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Database: UniProt
Entry: A0A0E9NBA2_SAICN
LinkDB: A0A0E9NBA2_SAICN
Original site: A0A0E9NBA2_SAICN 
ID   A0A0E9NBA2_SAICN        Unreviewed;       485 AA.
AC   A0A0E9NBA2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-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=G7K_1295-t1 {ECO:0000313|EMBL:GAO47083.1};
OS   Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS   / NRRL Y-17804).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Taphrinomycotina incertae sedis; Saitoella.
OX   NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO47083.1, ECO:0000313|Proteomes:UP000033140};
RN   [1] {ECO:0000313|EMBL:GAO47083.1, ECO:0000313|Proteomes:UP000033140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO47083.1,
RC   ECO:0000313|Proteomes:UP000033140};
RX   PubMed=21914972; DOI=10.2323/jgam.57.243;
RA   Nishida H., Hamamoto M., Sugiyama J.;
RT   "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL   J. Gen. Appl. Microbiol. 57:243-246(2011).
RN   [2] {ECO:0000313|EMBL:GAO47083.1, ECO:0000313|Proteomes:UP000033140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO47083.1,
RC   ECO:0000313|Proteomes:UP000033140};
RX   PubMed=24646756; DOI=10.2323/jgam.60.7;
RA   Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT   "The early diverging ascomycetous budding yeast Saitoella complicata has
RT   three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT   lineages.";
RL   J. Gen. Appl. Microbiol. 60:7-12(2014).
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:GAO47083.1}.
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DR   EMBL; BACD03000007; GAO47083.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E9NBA2; -.
DR   STRING; 698492.A0A0E9NBA2; -.
DR   OMA; RCMMSHR; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000033140; 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   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:UP000033140}.
FT   DOMAIN          50..181
FT                   /note="Enolase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01193"
FT   DOMAIN          190..480
FT                   /note="Enolase C-terminal TIM barrel"
FT                   /evidence="ECO:0000259|SMART:SM01192"
SQ   SEQUENCE   485 AA;  52497 MW;  A8A591E5D037DD21 CRC64;
     MEPVLFVIVN RRQQTVNRIT IIRSICYLII IAARRNNLNN PHTITEAMAI SKIHARTIYD
     SRGNPTVEVD LYTADGALHR CAVPSGASTG IHEALELRDK ESQWGGKGVL KAVSNVNDVI
     APALIKADLD LKDQAAVDKF LIELDGTKNK AKLGANAILG VSMAVAKAAA AEKGVPLYRH
     LADVSGAKKP FVLPVPAFNV INGGSHAGGR LAFQEFMIMP TGVASFSEAM RAGAEIYAVL
     KSLTKKKYGM SAGNVGDEGG VAPDIQTPEE ALDLIMDAIS KAGYEGKIKI AMDVASSEFY
     KDNKYDLDFK NPESDPSKFV SGEDLGKQYA ALAEKYPIVS IEDAFEQDDW EAWVNLCANS
     EFQLVGDDLT VTNVERIQTA IEKKACNALL LKINQIGTIT ESINAANDSF NAGWGVMVSH
     RSGETEDTFI ADLVVGLRAG QIKTGAPCRS ERLAKYNQLL RIEEELGSEA VYAGENFRNA
     SQHNF
//
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