ENO_SYNP6
ID ENO_SYNP6 Reviewed; 430 AA.
AC Q5N3P4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=syc0886_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
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; AP008231; BAD79076.1; -; Genomic_DNA.
DR RefSeq; WP_011243198.1; NC_006576.1.
DR PDB; 4ROP; X-ray; 2.05 A; A=1-430.
DR PDB; 5J04; X-ray; 2.30 A; A/B=5-429.
DR PDBsum; 4ROP; -.
DR PDBsum; 5J04; -.
DR AlphaFoldDB; Q5N3P4; -.
DR SMR; Q5N3P4; -.
DR STRING; 269084.syc0886_c; -.
DR EnsemblBacteria; BAD79076; BAD79076; syc0886_c.
DR KEGG; syc:syc0886_c; -.
DR eggNOG; COG0148; Bacteria.
DR OMA; EFMIIPV; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000001175; 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..430
FT /note="Enolase"
FT /id="PRO_0000133991"
FT ACT_SITE 209
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 159
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 246
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 STRAND 8..18
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:4ROP"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 179..199
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 219..232
FT /evidence="ECO:0007829|PDB:4ROP"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 267..280
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 295..305
FT /evidence="ECO:0007829|PDB:4ROP"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:4ROP"
FT TURN 315..319
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 376..383
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:4ROP"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 397..413
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:4ROP"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:4ROP"
SQ SEQUENCE 430 AA; 45379 MW; A21B12D699866725 CRC64;
MPDDYGTQIA EITAREILDS RGRPTVEAEV HLEDGSVGLA QVPSGASTGT FEAHELRDDD
PSRYGGKGVQ KAVENVSAIE DALIGLSALD QEGLDKAMIA LDGTPNKKNL GANAILAVSL
ATAHAAATSL NLPLYRYLGG PLANVLPVPM MNVINGGAHA DNNVDFQEFM IMPVGAPSFK
EALRWGAEVF HALAKVLKDK GLATGVGDEG GFAPNLGSNK EALELLLTAI EAAGYKPGEQ
VALAMDVASS EFYKNGLYTC DGVSHEPAGM IGILADLVSQ YPIVSIEDGL QEDDWSNWKT
LTQQLGSTVQ LVGDDLFVTN PDRLQSGIEQ GVGNAVLIKL NQIGTLTETL RTIDLATRSG
YRSVISHRSG ETEDTTIADL AVATRAGQIK TGSLSRSERI AKYNRLLRIE AALGENALYA
GAIGLGPKGR
