ENO_COXBU
ID ENO_COXBU Reviewed; 428 AA.
AC Q83B44;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=CBU_1674;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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 -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC complex involved in RNA processing and mRNA degradation.
CC {ECO:0000255|HAMAP-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; AE016828; AAO91170.1; -; Genomic_DNA.
DR RefSeq; NP_820656.1; NC_002971.3.
DR RefSeq; WP_005770583.1; NZ_CDBG01000001.1.
DR PDB; 3TQP; X-ray; 2.20 A; A/B=1-428.
DR PDBsum; 3TQP; -.
DR AlphaFoldDB; Q83B44; -.
DR SMR; Q83B44; -.
DR STRING; 227377.CBU_1674; -.
DR DNASU; 1209585; -.
DR EnsemblBacteria; AAO91170; AAO91170; CBU_1674.
DR GeneID; 1209585; -.
DR KEGG; cbu:CBU_1674; -.
DR PATRIC; fig|227377.7.peg.1663; -.
DR eggNOG; COG0148; Bacteria.
DR HOGENOM; CLU_031223_2_1_6; -.
DR OMA; EFMIIPV; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000002671; 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 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 Reference proteome; Secreted.
FT CHAIN 1..428
FT /note="Enolase"
FT /id="PRO_0000133877"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 337
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 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 337
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 364..367
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:3TQP"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:3TQP"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:3TQP"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 109..126
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:3TQP"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:3TQP"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:3TQP"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 177..197
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 217..230
FT /evidence="ECO:0007829|PDB:3TQP"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:3TQP"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:3TQP"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:3TQP"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:3TQP"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 293..303
FT /evidence="ECO:0007829|PDB:3TQP"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:3TQP"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:3TQP"
FT TURN 313..317
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 319..327
FT /evidence="ECO:0007829|PDB:3TQP"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 344..356
FT /evidence="ECO:0007829|PDB:3TQP"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 374..381
FT /evidence="ECO:0007829|PDB:3TQP"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:3TQP"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 395..411
FT /evidence="ECO:0007829|PDB:3TQP"
FT HELIX 419..422
FT /evidence="ECO:0007829|PDB:3TQP"
SQ SEQUENCE 428 AA; 46626 MW; B58295D02CC2BE61 CRC64;
MTATITDINA HEILDSRANP TLEVRVTLSS QAYGCAAVPS GASTGEREAV ELRDNDLERY
GGKGVLQAVE NVNGPIRDAL LGQDPRSQEE IDRIMIELDG TENKANLGAN AILGVSLAVA
YAAANNADLP LYRYLGGDGG PFSMPVPMMN IINGGAHATN NLDFQEFMIV PVGAPTFAEA
LRYGAEVFHA LKKRLVSRGL MSAVGDEGGF APDLPNNEAA FELILEAIED ANYVPGKDIY
LALDAASSEL YQNGRYDFEN NQLTSEEMID RLTEWTKKYP VISIEDGLSE NDWAGWKLLT
ERLENKVQLV GDDIFVTNPD ILEKGIKKNI ANAILVKLNQ IGTLTETLAT VGLAKSNKYG
VIISHRSGET EDTTIADLAV ATDARQIKTG SLCRSDRVAK YNRLLQIERE LNDQAPYAGK
EAFLFNRK
