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Database: UniProt
Entry: A0A3R9ARW7_9PSED
LinkDB: A0A3R9ARW7_9PSED
Original site: A0A3R9ARW7_9PSED 
ID   A0A3R9ARW7_9PSED        Unreviewed;       386 AA.
AC   A0A3R9ARW7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   03-MAY-2023, entry version 14.
DE   SubName: Full=Mandelate racemase/muconate lactonizing enzyme family protein {ECO:0000313|EMBL:RRV09313.1};
GN   ORFNames=EGJ27_05960 {ECO:0000313|EMBL:RRV09313.1};
OS   Pseudomonas sp. v388.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2479849 {ECO:0000313|EMBL:RRV09313.1, ECO:0000313|Proteomes:UP000268166};
RN   [1] {ECO:0000313|EMBL:RRV09313.1, ECO:0000313|Proteomes:UP000268166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=v388 {ECO:0000313|Proteomes:UP000268166};
RA   D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA   Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT   "Transmission dynamics of multidrug resistant bacteria on intensive care
RT   unit surfaces.";
RL   Submitted (OCT-2018) 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:RRV09313.1}.
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DR   EMBL; RHQN01000002; RRV09313.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R9ARW7; -.
DR   OrthoDB; 9782675at2; -.
DR   Proteomes; UP000268166; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000268166}.
FT   DOMAIN          164..261
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT   ACT_SITE        316
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT   BINDING         34..36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         70..71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         214
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         240
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT   BINDING         266
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT   BINDING         336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   SITE            289
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-4"
SQ   SEQUENCE   386 AA;  42586 MW;  F5AA9DAFA7F07108 CRC64;
     MLTQQQDRPS SDNDRIAWVK VSSVFLPLAN PISDAKVLTG RQKPMTEIAM LFVEIETVDG
     HSGLGFSYSK RAGGPGQFAH AKEIAPALIG ENPSDISKLW TKLCWAGASV GRSGLSTQAI
     GAFDVALWDL KAKRANLSLA RLLGSQRDSV RCYNTSGGFL HTPLDQLMKN TDLSREKGIG
     GIKLKVGQPD CAVDIQRVST VRKHLGENFP LMVDANQQWD RPTAQRMCRQ FEAYNLVWIE
     EPLDCYDAEG HAALAQQFDT PIATGEMLTS VAEHAEFIKL RGADYLMPDA PRVGGITPFL
     KVAAMAEQAG VMLAPHFAME LHVHLAATYP TEPWVEHFEW LEPLFNERLE TRDGRMLVPT
     RPGLGLSLSD QVKPWTAQEV EIGTRP
//
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