ID A0A367KXS7_RHIST Unreviewed; 437 AA.
AC A0A367KXS7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
GN ORFNames=CU098_012259 {ECO:0000313|EMBL:RCI07018.1};
OS Rhizopus stolonifer (Rhizopus nigricans).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=4846 {ECO:0000313|EMBL:RCI07018.1, ECO:0000313|Proteomes:UP000253551};
RN [1] {ECO:0000313|EMBL:RCI07018.1, ECO:0000313|Proteomes:UP000253551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSU 92-RS-03 {ECO:0000313|EMBL:RCI07018.1,
RC ECO:0000313|Proteomes:UP000253551};
RX PubMed=29674435; DOI=10.1534/g3.118.200235;
RA Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA Heitman J., Vilgalys R., Stajich J.E.;
RT "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL G3 (Bethesda) 8:2007-2018(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000767};
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}.
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:RCI07018.1}.
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DR EMBL; PJQM01000046; RCI07018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367KXS7; -.
DR STRING; 4846.A0A367KXS7; -.
DR EnsemblFungi; RCI07018; RCI07018; CU098_012259.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000253551; 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; 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:SF1; ENOLASE; 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; 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 Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000253551}.
FT DOMAIN 4..135
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 144..434
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT ACT_SITE 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 373..376
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
SQ SEQUENCE 437 AA; 47015 MW; 40EE70C7A1854A1C CRC64;
MSTVTKVHAR QIFDSRGNPT VEVEVTTAKG VFRAAVPSGA STGIHEAIEL RDGDKSAYMG
KGVLKAVANV IDVIQPALIE AKIPVTEQKA IDEFLIKLDG TANKGKLGAN AILGVSLAVA
KAAAADKGVP LYVHFADLAG SKKPFVLPVP AFNVINGGSH AGNKLAMQEF MILPTGAKSF
KEAMKIGGEV YHNLQSVIKA KYGLDATNVG DEGGFAPNIQ KNEEGLDLLV QAIEKAGYTG
KVKIGMDVAA SEFYKDGKYD LDFKNPESDK SEWIDGKELT ALYNSFASKY PIVSIEDAFD
QDDWENWSHL NDVSDFQLVG DDLLVTNPKR IVTAIEKKAC NALLLKVNQI GTVTESIQAA
KDSQAAGWGV MVSHRSGETE DTTIADLVVG LRTGQIKTGA PCRSERLAKY NQLLRIEEEL
GENCIYAGEN FRTAHDL
//
