ID A0A2T4JSI4_9RHOB Unreviewed; 386 AA.
AC A0A2T4JSI4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Enolase {ECO:0000313|EMBL:PTE20868.1};
GN ORFNames=C5F48_15260 {ECO:0000313|EMBL:PTE20868.1};
OS Cereibacter changlensis JA139.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cereibacter.
OX NCBI_TaxID=1188249 {ECO:0000313|EMBL:PTE20868.1, ECO:0000313|Proteomes:UP000241010};
RN [1] {ECO:0000313|EMBL:PTE20868.1, ECO:0000313|Proteomes:UP000241010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA139 {ECO:0000313|EMBL:PTE20868.1,
RC ECO:0000313|Proteomes:UP000241010};
RA Meyer T.E., Miller S., Lodha T., Gandham S., Chintalapati S.,
RA Chintalapati V.R.;
RT "Cereibacter changlensis.";
RL Submitted (MAR-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:PTE20868.1}.
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DR EMBL; PZKG01000078; PTE20868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4JSI4; -.
DR OrthoDB; 9802699at2; -.
DR Proteomes; UP000241010; 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:0000287; F:magnesium ion binding; IEA:UniProt.
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:UP000241010}.
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; 42332 MW; BE63C8C3A6C39BCA CRC64;
MTQSHPVQHA TQGDRIAWIR LSAIHLPLKT PISDAKVLTG RQKPLTEVAC LFAEIETVEG
HSGIGFSYSK RAGGPGQFEH AKEIAPVLLG EDPNDIGKLW RKLAWAGASV GRSGLAVQAI
AAFDIAFWDL KAKRAGLPLS KLLGAHRDSV QCYNTSGGFL SSPLEEVLDN VERSIAQGIG
GIKIKVGQPD MAEDLRRVAA VNDRIAGRVS LMVDANQQWD RPAAMRACRQ LEAFNLVWIE
EPLDAYDSEG HAALAAALDT PIATGEMLSS VAEHVDLIQK NAVDFIQPDA PRVGGITQFL
RICALAEEKK LKLAPHFAME IHLHLAAAYE FEPWVEHFDW LDPLFNERLE NRNGRMIVPN
RPGLGFTLSE QALGWKRAEA AFGRRP
//
