ENO_MYCTU
ID ENO_MYCTU Reviewed; 429 AA.
AC P9WNL1; L0T876; P96377;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
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=Rv1023;
GN ORFNames=MTCY10G2.26c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP43773.1; -; Genomic_DNA.
DR PIR; B70623; B70623.
DR RefSeq; NP_215539.1; NC_000962.3.
DR RefSeq; WP_003898693.1; NZ_NVQJ01000018.1.
DR PDB; 6L7D; X-ray; 3.00 A; A=1-429.
DR PDB; 7CKP; X-ray; 2.90 A; A=1-428.
DR PDB; 7E4F; X-ray; 2.30 A; A=1-429.
DR PDBsum; 6L7D; -.
DR PDBsum; 7CKP; -.
DR PDBsum; 7E4F; -.
DR AlphaFoldDB; P9WNL1; -.
DR SMR; P9WNL1; -.
DR STRING; 83332.Rv1023; -.
DR PaxDb; P9WNL1; -.
DR DNASU; 886062; -.
DR GeneID; 886062; -.
DR KEGG; mtu:Rv1023; -.
DR TubercuList; Rv1023; -.
DR eggNOG; COG4948; Bacteria.
DR OMA; EFMIIPV; -.
DR PhylomeDB; P9WNL1; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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..429
FT /note="Enolase"
FT /id="PRO_0000133932"
FT ACT_SITE 204
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 154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 241
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 3..13
FT /evidence="ECO:0007829|PDB:7CKP"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:7CKP"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:7CKP"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 107..125
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:7CKP"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:7CKP"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:6L7D"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 174..194
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 214..228
FT /evidence="ECO:0007829|PDB:7CKP"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:7CKP"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:7CKP"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:6L7D"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:6L7D"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:6L7D"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:7CKP"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 291..301
FT /evidence="ECO:0007829|PDB:7CKP"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:7CKP"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:7CKP"
FT TURN 311..315
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:7CKP"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 342..355
FT /evidence="ECO:0007829|PDB:7CKP"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 372..379
FT /evidence="ECO:0007829|PDB:7CKP"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 393..409
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:7CKP"
FT HELIX 417..420
FT /evidence="ECO:0007829|PDB:7CKP"
SQ SEQUENCE 429 AA; 44962 MW; 5AC59531AC9F00E8 CRC64;
MPIIEQVRAR EILDSRGNPT VEVEVALIDG TFARAAVPSG ASTGEHEAVE LRDGGDRYGG
KGVQKAVQAV LDEIGPAVIG LNADDQRLVD QALVDLDGTP DKSRLGGNAI LGVSLAVAKA
AADSAELPLF RYVGGPNAHI LPVPMMNILN GGAHADTAVD IQEFMVAPIG APSFVEALRW
GAEVYHALKS VLKKEGLSTG LGDEGGFAPD VAGTTAALDL ISRAIESAGL RPGADVALAL
DAAATEFFTD GTGYVFEGTT RTADQMTEFY AGLLGAYPLV SIEDPLSEDD WDGWAALTAS
IGDRVQIVGD DIFVTNPERL EEGIERGVAN ALLVKVNQIG TLTETLDAVT LAHHGGYRTM
ISHRSGETED TMIADLAVAI GSGQIKTGAP ARSERVAKYN QLLRIEEALG DAARYAGDLA
FPRFACETK
