ID A0A0G1RMM2_9BACT Unreviewed; 414 AA.
AC A0A0G1RMM2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
DE Flags: Fragment;
GN ORFNames=UX45_C0029G0017 {ECO:0000313|EMBL:KKU31208.1};
OS Candidatus Uhrbacteria bacterium GW2011_GWF2_46_218.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1619001 {ECO:0000313|EMBL:KKU31208.1, ECO:0000313|Proteomes:UP000034705};
RN [1] {ECO:0000313|EMBL:KKU31208.1, ECO:0000313|Proteomes:UP000034705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|ARBA:ARBA00005031}.
CC -!- SIMILARITY: Belongs to the enolase family.
CC {ECO:0000256|ARBA:ARBA00009604}.
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:KKU31208.1}.
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DR EMBL; LCMG01000029; KKU31208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1RMM2; -.
DR PATRIC; fig|1619001.3.peg.961; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000034705; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03313; enolase; 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 HAMAP; MF_00318; Enolase; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR NCBIfam; TIGR01060; eno; 1.
DR PANTHER; PTHR11902; ENOLASE; 1.
DR PANTHER; PTHR11902:SF1; ENOLASE; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SFLD; SFLDF00002; enolase; 1.
DR SFLD; SFLDG00178; enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 1..130
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 140..414
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 366..369
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKU31208.1"
SQ SEQUENCE 414 AA; 45976 MW; 10A764BC78269D6F CRC64;
EFIHAHEILD SRGNPTVQAT VLLKDGTTGV ASVPSGASTG IHEALELRDG DASRYGGKGV
LKAIRNIQTI ISKELIGMRV TEQRKIDNTM ILLDGTENKS RLGANAILAV SLACAHAGAK
AKKLPLYAYL RFAYDFPFKS YKLPLATMNV LNGGAHAGFA IDFQEFMIVP QQRRFKERVR
CGAEVFHTLG KELRKKGFST MVGDEGGYAV SFLHNEDALK FLMRAITQAG YQPGKDVMLA
MDPAVSELYD PKTKMYHLKK EGKDLTREDM IAKWEHWVEK YPIMSLEDGL EQDDWEGWHN
LTQRLGKKIT LVGDDLFVTN PVRLDLGIRE GVANAILIKL NQIGTLSETM DAISLAQKNH
YCISISHRSG ETSDTTIADL AVAVNADFIK TGSLCRSERV AKYNRLMEIE EEIL
//
