ENO2_LACGA
ID ENO2_LACGA Reviewed; 432 AA.
AC Q042F4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Enolase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phosphoglycerate dehydratase 2 {ECO:0000255|HAMAP-Rule:MF_00318};
GN Name=eno2 {ECO:0000255|HAMAP-Rule:MF_00318}; OrderedLocusNames=LGAS_1305;
OS Lactobacillus gasseri (strain ATCC 33323 / DSM 20243 / BCRC 14619 / CIP
OS 102991 / JCM 1131 / KCTC 3163 / NCIMB 11718 / NCTC 13722 / AM63).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=324831;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33323 / DSM 20243 / BCRC 14619 / CIP 102991 / JCM 1131 / KCTC
RC 3163 / NCIMB 11718 / NCTC 13722 / AM63;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000413; ABJ60668.1; -; Genomic_DNA.
DR RefSeq; WP_003647015.1; NZ_WBMG01000002.1.
DR PDB; 4MKS; X-ray; 2.08 A; A/B=1-432.
DR PDBsum; 4MKS; -.
DR AlphaFoldDB; Q042F4; -.
DR SMR; Q042F4; -.
DR GeneID; 66535337; -.
DR KEGG; lga:LGAS_1305; -.
DR HOGENOM; CLU_031223_2_1_9; -.
DR OMA; EFMIIPV; -.
DR OrthoDB; 533698at2; -.
DR BioCyc; LGAS324831:G1G6Y-1300-MON; -.
DR BRENDA; 4.2.1.11; 2868.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000000664; 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..432
FT /note="Enolase 2"
FT /id="PRO_0000280856"
FT ACT_SITE 205
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 155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 242
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 4..13
FT /evidence="ECO:0007829|PDB:4MKS"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:4MKS"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:4MKS"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 108..126
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:4MKS"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:4MKS"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 175..195
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:4MKS"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:4MKS"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 271..280
FT /evidence="ECO:0007829|PDB:4MKS"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 295..305
FT /evidence="ECO:0007829|PDB:4MKS"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:4MKS"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:4MKS"
FT TURN 315..319
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:4MKS"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:4MKS"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 376..383
FT /evidence="ECO:0007829|PDB:4MKS"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:4MKS"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 397..413
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:4MKS"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:4MKS"
SQ SEQUENCE 432 AA; 46911 MW; 8567FD11E2EC934C CRC64;
MSVITDIHAR EVLDSRGNPT VEAEVYTELG GFGRAIVPSG ASTGEHEAVE LRDGDKSRFG
GQGVLTAVEN VNGEIAKAVI GLDVTDQRLI DQTMIDLDGT PNKGRLGANA ILSVSLASAR
AAADELGLPL YEYLGGPNAH VLPTPMMNVI NGGKHADNNV DIQEFMIMPV GAKSLHEAVR
MGAETFHTLK GLLQERGEST AVGDEGGFAP NLKNNEEPFE ILVEAIQRAG YKPGQDIAIA
FDCAASEFYN KDTKKYVTVA DGREYTAEEW TSLIEDLVDK YPVISVEDPL DENDWEGWKT
FTERLGDKVQ IVGDDLFVTN TSYLEKGIKM GVANSILIKL NQIGTLTETF EAIEMAKEAG
YTAVVSHRSG ETEDTTIADL VVATNAGQIK TGSMSRTDRI AKYNQLMRIE EALGSTAQYK
GIHSFYNLHK QF
