ID A0A3B4VH36_SERDU Unreviewed; 542 AA.
AC A0A3B4VH36;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
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};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000030253.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000030253.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3B4VH36; -.
DR Ensembl; ENSSDUT00000030777.1; ENSSDUP00000030253.1; ENSSDUG00000021802.1.
DR GeneTree; ENSGT00950000182805; -.
DR OMA; MKELICI; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000261420; 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 Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 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:SF30; ENOLASE 4; 1.
DR Pfam; PF00113; Enolase_C; 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.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT DOMAIN 35..224
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 235..520
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT REGION 142..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 60025 MW; E357C764D7C5A9FB CRC64;
MEYWIDQMWQ KRRKLFLKRC REANYFANLA APPRINRLRG REVYDTRGQL SIEVEVFCIV
SNKEKSISSA AVSSLFGSKE SSLDWRAQSQ ERADHVMTAV QWINEPLNNM LKDQNPCDQS
EVDHALSNFF MARYLEEKDI RNREEEESHS PNESEAVLPS APSAQAKDKR TVDKGKKSNT
SEKPFPPAEP PEPVLPGSLA IGSVSVAVAR TGAQLQGLPL YGYIAALKNG ETPTQFYIPV
SLVTLLSCGK TSAGKLSLLE EIILIPKAGQ RVKQIITMTL ELQKEMMRIM NTSTKAGATQ
ATLHDSGAPA VSYERPEQPL DLIAEACINL GLALGTEIHL ALNCDAHELM DFSKGKYEVA
TGVLKSPDEL VDMYQTLVSK YPAVVALINP LRREDIVQWE KLSNVIGDSC SLLFDVTYKA
KALPHLGVRG HILKHTDEMT VSDLVRITSE HQGSVLLGTT YSEPCSSDSF SDIAVGLGLD
YVKLGGLSGA ERMTKYNRLI SIEEELAQQG ILVSKEKHPP PLFNENLQKQ STTAERHLSD
KA
//
