ID A0A0Q7YLW1_9SPHN Unreviewed; 390 AA.
AC A0A0Q7YLW1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Mandelate racemase {ECO:0000313|EMBL:KQZ60590.1};
GN ORFNames=ASD67_14810 {ECO:0000313|EMBL:KQZ60590.1};
OS Sphingopyxis sp. Root1497.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1736474 {ECO:0000313|EMBL:KQZ60590.1, ECO:0000313|Proteomes:UP000051141};
RN [1] {ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|Proteomes:UP000051141};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ60590.1, ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|EMBL:KQZ60590.1,
RC ECO:0000313|Proteomes:UP000051141};
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:PIRSR634611-3};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR634611-3};
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:KQZ60590.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMGF01000005; KQZ60590.1; -; Genomic_DNA.
DR RefSeq; WP_056348750.1; NZ_LMGF01000005.1.
DR AlphaFoldDB; A0A0Q7YLW1; -.
DR STRING; 1736474.ASD67_14810; -.
DR OrthoDB; 9802699at2; -.
DR Proteomes; UP000051141; Unassembled WGS sequence.
DR GO; GO:0047808; F:D(-)-tartrate dehydratase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03326; MR_like_1; 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; IPR034611; D-tartrate_dehydratase.
DR InterPro; IPR034593; DgoD-like.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR PANTHER; PTHR48080:SF5; D(-)-TARTRATE DEHYDRATASE; 1.
DR PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR SFLD; SFLDF00118; D-tartrate_dehydratase; 1.
DR SFLD; SFLDS00001; Enolase; 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:PIRSR634611-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR634611-3}.
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="acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-1"
FT ACT_SITE 323
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-1"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-3"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-3"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-3"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-2"
FT SITE 56
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-4"
FT SITE 183
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-4"
FT SITE 293
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-4"
FT SITE 342
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634611-4"
SQ SEQUENCE 390 AA; 43248 MW; 7D1B18CFE0FD9125 CRC64;
MTQPQIIDIV EVTKPISSPI RNAYIDFSKM TASLVAVVTN VVRDGRRVVG YGFNSNGRYG
QGGLIRERFR DRLIEAEPAS LLDTTGENFD PDKIWKTLMT NEKPGGHGER SVAVGTIDMA
VWDAVAKIAE KPLFRLLADM KGREANPRVF VYAAGGYYYP GKDDDALRAE MRGYIDRGYN
VVKMKIGGES LAIDRRRIES VLQEIEGDAQ LAVDANGRFD TLTAIEYAKA LRDYPLFWYE
EAGDPLDYKL QAALAEFYPG SMATGENLFS HQDARNLLRY GGMRPDRDYL QMDCALSYGL
VEYLRTLDAL AECGWSPSRC IPHGGHQMSL NIAAGLGLGG NESYPDLFQP YGGFPDTVKV
EDGHIVMPDL PGIGFEGKSD LIKVMRELAE
//
