ID H1SHW0_9BURK Unreviewed; 385 AA.
AC H1SHW0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Mandelate racemase/muconate lactonizing protein {ECO:0000313|EMBL:EHP37885.1};
GN ORFNames=OR16_40314 {ECO:0000313|EMBL:EHP37885.1};
OS Cupriavidus basilensis OR16.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP37885.1, ECO:0000313|Proteomes:UP000005808};
RN [1] {ECO:0000313|EMBL:EHP37885.1, ECO:0000313|Proteomes:UP000005808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR16 {ECO:0000313|EMBL:EHP37885.1,
RC ECO:0000313|Proteomes:UP000005808};
RX PubMed=22461549; DOI=10.1128/JB.06752-11;
RA Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA Nagy I., Horvath B., Nagy I., Kukolya J.;
RT "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL J. Bacteriol. 194:2109-2110(2012).
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:EHP37885.1}.
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DR EMBL; AHJE01000172; EHP37885.1; -; Genomic_DNA.
DR RefSeq; WP_006164171.1; NZ_AHJE01000172.1.
DR AlphaFoldDB; H1SHW0; -.
DR PATRIC; fig|1127483.3.peg.8017; -.
DR OrthoDB; 8609034at2; -.
DR Proteomes; UP000005808; 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 163..260
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT ACT_SITE 315
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT BINDING 33..35
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 69..70
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT SITE 288
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-4"
SQ SEQUENCE 385 AA; 41993 MW; D1D4574D80F19892 CRC64;
MTMQHQQKTG ANDNIASIRL SSVYLPLATP ISDAKVLTGR QKPMTEIAIL FAEIETQGGG
KGIGFSYSKR AGGPGQFAHA KEIAPALIGE DANDIARLWN KLIWAGASVG RSGLATQAIG
AFDVALWDLK AKRANLPLAK LLGAHRDSVK CYNTSGGFLH TPLDQLLVNA SKSVEKGIGG
IKLKVGQPDC AADIKRVETV RKHLGDGFPL MVDANQQWDR PTAQRMCRIL EQFNLIWIEE
PLDAYDCEGH AALAAQFDTP IATGEMLTSV AEHWDLIRHR AADYLMPDGP RVGGITPFLT
VATLADHAGL MIAPHFAMEL HVHLAAAYSR EPWVEHFEWL EPLFNERLEI KDGRMLVPTR
PGIGVSLSGQ VAGWTREEAE FGAKR
//
