ID A0A174WL38_9BACE Unreviewed; 426 AA.
AC A0A174WL38;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Enolase {ECO:0000256|HAMAP-Rule:MF_00318};
DE EC=4.2.1.11 {ECO:0000256|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000256|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000256|HAMAP-Rule:MF_00318};
GN Name=eno {ECO:0000256|HAMAP-Rule:MF_00318,
GN ECO:0000313|EMBL:CUQ44967.1};
GN ORFNames=DW190_03265 {ECO:0000313|EMBL:RHH95253.1}, DW794_09380
GN {ECO:0000313|EMBL:RHD48926.1}, DWY26_06035
GN {ECO:0000313|EMBL:RGR72870.1}, DXA49_16610
GN {ECO:0000313|EMBL:RGY23522.1}, ERS852494_00783
GN {ECO:0000313|EMBL:CUO80944.1}, ERS852558_03395
GN {ECO:0000313|EMBL:CUQ44967.1}, F2Y31_04815
GN {ECO:0000313|EMBL:KAA5502570.1}, F2Y35_18105
GN {ECO:0000313|EMBL:KAA5488373.1}, F2Y36_15825
GN {ECO:0000313|EMBL:KAA5461574.1}, F2Y39_11740
GN {ECO:0000313|EMBL:KAA5476612.1}, NXW23_09520
GN {ECO:0000313|EMBL:UVQ98522.1};
OS Bacteroides caccae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=47678 {ECO:0000313|EMBL:CUQ44967.1, ECO:0000313|Proteomes:UP000095725};
RN [1] {ECO:0000313|Proteomes:UP000095657, ECO:0000313|Proteomes:UP000095725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5834880 {ECO:0000313|EMBL:CUO80944.1,
RC ECO:0000313|Proteomes:UP000095657}, and 2789STDY5834946
RC {ECO:0000313|EMBL:CUQ44967.1, ECO:0000313|Proteomes:UP000095725};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000283512, ECO:0000313|Proteomes:UP000284205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF24-29LB {ECO:0000313|EMBL:RGR72870.1,
RC ECO:0000313|Proteomes:UP000284205}, AM16-49B
RC {ECO:0000313|EMBL:RHH95253.1, ECO:0000313|Proteomes:UP000283512},
RC AM31-16AC {ECO:0000313|EMBL:RHD48926.1,
RC ECO:0000313|Proteomes:UP000284689}, and OF02-6LB
RC {ECO:0000313|EMBL:RGY23522.1, ECO:0000313|Proteomes:UP000284431};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000368418, ECO:0000313|Proteomes:UP000427825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A19 {ECO:0000313|EMBL:KAA5502570.1,
RC ECO:0000313|Proteomes:UP000368418}, BIOML-A21
RC {ECO:0000313|EMBL:KAA5488373.1, ECO:0000313|Proteomes:UP000491168},
RC BIOML-A25 {ECO:0000313|EMBL:KAA5476612.1,
RC ECO:0000313|Proteomes:UP000427825}, and BIOML-A31
RC {ECO:0000313|EMBL:KAA5461574.1, ECO:0000313|Proteomes:UP000475905};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
RN [4] {ECO:0000313|EMBL:UVQ98522.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BFG-474 {ECO:0000313|EMBL:UVQ98522.1};
RA Tisza M.J., Smith D., Dekker J.P.;
RT "Genome Sequencing of Bacteroides fragilis Group Isolates with Nanopore
RT Technology.";
RL Submitted (AUG-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate
CC into phosphoenolpyruvate. It is essential for the degradation of
CC carbohydrates via glycolysis. {ECO:0000256|HAMAP-Rule:MF_00318}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00318};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00318};
CC -!- ACTIVITY REGULATION: The covalent binding to the substrate causes
CC inactivation of the enzyme, and possibly serves as a signal for the
CC export of the protein. {ECO:0000256|HAMAP-Rule:MF_00318}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|ARBA:ARBA00005031,
CC ECO:0000256|HAMAP-Rule:MF_00318}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318}.
