ENO_BACSU
ID ENO_BACSU Reviewed; 430 AA.
AC P37869; O32249;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318};
DE EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318};
GN Name=eno {ECO:0000255|HAMAP-Rule:MF_00318}; OrderedLocusNames=BSU33900;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8021172; DOI=10.1128/jb.176.13.3903-3910.1994;
RA Leyva-Vazquez M.A., Setlow P.;
RT "Cloning and nucleotide sequences of the genes encoding triose phosphate
RT isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis.";
RL J. Bacteriol. 176:3903-3910(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-10, AND PHOSPHORYLATION.
RX PubMed=1556067; DOI=10.1128/jb.174.8.2474-2477.1992;
RA Mitchell C., Morris P.W., Vary J.C.;
RT "Identification of proteins phosphorylated by ATP during sporulation of
RT Bacillus subtilis.";
RL J. Bacteriol. 174:2474-2477(1992).
RN [4]
RP CHARACTERIZATION, AND SUBUNIT.
RX PubMed=9988532; DOI=10.1023/a:1020790604887;
RA Brown C.K., Kuhlman P.L., Mattingly S., Slates K., Calie P.J., Farrar W.W.;
RT "A model of the quaternary structure of enolases, based on structural and
RT evolutionary analysis of the octameric enolase from Bacillus subtilis.";
RL J. Protein Chem. 17:855-866(1998).
RN [5]
RP SUBSTRATE BINDING AT LYS-339, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=168;
RX PubMed=15003462; DOI=10.1016/j.jmb.2003.12.082;
RA Boeel G., Pichereau V., Mijakovic I., Maze A., Poncet S., Gillet S.,
RA Giard J.-C., Hartke A., Auffray Y., Deutscher J.;
RT "Is 2-phosphoglycerate-dependent automodification of bacterial enolases
RT implicated in their export?";
RL J. Mol. Biol. 337:485-496(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141; SER-259; TYR-281 AND
RP SER-325, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
RN [7]
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=19193632; DOI=10.1074/mcp.m800546-mcp200;
RA Commichau F.M., Rothe F.M., Herzberg C., Wagner E., Hellwig D.,
RA Lehnik-Habrink M., Hammer E., Volker U., Stulke J.;
RT "Novel activities of glycolytic enzymes in Bacillus subtilis: interactions
RT with essential proteins involved in mRNA processing.";
RL Mol. Cell. Proteomics 8:1350-1360(2009).
RN [8]
RP INTERACTION WITH RNY, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=21803996; DOI=10.1128/jb.05500-11;
RA Lehnik-Habrink M., Newman J., Rothe F.M., Solovyova A.S., Rodrigues C.,
RA Herzberg C., Commichau F.M., Lewis R.J., Stulke J.;
RT "RNase Y in Bacillus subtilis: a natively disordered protein that is the
RT functional equivalent of RNase E from Escherichia coli.";
RL J. Bacteriol. 193:5431-5441(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), POSSIBLE COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH PFKA; RNY, AND
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=22198292; DOI=10.1016/j.jmb.2011.12.024;
RA Newman J.A., Hewitt L., Rodrigues C., Solovyova A.S., Harwood C.R.,
RA Lewis R.J.;
RT "Dissection of the network of interactions that links RNA processing with
RT glycolysis in the Bacillus subtilis degradosome.";
RL J. Mol. Biol. 416:121-136(2012).
CC -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate
CC into phosphoenolpyruvate. It is essential for the degradation of
CC carbohydrates via glycolysis. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00318};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: The covalent binding to the substrate at Lys-339
CC of a small fraction of enolase causes inactivation of the enzyme, and
CC possibly serves as a signal for the export of the protein
CC (PubMed:15003462). Citrate acts as a non-competitive inhibitor for both
CC forward and reverse reactions, probably by chelating Mg(2+)
CC (PubMed:22198292). {ECO:0000269|PubMed:15003462,
CC ECO:0000269|PubMed:22198292}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.44 uM for 2-phospho-D-glycerate {ECO:0000269|PubMed:22198292};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
CC -!- SUBUNIT: Homooctamer. Component of a possible RNA degradosome complex
CC composed of rny, rnjA, rnjB, pnp, pfkA and eno (PubMed:19193632)
CC (although rnjA and rnjB's presence is unclear).
CC {ECO:0000269|PubMed:19193632, ECO:0000269|PubMed:21803996,
CC ECO:0000269|PubMed:22198292, ECO:0000269|PubMed:9988532}.
