ID V6ARM4_9ARCH Unreviewed; 412 AA.
AC V6ARM4;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Enolase {ECO:0000256|HAMAP-Rule:MF_00318};
DE EC=4.2.1.11 {ECO:0000256|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000256|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000256|HAMAP-Rule:MF_00318};
GN Name=eno {ECO:0000256|HAMAP-Rule:MF_00318,
GN ECO:0000313|EMBL:CDI05175.1};
GN ORFNames=NITUZ_140250 {ECO:0000313|EMBL:CDI05175.1}, NUZ5A_50219
GN {ECO:0000313|EMBL:CAE6493844.1};
OS Candidatus Nitrosotenuis uzonensis.
OC Archaea; Nitrososphaerota; Nitrosotenuis.
OX NCBI_TaxID=1407055 {ECO:0000313|EMBL:CDI05175.1, ECO:0000313|Proteomes:UP000018159};
RN [1] {ECO:0000313|EMBL:CDI05175.1, ECO:0000313|Proteomes:UP000018159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N4 {ECO:0000313|EMBL:CDI05175.1,
RC ECO:0000313|Proteomes:UP000018159};
RX DOI=10.1371/journal.pone.0080835;
RA Lebedeva E.V., Hatzenpichler R., Pelletier E., Schuster N., Hauzmayer S.,
RA Bulaev A., Grigor'eva N.V., Galushko A., Schmid M., Palatinszky M.,
RA Le Paslier D., Daims H., Wagner M.;
RT "Enrichment and Genome Sequence of the Group I.1a Ammonia-Oxidizing
RT Archaeon ?Ca. Nitrosotenuis uzonensis? Representing a Clade Globally.";
RL PLoS ONE 0:0-0(2013).
RN [2] {ECO:0000313|EMBL:CDI05175.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=N4 {ECO:0000313|EMBL:CDI05175.1};
RA Regsiter A.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAE6493844.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Candidatus Nitrosotenuis uzonensis 5A
RC {ECO:0000313|EMBL:CAE6493844.1};
RA Han P.;
RL Submitted (FEB-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate
CC into phosphoenolpyruvate. It is essential for the degradation of
CC carbohydrates via glycolysis. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_00318};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|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:0000256|HAMAP-Rule:MF_00318}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|ARBA:ARBA00005031,
CC ECO:0000256|HAMAP-Rule:MF_00318}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318}.
CC Secreted {ECO:0000256|HAMAP-Rule:MF_00318}. Cell surface
CC {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_00318}.
CC -!- SIMILARITY: Belongs to the enolase family.
CC {ECO:0000256|ARBA:ARBA00009604, ECO:0000256|HAMAP-Rule:MF_00318}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDI05175.1}.
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DR EMBL; CAJNAQ010000005; CAE6493844.1; -; Genomic_DNA.
DR EMBL; CBTY010000006; CDI05175.1; -; Genomic_DNA.
DR RefSeq; WP_048194627.1; NZ_CBTY010000006.1.
DR AlphaFoldDB; V6ARM4; -.
DR STRING; 1407055.NITUZ_140250; -.
DR OrthoDB; 8680at2157; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000018159; Unassembled WGS sequence.
DR Proteomes; UP000655759; Unassembled WGS sequence.
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 Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 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; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; ENOLASE; 1.
DR PANTHER; PTHR11902:SF1; ENOLASE; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00318};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00318};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00318};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00318};
KW Secreted {ECO:0000256|HAMAP-Rule:MF_00318}.
FT DOMAIN 4..125
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 130..405
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT ACT_SITE 199
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-1"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-1"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 331
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 358..361
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
SQ SEQUENCE 412 AA; 45044 MW; 54FECC1082745482 CRC64;
MPKITSVKGR LVYNSRGSKT IEIDIISDKR YLGRACAPSG ASVGKYEAQS FADNKPEKSL
QILNENIKKF IGLDSDDLKS IQSQIRKIDN TPNYSKIGGA VAYSLTIAAT DSAAKALDEP
MFKIISQTKR PKFPFPLGNI LGGGAHAGPG TPDIQEILIC SIGAKSPREA IERNFAVHRE
LGKLLQESDS RFTNGRGDEG GWAPQMDNEE ALEISAKACE RLGYTLGKEV ALGVDFASST
QWDEKKKKYV YERAGFENTP EEQIDFASNI IKKYKLIYAE DAVHEEAFSE MAIIRKKFPR
TYVTGDDLTV TNPKILKKAI IKKSCSGVIL KVNQAGSLYD ALEFAQIATK NKIGIITSHR
SGESTDHQIS HIGVATGSKM LKVGVLGGER VSKLNELIRL SEHSLISGMA EV
//
