ENO_MYCPN
ID ENO_MYCPN Reviewed; 456 AA.
AC P75189; Q50324;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
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=MPN_606;
GN ORFNames=MP236;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 309-456.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8604303; DOI=10.1093/nar/24.4.628;
RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.;
RT "Sequence analysis of 56 kb from the genome of the bacterium Mycoplasma
RT pneumoniae comprising the dnaA region, the atp operon and a cluster of
RT ribosomal protein genes.";
RL Nucleic Acids Res. 24:628-639(1996).
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;
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 -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
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; U00089; AAB95884.1; -; Genomic_DNA.
DR EMBL; U43738; AAC43651.1; -; Genomic_DNA.
DR PIR; S73562; S73562.
DR RefSeq; NP_110295.1; NC_000912.1.
DR RefSeq; WP_010874963.1; NC_000912.1.
DR AlphaFoldDB; P75189; -.
DR SMR; P75189; -.
DR IntAct; P75189; 6.
DR STRING; 272634.MPN_606; -.
DR EnsemblBacteria; AAB95884; AAB95884; MPN_606.
DR GeneID; 66608709; -.
DR KEGG; mpn:MPN_606; -.
DR PATRIC; fig|272634.6.peg.669; -.
DR HOGENOM; CLU_031223_2_1_14; -.
DR OMA; EFMIIPV; -.
DR BioCyc; MetaCyc:MON-551; -.
DR BioCyc; MPNE272634:G1GJ3-981-MON; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
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 3: Inferred from homology;
KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome;
KW Secreted.
FT CHAIN 1..456
FT /note="Enolase"
FT /id="PRO_0000133930"
FT ACT_SITE 219
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 362
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 362
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 389..392
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 413
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT CONFLICT 309..311
FT /note="IED -> HRS (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 327..332
FT /note="TLGQHI -> HWSTH (in Ref. 2; AAC43651)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 49228 MW; 5B4B5442ADDC0E86 CRC64;
MSAQTGTDLF KIADLFAYQV FDSRGFPTVA CVVKLASGHT GEAMVPSGAS TGEKEAIELR
DGDPKAYFGK GVSQAVQNVN QTIAPKLIGL NATDQAAIDA LMIQLDGTPN KAKLGANAIL
AVSLAVAKAA ASAQKTSLFK YLANQVMGLN KTEFILTVPM LNVINGGAHA DNNIDFQEFM
IMPLGANSMH QALKMASETF HALQKLLKQR GLNTNKGDEG GFAPNLKLAE EALDLMVEAI
KAAGYQPGSD IAIALDVAAS EFYDDTTKRY VFKKGIKAKI LDEKEWSLTT AQMIAYLKKL
TEQYPIISIE DGLSEHDWEG METLTKTLGQ HIQIVGDDLY CTNPAIAEKG VAHKATNSIL
IKLNQIGTLT ETIKAINIAK DANWSQVISH RSGETEDTTI ADLAVAACTG QIKTGSMSRS
ERIAKYNRLL QIELELGNNA KYLGWNTFKN IKPQKA
