ID A0A1Q9F503_SYMMI Unreviewed; 762 AA.
AC A0A1Q9F503;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
GN Name=ENO2 {ECO:0000313|EMBL:OLQ14727.1};
GN ORFNames=AK812_SmicGene1049 {ECO:0000313|EMBL:OLQ14727.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ14727.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ14727.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ14727.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OLQ14727.1}.
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DR EMBL; LSRX01000011; OLQ14727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9F503; -.
DR OrthoDB; 2563030at2759; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
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 InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; PTHR24198; ANKYRIN REPEAT AND PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24198:SF165; IPT_TIG DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 2.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 8.
DR PROSITE; PS50088; ANK_REPEAT; 8.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 5..563
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT REPEAT 266..298
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 299..331
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 332..364
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 365..397
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 398..430
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 431..463
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 464..496
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 498..530
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 581..749
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
SQ SEQUENCE 762 AA; 82565 MW; 735330CDB198091E CRC64;
MAAKIKQIRA REIFDSRGFG CSIYEALELR DGVKERLLGK GVQKAALLLF KAVANVNDII
APKLIGMEVT KQTEIDKLMV ESLASRVAAH NRHPPLQTFS PERDSVVKLQ LLRCTVLDML
QVRAVSGEGL IEINLVSFLE TLPAEMSPVR ALKQHLHSIF GLSRFRQRLV FPNDDDVVPD
DECALRPGEV QVVILSFCPA SEAQVKALRD AARRGLTSKV ETILHRPQDP DLGDPAPLFE
ASEHGQSEVA RLLLEAKADK DKAIENGATP LYTAAARGHL KVARLLLEAN ADKDKATHEG
TTPLFIAAQN GELAVARFLL EAKADKDKAI DGGATPLHIA AASGHFKVTR LLLEASADKD
KADENGATPL FIAAAHGELA VARFLLAASA DKEKAEQNGA TPVHIAAQEG QLEVVRLLLE
ASADKDKAKA NKATPLYVAA GLGELEVARF LLVASADKEK ADQNGATPLH IAAQEGQLEV
VRLLLEAKAD KDKAMENGGA TPLFVAAQTG QSEVVRLLLE ANADKNKSVH DGTTPLFVAT
QAVSMAVCRA GAAASRMPLY KYIARSSTAA ATLATDWLAR PAPFCIIVNL MLIIYSGSQV
YHNLKSVIKK KYGQDACNVG DEGGFAPSVQ DNNEALDVLM EAIEKSGHAG KVKIGTDVAA
SEFYGAETKK YDLDFKNPES PDSMKKTAEE MIAYYKDWIG KYPFVSIEDP FDQDDWEAYS
KFQAEVGETI QRLFGDSNIE NCRISLLPLL LMRLLATRAM KP
//
