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Database: UniProt
Entry: A0A371BGT7_9SPHN
LinkDB: A0A371BGT7_9SPHN
Original site: A0A371BGT7_9SPHN 
ID   A0A371BGT7_9SPHN        Unreviewed;       424 AA.
AC   A0A371BGT7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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   ORFNames=DXH95_05250 {ECO:0000313|EMBL:RDV06809.1};
OS   Sphingorhabdus pulchriflava.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=2292257 {ECO:0000313|EMBL:RDV06809.1, ECO:0000313|Proteomes:UP000263833};
RN   [1] {ECO:0000313|Proteomes:UP000263833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GY_G {ECO:0000313|Proteomes:UP000263833};
RA   Kim S.-J., Jung G.-Y.;
RL   Submitted (AUG-2018) 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:RDV06809.1}.
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DR   EMBL; QRGP01000001; RDV06809.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371BGT7; -.
DR   OrthoDB; 9804716at2; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000263833; 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; SFLDS00001; 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}; Pyruvate {ECO:0000313|EMBL:RDV06809.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000263833};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|HAMAP-Rule:MF_00318}.
FT   DOMAIN          4..134
FT                   /note="Enolase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01193"
FT   DOMAIN          139..424
FT                   /note="Enolase C-terminal TIM barrel"
FT                   /evidence="ECO:0000259|SMART:SM01192"
FT   REGION          37..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-1"
FT   ACT_SITE        337
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-1"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         285
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         312
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         337
FT                   /ligand="substrate"
FT                   /note="covalent; in inhibited form"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         364..367
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
SQ   SEQUENCE   424 AA;  45055 MW;  1D351FFD62141C2E CRC64;
     MTAILDIHAR EILDSRGNPT VEVDVLLEDG SFGRAAVPSG ASTGAHEAVE KRDGDKGRYL
     GKGVRQAVEA VVNEISPLLA DYDAEDQEDI DAAMIALDGT ENKSRLGANA ILGVSLAVAK
     AAADARGLPL YRYVGGVNAK VLPVPMMNII NGGEHADNPI DFQEFMIMPV GADSLAEGVR
     WGSEIFHTLK KGLHEKGLAT AVGDEGGFAP NLSSTRAALD FIMASIDKAG FKAGEDVVLA
     LDCAATEFFK VGKYEISGEG LSLDPHTMAQ YLADLCADYP IKSIEDGMAE DDFEGWKAVT
     DLIGNKVQLV GDDLFVTNPK RLAMGIEMGL ANSLLVKVNQ IGTLSETMAA VSMAHRSSYT
     AVMSHRSGET EDTTIADLAV ATNCGQIKTG SLARSDRLAK YNQLIRIEEE LGVSAIYAGR
     SIFR
//
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