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Database: UniProt
Entry: A0A3B5ADH2_9TELE
LinkDB: A0A3B5ADH2_9TELE
Original site: A0A3B5ADH2_9TELE 
ID   A0A3B5ADH2_9TELE        Unreviewed;       434 AA.
AC   A0A3B5ADH2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE            EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000256|ARBA:ARBA00031125};
GN   Name=LOC103356836 {ECO:0000313|RefSeq:XP_008279358.1};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000018431.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000018431.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_008279358.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|ARBA:ARBA00005031}.
CC   -!- SIMILARITY: Belongs to the enolase family.
CC       {ECO:0000256|ARBA:ARBA00009604}.
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DR   RefSeq; XP_008279358.1; XM_008281136.1.
DR   AlphaFoldDB; A0A3B5ADH2; -.
DR   STRING; 144197.ENSSPAP00000018431; -.
DR   Ensembl; ENSSPAT00000018709.1; ENSSPAP00000018431.1; ENSSPAG00000013903.1.
DR   GeneID; 103356836; -.
DR   CTD; 2026; -.
DR   GeneTree; ENSGT00950000182805; -.
DR   OrthoDB; 1093250at2759; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000261400; Unplaced.
DR   Proteomes; UP000694891; Unplaced.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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:SF10; GAMMA-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   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694891}.
FT   DOMAIN          3..134
FT                   /note="Enolase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01193"
FT   DOMAIN          142..431
FT                   /note="Enolase C-terminal TIM barrel"
FT                   /evidence="ECO:0000259|SMART:SM01192"
FT   ACT_SITE        210
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT   ACT_SITE        343
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         370..373
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         394
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
SQ   SEQUENCE   434 AA;  46917 MW;  06C4F6A01D340B7E CRC64;
     MSIVSIIARE ILDSRGNPTV EVDLRTEKGL FRAAVPSGAS TGIYEALELR DGDKSRYKGK
     GVLKAVGHIN DTLGPALIAS GISVVEQEQL DNMMIEMDGT ENKSQFGANA ILGVSLAICK
     AGAAEKDTPL YRHIADLAGN TELVLPVPAF NVINGGSHAG NKLAMQEFMV LPVGAESFKE
     ALRIGAELYH TLKGVIQEKY GQDATNVGDE GGFAPNILEN SEALDLLQTA IEKAGFTEKV
     VVGMDVAASE FYRDGKYDLD FKSPPDPERH ISGEELADIY QGFVNNYPVV SIEDPFDQDD
     WEAWSRLTAQ VGIQVVGDDL TVTNPKRIEK AAEERACNCL LLKVNQIGSV TEAIQACKLA
     QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGDQ
     ARFAGHNFRN PSAL
//
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