ENO_ZYMMO
ID ENO_ZYMMO Reviewed; 429 AA.
AC P33675; O69010; Q5NM28;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
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=ZMO1608;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1400207; DOI=10.1128/jb.174.20.6548-6553.1992;
RA Burnett M.E., Liu J., Conway T.;
RT "Molecular characterization of the Zymomonas mobilis enolase (eno) gene.";
RL J. Bacteriol. 174:6548-6553(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Lee J., Jin S., Kang H.S.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 29191 / DSM 3580 / JCM 10190 / CECT 560 / NBRC 13756 / NCIMB
RC 11199 / NRRL B-4490 / ZM6;
RX PubMed=3026343; DOI=10.1042/bj2380275;
RA Pawluk A., Scopes R.K., Griffiths-Smith K.;
RT "Isolation and properties of the glycolytic enzymes from Zymomonas mobilis.
RT The five enzymes from glyceraldehyde-3-phosphate dehydrogenase through to
RT pyruvate kinase.";
RL Biochem. J. 238:275-281(1986).
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 ECO:0000269|PubMed:3026343}.
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, ECO:0000269|PubMed:3026343};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00318}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.08 mM for 2-phospho-D-glycerate {ECO:0000269|PubMed:3026343};
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. {ECO:0000269|PubMed:3026343}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}.
CC Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface
CC {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00318}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
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DR EMBL; M99380; AAA27686.1; -; Genomic_DNA.
DR EMBL; AF086791; AAC70360.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV90232.1; -; Genomic_DNA.
DR PIR; A45732; A45732.
DR PIR; T33721; T33721.
DR RefSeq; WP_011241362.1; NZ_CP035711.1.
DR AlphaFoldDB; P33675; -.
DR SMR; P33675; -.
DR STRING; 264203.ZMO1608; -.
DR PRIDE; P33675; -.
DR EnsemblBacteria; AAV90232; AAV90232; ZMO1608.
DR GeneID; 58027327; -.
DR KEGG; zmo:ZMO1608; -.
DR eggNOG; COG0148; Bacteria.
DR HOGENOM; CLU_031223_2_1_5; -.
DR OMA; EFMIIPV; -.
DR OrthoDB; 533698at2; -.
DR SABIO-RK; P33675; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000001173; 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; -; 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 Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome;
KW Secreted.
FT CHAIN 1..429
FT /note="Enolase"
FT /id="PRO_0000134018"
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:0000255|HAMAP-Rule:MF_00318"
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 /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
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 CONFLICT 186
FT /note="F -> S (in Ref. 2; AAC70360)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="Missing (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="G -> F (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="A -> P (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="G -> V (in Ref. 1; AAA27686)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..429
FT /note="ETEDTTIADLAVATNCGQIKTGSLCRSERIAKYNQLMRIEEELGSVAKYAGR
FT SVLRKAK -> GNRRHHDC (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 45743 MW; 557E9E258FD9F93E CRC64;
MTAIVSIHGR QVVDSRGNPT VEVDVTLEDG SFGRAAVPSG ASTGVHEAVE LRDGDKTRWG
GKGVTKAVHA VNNEIANAII GLEAEDQELI DQTMIKLDGT PNKGKFGANA ILGVSLAVAK
AAAEARGLPL YRYVGGTAAH VLPVPMMNIV NGGMHADNPI DFQEFMIAPV GASSINEAVR
IGTEVFHTLK KELSAKGMNT NVGDEGGFAP SLDSASSALD FIVDSISKAG YKPGEDVFIA
LDAASSEFYN KDQNIYDLKG EGRKLTSAQL VDYYVELCGK YPIYSIEDGL AEDDFEGWKI
LTEKLGDKVQ LVGDDLFVTN VKRLSDGIER GIANSLLVKF NQIGSLSETL AAVNMANDAS
YTAVMSHRSG ETEDTTIADL AVATNCGQIK TGSLCRSERI AKYNQLMRIE EELGSVAKYA
GRSVLRKAK
