ID A0A1S3YTS3_TOBAC Unreviewed; 396 AA.
AC A0A1S3YTS3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
GN Name=LOC107779604 {ECO:0000313|RefSeq:XP_016455543.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016455543.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016455543.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_016455543.1; XM_016600057.1.
DR STRING; 4097.A0A1S3YTS3; -.
DR PaxDb; 4097-A0A1S3YTS3; -.
DR GeneID; 107779604; -.
DR KEGG; nta:107779604; -.
DR OMA; LETWKTM; -.
DR OrthoDB; 1093250at2759; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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; IPR020811; Enolase_N.
DR PANTHER; PTHR11902:SF55; CYTOSOLIC ENOLASE 3; 1.
DR PANTHER; PTHR11902; ENOLASE; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000084051}.
FT DOMAIN 1..104
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 112..396
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 336..339
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT NON_TER 1
FT /evidence="ECO:0000313|RefSeq:XP_016455543.1"
SQ SEQUENCE 396 AA; 42755 MW; 4E06255D58040925 CRC64;
GVFRASVPSG ASSGMYEAIE LRDGEKGTYL GNGVNRAVKN INEKISVALV GMDPTLQSQI
DQVMIDLDKT ENKSELGANA ILAVSIAACK AGAAEKEVPL YKHIADLSGQ TSVLLPIPVF
TLVTGGKHAG NNLAIQEIMI LPVGSKTFEE ALQIGSETYH HLKVVITEKY GAHGCNVGED
GGFAPDISSL RDGLDLVQEA IGRTGYKEKI KIAIGVAATE FCIGTKYDLD FMTPNKSGQN
FKSGQDMIDI YKELCADYPV VSIEDPFDKE DWEHVKYFSS LGVCQVVGDH LLMSNPKRXS
GWHGLAGIQV NQIGTVTEAI EVVKMAKDAQ WGVVISQRSG ETEDSFIADL SVGLATGQIK
AGAPCRGERL AKYNQLLRIE QELGDQAFYI GEKWRT
//