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Database: UniProt
Entry: A0A0Q1C6B2_9FLAO
LinkDB: A0A0Q1C6B2_9FLAO
Original site: A0A0Q1C6B2_9FLAO 
ID   A0A0Q1C6B2_9FLAO        Unreviewed;       429 AA.
AC   A0A0Q1C6B2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
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:KQC32956.1};
GN   ORFNames=AAU57_06185 {ECO:0000313|EMBL:KQC32956.1};
OS   Nonlabens sp. YIK11.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Nonlabens.
OX   NCBI_TaxID=1453349 {ECO:0000313|EMBL:KQC32956.1, ECO:0000313|Proteomes:UP000051409};
RN   [1] {ECO:0000313|EMBL:KQC32956.1, ECO:0000313|Proteomes:UP000051409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIK11 {ECO:0000313|EMBL:KQC32956.1,
RC   ECO:0000313|Proteomes:UP000051409};
RA   Kwon Y.M., Kim S.-J.;
RT   "Complete genome of flavobacterium.";
RL   Submitted (APR-2015) 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:KQC32956.1}.
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DR   EMBL; LBMJ01000001; KQC32956.1; -; Genomic_DNA.
DR   RefSeq; WP_055412088.1; NZ_LBMJ01000001.1.
DR   AlphaFoldDB; A0A0Q1C6B2; -.
DR   STRING; 1453349.AAU57_06185; -.
DR   PATRIC; fig|1453349.3.peg.1285; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000051409; 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   CDD; cd03313; enolase; 1.
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; IPR020809; Enolase_CS.
DR   InterPro; IPR020811; Enolase_N.
DR   NCBIfam; TIGR01060; eno; 1.
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   SFLD; SFLDF00002; enolase; 1.
DR   SFLD; SFLDG00178; enolase; 1.
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.
DR   PROSITE; PS00164; ENOLASE; 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|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00318};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|HAMAP-Rule:MF_00318}.
FT   DOMAIN          4..133
FT                   /note="Enolase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01193"
FT   DOMAIN          138..428
FT                   /note="Enolase C-terminal TIM barrel"
FT                   /evidence="ECO:0000259|SMART:SM01192"
FT   ACT_SITE        204
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-1"
FT   ACT_SITE        340
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-1"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         241
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         288
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         315
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         340
FT                   /ligand="substrate"
FT                   /note="covalent; in inhibited form"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         367..370
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         391
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
SQ   SEQUENCE   429 AA;  46157 MW;  03C51BCDBE0BFE73 CRC64;
     MSTIIDVHAR QIFDSRGNPT VEVDVLTSNG IMGRAAVPSG ASTGEHEAVE LRDGGSDFMG
     KGVMKAVDNV NKTIADELRG VSVFEQNFID QTMIELDGTP NKANLGANAI LGVSLAVAKA
     AANELNQPLY KYIGGMSAAT LPVPMMNIIN GGSHSDAPIA FQEFMVMPVE AESFSEALKM
     GTEIFHHLKK VLHDRGLSTA VGDEGGFAPT LDGTEDALDT ILLAIKNAGY TPGKQIMIAL
     DCAAAEFFVD GKYDYTKFEG DKGVIRTSKE QAEYLADLAS KYPIISIEDG MDENDWDGWK
     MLTEIAGDKV QLVGDDLFVT NVERLSRGIK ENIANSILIK VNQIGTLTET IAAVNMAHKA
     GYTSVMSHRS GETEDNTIAD LAVALSTGQI KTGSASRSDR MAKYNQLLRI EEELNSSAYF
     PGRKAFRIS
//
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