ID A0A0S9N3I2_9BURK Unreviewed; 376 AA.
AC A0A0S9N3I2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Mandelate racemase/muconate lactonizing protein {ECO:0000313|EMBL:KQP39825.1};
GN ORFNames=ASF44_08890 {ECO:0000313|EMBL:KQP39825.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP39825.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP39825.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP39825.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP39825.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP39825.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQP39825.1}.
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DR EMBL; LMNA01000023; KQP39825.1; -; Genomic_DNA.
DR RefSeq; WP_056900622.1; NZ_LMNA01000023.1.
DR AlphaFoldDB; A0A0S9N3I2; -.
DR STRING; 1736318.ASF44_08890; -.
DR OrthoDB; 8609034at2; -.
DR Proteomes; UP000051759; 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; 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.
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:UP000051759}.
FT DOMAIN 154..251
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT ACT_SITE 306
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 60..61
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT SITE 279
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-4"
SQ SEQUENCE 376 AA; 41171 MW; EE508D8293C75C3D CRC64;
MTHDSIAHIR LSSCYLPLAN PISDAKVLTG RQKPMTEIAM LFAEIETKDG HKGLGFSYSK
RAGGPGQFAH AKEVAPALIG EDPSDIAKLW TKLCWAGASV GRSGLAVQAY GAFDVALYDL
KARRAGLSLS KLLGSQRDSV RCYNTSGGFL HTPIDQLSVN AAASIERGIG GIKLKVGQPD
GKIDIQRVEA VRKHLGDHVP LMVDANQQWD RPTAQRMCRI FEQFNLVWIE EPLDAYDHEG
HAALAATFDT PIATGEMLTS LSEHYDLIRH RAADYLMPDA PRVGGITPFL KIAALAEHAG
IALGPHFAME LHVHLGACYA TEPWVEHFDW LEPLFNERLE TKNGRMIVPT RPGLGLSLSE
QARGWTRETA EIGQRA
//