CC Secreted {ECO:0000256|HAMAP-Rule:MF_00318}. Cell surface
CC {ECO:0000256|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are
CC present in both the cytoplasm and on the cell surface. The export of
CC enolase possibly depends on the covalent binding to the substrate; once
CC secreted, it remains attached to the cell surface. {ECO:0000256|HAMAP-
CC Rule:MF_00318}.
CC -!- SIMILARITY: Belongs to the enolase family.
CC {ECO:0000256|ARBA:ARBA00009604, ECO:0000256|HAMAP-Rule:MF_00318}.
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DR EMBL; CZAI01000002; CUO80944.1; -; Genomic_DNA.
DR EMBL; CZBL01000016; CUQ44967.1; -; Genomic_DNA.
DR EMBL; VVYP01000021; KAA5461574.1; -; Genomic_DNA.
DR EMBL; VVYJ01000006; KAA5476612.1; -; Genomic_DNA.
DR EMBL; VVYF01000020; KAA5488373.1; -; Genomic_DNA.
DR EMBL; VVYD01000002; KAA5502570.1; -; Genomic_DNA.
DR EMBL; QRUO01000004; RGR72870.1; -; Genomic_DNA.
DR EMBL; QSCS01000029; RGY23522.1; -; Genomic_DNA.
DR EMBL; QSJD01000012; RHD48926.1; -; Genomic_DNA.
DR EMBL; QRKD01000001; RHH95253.1; -; Genomic_DNA.
DR EMBL; CP103166; UVQ98522.1; -; Genomic_DNA.
DR RefSeq; WP_005680321.1; NZ_WQQZ01000040.1.
DR STRING; 47678.ERS852494_00783; -.
DR GeneID; 75113517; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000095657; Unassembled WGS sequence.
DR Proteomes; UP000095725; Unassembled WGS sequence.
DR Proteomes; UP000283512; Unassembled WGS sequence.
DR Proteomes; UP000284205; Unassembled WGS sequence.
DR Proteomes; UP000284431; Unassembled WGS sequence.
DR Proteomes; UP000284689; Unassembled WGS sequence.
DR Proteomes; UP000368418; Unassembled WGS sequence.
DR Proteomes; UP000427825; Unassembled WGS sequence.
DR Proteomes; UP000475905; Unassembled WGS sequence.
DR Proteomes; UP000491168; Unassembled WGS sequence.
DR Proteomes; UP001060260; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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; SFLDS00001; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00318};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00318};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00318};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00318};
KW Pyruvate {ECO:0000313|EMBL:KAA5461574.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095657};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|HAMAP-Rule:MF_00318}.
FT DOMAIN 3..133
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 138..424
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-1"
FT ACT_SITE 340
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-1"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 340
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 367..370
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
SQ SEQUENCE 426 AA; 46158 MW; 5343438D42F58570 CRC64;
MKIEKIVARE ILDSRGNPTV EVDVVLESGI MGRASVPSGA STGEHEALEL RDGDKQRYGG
KGVQKAVDNV NKIIAPKLIG MSSLNQRGID YAMLALDGTK TKSNLGANAI LGVSLAVAKA
AASYLDLPLY RYIGGTNTYV MPVPMMNIIN GGSHSDAPIA FQEFMIRPVG APSFREGLRM
GAEVFHALKK VLKDRGLSTA VGDEGGFAPN LEGTEDALNS ILAAIKAAGY EPGKDVMIGM
DCASSEFYHD GIYDYTKFEG AKGKKRTAEE QIDYLEELIN KYPIDSIEDG MSENDWNGWK
KLTERIGNRC QLVGDDLFVT NVDFLAMGIE KGCANSILIK VNQIGSLTET LNAIEMAHRH
GYTTVTSHRS GETEDATIAD IAVATNSGQI KTGSLSRSDR MAKYNQLLRI EEELGDLAVY
GYKRIK
//
