ENO_CHLTB
ID ENO_CHLTB Reviewed; 424 AA.
AC B0BA40;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=CTLon_0844;
OS Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471473;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCH-1/proctitis;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM884177; CAP07241.1; -; Genomic_DNA.
DR RefSeq; WP_009873920.1; NC_010280.2.
DR PDB; 6O4N; X-ray; 1.80 A; A/B=1-424.
DR PDBsum; 6O4N; -.
DR AlphaFoldDB; B0BA40; -.
DR SMR; B0BA40; -.
DR KEGG; ctl:CTLon_0844; -.
DR HOGENOM; CLU_031223_2_1_0; -.
DR OMA; EFMIIPV; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000000794; 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 3D-structure; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding;
KW Secreted.
FT CHAIN 1..424
FT /note="Enolase"
FT /id="PRO_1000115848"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 335
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 283
FT /ligand="substrate"
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 335
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 362..365
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT STRAND 5..15
FT /evidence="ECO:0007829|PDB:6O4N"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:6O4N"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:6O4N"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 110..128
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:6O4N"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:6O4N"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 177..197
FT /evidence="ECO:0007829|PDB:6O4N"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 217..230
FT /evidence="ECO:0007829|PDB:6O4N"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:6O4N"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:6O4N"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:6O4N"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 291..301
FT /evidence="ECO:0007829|PDB:6O4N"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:6O4N"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:6O4N"
FT TURN 311..315
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:6O4N"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 342..353
FT /evidence="ECO:0007829|PDB:6O4N"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:6O4N"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 372..379
FT /evidence="ECO:0007829|PDB:6O4N"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:6O4N"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 393..409
FT /evidence="ECO:0007829|PDB:6O4N"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:6O4N"
SQ SEQUENCE 424 AA; 45434 MW; E700B8BA4205EF6F CRC64;
MFDVVISDIE AREILDSRGY PTLCVKVITN TGTFGEACVP SGASTGIKEA LELRDKDPKR
YQGKGVLQAI SNVEKVLVPA LQGFSVFDQI TADAIMIDAD GTPNKEKLGA NAILGVSLAL
AKAAANTLQR PLYRYLGGSF SHVLPCPMMN LINGGMHATN GLQFQEFMIR PISAPSLKEA
VRMGAEVFNA LKKILQNRQL ATGVGDEGGF APNLASNAEA LDLLLTAIET AGFTPREDIS
LALDCAASSF YNTQDKTYDG KSYADQVGIL AELCEHYPID SIEDGLAEED FEGWKLLSET
LGDRVQLVGD DLFVTNSALI AEGIAQGLAN AVLIKPNQIG TLTETAEAIR LATIQGYATI
LSHRSGETED TTIADLAVAF NTGQIKTGSL SRSERIAKYN RLMAIEEEMG PEALFQDSNP
FSKA
