000313|Proteomes:UP000076959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR 10245 {ECO:0000313|EMBL:OAE97724.1,
RC   ECO:0000313|Proteomes:UP000076959};
RA   Simoes-Araujo J.L.Sr., Barauna A.C., Silva K., Zilli J.E.;
RT   "Draft Genome Sequence of the Strain BR 10245 (Bradyrhizobium sp.) isolated
RT   from nodules of Centrolobium paraense.";
RL   Submitted (MAR-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};
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:OAE97724.1}.
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DR   EMBL; LUUB01000124; OAE97724.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176Y9G6; -.
DR   STRING; 1505087.AYJ54_34760; -.
DR   OrthoDB; 9802699at2; -.
DR   Proteomes; UP000076959; 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; 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.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR633978-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR633978-3}.
FT   DOMAIN          168..264
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT   ACT_SITE        319
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT   BINDING         38..40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         74..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT   BINDING         219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT   BINDING         269
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT   BINDING         339
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   SITE            292
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-4"
SQ   SEQUENCE   389 AA;  42891 MW;  49D6D9094B385EF1 CRC64;
     MLANPLAAGL AVGEATTDRI AWVRTSLVFL PLAQAISDAK VLTGRQKPLT EIAFLFAEIE
     TENGHSGIGY SYSKRAGGPG QFAHAREIAG ELIGEDPSDI ARLWDKLVWA GASVGRSGMS
     TQAIAAFDIA LWDLKAKRAK LPLAKLLGAH RDSVRCYNTS GGYLSMPIEE VKERITMALE
     KGIGAIKLKV GQPDPMVDLK RIEAVRNHIG DVPLAIDANQ QWDRTTALRF GRIAEQFNLT
     WIEEPLDAYD YEGHAALAAE LAAPVATGEM LTSVDEHYEL IRNNSVDFIQ PDAPRVGGIT
     PFLKIMALAD HKKLQLAPHY CMEIHLHLTA AYAREPWVEH FEWSEAMFNE KLEVMNGRMI
     VPNRPGLGFS LSEQARAWAR DVHEVGKRP
//
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