CC -!- INTERACTION:
CC P37869; O31774: rny; NbExp=2; IntAct=EBI-6415666, EBI-6415578;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318,
CC ECO:0000269|PubMed:15003462}. Secreted {ECO:0000255|HAMAP-
CC Rule:MF_00318, ECO:0000269|PubMed:15003462}. Cell surface
CC {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15003462}.
CC Note=Fractions of enolase are present in both the cytoplasm and on the
CC cell surface. The export of enolase possibly depends on the covalent
CC binding to the substrate at Lys-339; once secreted, it remains attached
CC to the cell surface.
CC -!- PTM: Phosphorylated during sporulation. {ECO:0000269|PubMed:1556067,
CC ECO:0000269|PubMed:17218307}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
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DR EMBL; L29475; AAA21681.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15395.1; -; Genomic_DNA.
DR PIR; B69620; B69620.
DR RefSeq; NP_391270.1; NC_000964.3.
DR RefSeq; WP_003228333.1; NZ_JNCM01000033.1.
DR PDB; 4A3R; X-ray; 2.20 A; A/B/C/D=1-430.
DR PDBsum; 4A3R; -.
DR AlphaFoldDB; P37869; -.
DR SMR; P37869; -.
DR IntAct; P37869; 2.
DR MINT; P37869; -.
DR STRING; 224308.BSU33900; -.
DR iPTMnet; P37869; -.
DR jPOST; P37869; -.
DR PaxDb; P37869; -.
DR PRIDE; P37869; -.
DR EnsemblBacteria; CAB15395; CAB15395; BSU_33900.
DR GeneID; 938641; -.
DR KEGG; bsu:BSU33900; -.
DR PATRIC; fig|224308.179.peg.3675; -.
DR eggNOG; COG0148; Bacteria.
DR InParanoid; P37869; -.
DR OMA; EFMIIPV; -.
DR PhylomeDB; P37869; -.
DR BioCyc; BSUB:BSU33900-MON; -.
DR BRENDA; 4.2.1.11; 658.
DR SABIO-RK; P37869; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000001570; 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; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd03313; enolase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 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 PANTHER; PTHR11902; PTHR11902; 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 SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome; Secreted;
KW Sporulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1556067"
FT CHAIN 2..430
FT /note="Enolase"
FT /id="PRO_0000133841"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 339
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT BINDING 366..369
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT MOD_RES 281
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT CONFLICT 45
FT /note="E -> Q (in Ref. 1; AAA21681)"
FT /evidence="ECO:0000305"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:4A3R"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:4A3R"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:4A3R"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 108..126
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:4A3R"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:4A3R"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:4A3R"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 175..195
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 215..229
FT /evidence="ECO:0007829|PDB:4A3R"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:4A3R"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:4A3R"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:4A3R"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:4A3R"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:4A3R"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 267..280
FT /evidence="ECO:0007829|PDB:4A3R"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 295..305
FT /evidence="ECO:0007829|PDB:4A3R"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:4A3R"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:4A3R"
FT TURN 315..319
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:4A3R"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:4A3R"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 376..383
FT /evidence="ECO:0007829|PDB:4A3R"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 397..413
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:4A3R"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:4A3R"
SQ SEQUENCE 430 AA; 46581 MW; C82B60F49D11AE68 CRC64;
MPYIVDVYAR EVLDSRGNPT VEVEVYTETG AFGRALVPSG ASTGEYEAVE LRDGDKDRYL
GKGVLTAVNN VNEIIAPELL GFDVTEQNAI DQLLIELDGT ENKGKLGANA ILGVSMACAR
AAADFLQIPL YQYLGGFNSK TLPVPMMNIV NGGEHADNNV DIQEFMIMPV GAPNFREALR
MGAQIFHSLK SVLSAKGLNT AVGDEGGFAP NLGSNEEALQ TIVEAIEKAG FKPGEEVKLA
MDAASSEFYN KEDGKYHLSG EGVVKTSAEM VDWYEELVSK YPIISIEDGL DENDWEGHKL
LTERLGKKVQ LVGDDLFVTN TKKLSEGIKN GVGNSILIKV NQIGTLTETF DAIEMAKRAG
YTAVISHRSG ETEDSTIADI AVATNAGQIK TGAPSRTDRV AKYNQLLRIE DQLAETAQYH
GINSFYNLNK
