ID A0A0S3RZ19_PHAAN Unreviewed; 444 AA.
AC A0A0S3RZ19;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
GN Name=Vigan.04G340000 {ECO:0000313|EMBL:BAT85810.1};
GN ORFNames=VIGAN_04340000 {ECO:0000313|EMBL:BAT85810.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT85810.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT85810.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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 EMBL; AP015037; BAT85810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3RZ19; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000291084; Chromosome 4.
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:SF56; PHOSPHOPYRUVATE HYDRATASE; 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; 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:UP000291084}.
FT DOMAIN 4..139
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 147..440
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT ACT_SITE 352
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 379..382
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
SQ SEQUENCE 444 AA; 47769 MW; 2DECC00A2D1BB643 CRC64;
MATILSIKAR EIFDSRGNPT VEVDLLCSDG TFARAAVPSG ASTGIYEALE LRDGGSDYLG
KGVSKAVDNV NSIIAPALIG KDPTQQTAID NLMVQQLDGT VNEWGWCKQK LGANAILAVS
LAVCKAGASV LKIPLYKHIA NLAGNKNLVL PVPAFNVING GSHAGNKLAM QEFMVLPVGA
SSFKEAMKMG VEVYHHLKSV IKKKYGQDAI NVGDEGGFAP NIQENKEGLE LLNSAIAKAG
YTGKVVIGMD VAASEFYKED KTYDLNFKED DNDGSQRISG DALKELYKSF VSEYPIVSIE
DPFDQDDWEH YAKLTAEVGT NVQIVGDDLL VTNPKRVQKA IDTKACNALL LKVNQIGSVT
ESIEAVRMSK KAGWGVMTSH RSGETEDTFI ADLAVGLSTG QIKTGAPCRS ERLAKYNQLL
RIEEELGAEA VYAGANFRTP VEPY
//
