ID A0A2U9AXN7_SCOMX Unreviewed; 650 AA.
AC A0A2U9AXN7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 13-SEP-2023, entry version 18.
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 ORFNames=SMAX5B_011739 {ECO:0000313|EMBL:AWO96388.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWO96388.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWO96388.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the MLF family. {ECO:0000256|ARBA:ARBA00008332}.
CC -!- SIMILARITY: Belongs to the enolase family.
CC {ECO:0000256|ARBA:ARBA00009604}.
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DR EMBL; CP026243; AWO96388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9AXN7; -.
DR STRING; 52904.ENSSMAP00000017717; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000246464; Chromosome 1.
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 InterPro; IPR019376; Myeloid_leukemia_factor.
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 Pfam; PF10248; Mlf1IP; 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|ARBA:ARBA00022490};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 245..350
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 358..647
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT REGION 115..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 70936 MW; 805A0212E246C9D4 CRC64;
MFRYLNDVDD DPYMMDPFAA HRQQMSLFTP FAMDPFALAP QMQPHRAAPR RQAGPLTPFG
MMGMGGGFMD MFGMMGEMMG NMERMTGSPN CQTFSSSTVI SYSSSDIGAP KVYQQTSATR
TGPGGIRETH QSVRDSESGL ERLAIGHHIG ARAHIMERSR NRRTGDREER QDYINLDETE
AAAFDEEWRR GAGRYVPPGA RALDYGRDRR AGGQQLALTA PPSSTTPPGH GHESPRHRQP
QTRPRYDWAA VPSGASTGIY EALELRDGDK TRYKGKGVTK AVGHINDTLG PALVEAGVNV
LEQEKLDNMM IEMDGTDNKS KFGANAILGV SLAICKAGAA EKGVPLYRHI ADLAGNGELV
LPVPAFNVIN GGSHAGNRLA MQEFMVLPVG AESFRDALRV GAELYQTLRG VIKEKYGQDA
TNVGDEGGFA PNIQENSEAL ELIKTAIEKA GFTDKVVIGM DVAASEFFIE GKYDLDFKSP
PNAARNISGE ELASIYQGFI NNYPVVSIED PFDQDDWPAW SQFTASVGIQ VVGDDLTVTN
PRRIQRAVED KACNCLLLKV NQIGSVTEAI KACKLAQENG WGVMVSHRSG ETEDTFIADL
VVGLCTGQIK TGAPCRSERL AKYNQLMRIE EELGDQARFA GHNFRNPSAL
//
