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Database: UniProt
Entry: A0A3M0K532_HIRRU
LinkDB: A0A3M0K532_HIRRU
Original site: A0A3M0K532_HIRRU 
ID   A0A3M0K532_HIRRU        Unreviewed;       763 AA.
AC   A0A3M0K532;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE            EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000256|ARBA:ARBA00031125};
GN   ORFNames=DUI87_17067 {ECO:0000313|EMBL:RMC07591.1};
OS   Hirundo rustica rustica.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC   Hirundo.
OX   NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC07591.1, ECO:0000313|Proteomes:UP000269221};
RN   [1] {ECO:0000313|EMBL:RMC07591.1, ECO:0000313|Proteomes:UP000269221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chelidonia {ECO:0000313|EMBL:RMC07591.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:RMC07591.1};
RA   Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA   Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT   "A high quality draft genome assembly of the barn swallow (H. rustica
RT   rustica).";
RL   Submitted (JUL-2018) 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   -!- 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:RMC07591.1}.
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DR   EMBL; QRBI01000120; RMC07591.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0K532; -.
DR   STRING; 333673.A0A3M0K532; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000269221; 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   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   NCBIfam; TIGR01060; eno; 1.
DR   PANTHER; PTHR11902; ENOLASE; 1.
DR   PANTHER; PTHR11902:SF10; GAMMA-ENOLASE; 1.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   Pfam; PF14580; LRR_9; 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   SMART; SM00365; LRR_SD22; 5.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
DR   PROSITE; PS51450; LRR; 3.
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:UP000269221}.
FT   DOMAIN          332..463
FT                   /note="Enolase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01193"
FT   DOMAIN          471..760
FT                   /note="Enolase C-terminal TIM barrel"
FT                   /evidence="ECO:0000259|SMART:SM01192"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   763 AA;  84945 MW;  EAB3F410EC87401C CRC64;
     MQDEEPEEEK EEREEDEEKE EGDDEEKEGK EPAPCPLTEE ILKEGLSLLS KTGNGLAHAY
     VKFEAKDKGL TDISLLERFI HLRYVDLSKN KLKDLAPLSS LTQLLWLKVD GNLLTSASMQ
     EMPYLQVISF DRNQIVDLEG ITHPLLANLS LKENKIQTVL GLSQDQLFSL QVLELRGNQI
     KTTAGLGVPK LKQLYLAKNT ICSLEGLEEF EQLETLHLRD NKLEALDGFC DSMKCLQYLN
     LRNNGIKSFQ EVEKLQVLPM LQALVLMDNP CAEEPNYRLE VLSRLSQLQR LDKESVEEEE
     REEAEKMRQT RKEKHFLNLS STPALGRLTM AVERIHAREI LDSRGNPTVE VDLYTHKGMF
     RAAVPSGAST GIYEALELRD NDKSRFLGKG VLQAVDHINS TVAPALVGSG LSVVDQEKID
     NLMLEMDGTE NKSKFGANAI LGVSLAVCKA GAAEKDVPLY RHIADLAGNS DLILPVPAFN
     VINGGSHAGN KLAMQEFMIL PVGAESFRDA MRIGAEVYHN LKSVIKEKYG KDATNVGDEG
     GFAPNILENS EALELLKEAI DKAGYTDKIV IGMDVAASEF YRDGKYDLDF KSPDDPSRYI
     SGDELGDLYQ SFVRDYPVVS IEDPFDQDDW ENWSKFTANV GIQIVGDDLT VTNPKRIERA
     VEEKACNCLL LKVNQIGSVT EAIQACKLAQ ENGWGVMVSH RSGETEDTFI ADLVVGLCTG
     QIKTGAPCRS ERLAKYNQLM RIEEELGDEA RFAGHNFRNP SVL
//
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