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Database: UniProt
Entry: A0A1R3IHJ7_COCAP
LinkDB: A0A1R3IHJ7_COCAP
Original site: A0A1R3IHJ7_COCAP 
ID   A0A1R3IHJ7_COCAP        Unreviewed;       402 AA.
AC   A0A1R3IHJ7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE            EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
GN   ORFNames=CCACVL1_12096 {ECO:0000313|EMBL:OMO82054.1};
OS   Corchorus capsularis (Jute).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX   NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO82054.1, ECO:0000313|Proteomes:UP000188268};
RN   [1] {ECO:0000313|EMBL:OMO82054.1, ECO:0000313|Proteomes:UP000188268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC   TISSUE=Whole seedling {ECO:0000313|EMBL:OMO82054.1};
RA   Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA   Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA   Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT   "Corchorus capsularis genome sequencing.";
RL   Submitted (SEP-2013) 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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the enolase family.
CC       {ECO:0000256|ARBA:ARBA00009604}.
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:OMO82054.1}.
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DR   EMBL; AWWV01010055; OMO82054.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3IHJ7; -.
DR   STRING; 210143.A0A1R3IHJ7; -.
DR   EnsemblPlants; OMO82054; OMO82054; CCACVL1_12096.
DR   Gramene; OMO82054; OMO82054; CCACVL1_12096.
DR   OMA; KHADNGI; -.
DR   OrthoDB; 1093250at2759; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000188268; Unassembled WGS sequence.
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; 2.
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:SF47; BIFUNCTIONAL ENOLASE 2/TRANSCRIPTIONAL ACTIVATOR; 1.
DR   PANTHER; PTHR11902; ENOLASE; 1.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PIRSF; PIRSF001400; Enolase; 2.
DR   PRINTS; PR00148; ENOLASE.
DR   SFLD; SFLDG00178; 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   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188268}.
FT   DOMAIN          5..97
FT                   /note="Enolase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01193"
FT   DOMAIN          105..398
FT                   /note="Enolase C-terminal TIM barrel"
FT                   /evidence="ECO:0000259|SMART:SM01192"
FT   ACT_SITE        173
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT   ACT_SITE        310
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         337..340
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
SQ   SEQUENCE   402 AA;  43551 MW;  5987B4505F6B6D14 CRC64;
     MAVTITAVKA RQIFDSRGNP TVEAVSNVNA IIGPALIGKD PTEQTAIDNF MVQQLDGTQN
     EWGWCKQKLG ANAILAVSLA VCKAGAEVKN IPLYKHIANL AGNKKLVLPV PAFNVINGGS
     HAGNKLAMQE FMILPVGASS FKEAMKMGVE VYHHLKSVIK KKYGQDATNV GDEGGFAPNI
     QENKEGLELL KTAIEKAGYT GKVVIGMDVA ASEFYGTDKT YDLNFKAENN DGSQKISGDA
     LKDLYKSFAC EYPIVSIEDP FDQDDWEHYA KMTKEIGEKV QIVGDDLLVT NPKRVEKAIK
     EKTCNALLLK VNQIGSVTES IEAVRMSKKA GWGVMASHRS GETEDTFIAD LSVGLATGQI
     KTGAPCRSER LAKYNQLLRI EEELGADAVY AGASFRAPVE PY
//
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