ID A0A182EHI4_ONCOC Unreviewed; 436 AA.
AC A0A182EHI4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Enolase {ECO:0000256|ARBA:ARBA00017068};
DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000256|ARBA:ARBA00031125};
DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000256|ARBA:ARBA00032132};
GN ORFNames=NOO_LOCUS7559 {ECO:0000313|EMBL:VDK86574.1};
OS Onchocerca ochengi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t07559-RA};
RN [1] {ECO:0000313|Proteomes:UP000077448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
RN [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t07559-RA}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [3] {ECO:0000313|EMBL:VDK86574.1, ECO:0000313|Proteomes:UP000271087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-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}.
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DR EMBL; UYRW01002747; VDK86574.1; -; Genomic_DNA.
DR STRING; 42157.A0A182EHI4; -.
DR WBParaSite; nOo.2.0.1.t07559-RA; nOo.2.0.1.t07559-RA; nOo.2.0.1.g07559.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000077448; Unassembled WGS sequence.
DR Proteomes; UP000271087; 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; 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:UP000271087}.
FT DOMAIN 3..134
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 142..434
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT ACT_SITE 210
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 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 167
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 436 AA; 47508 MW; 1FA4770B38BEE196 CRC64;
MPITRVHARP IYDSRGNPTV EVDLTTEKGI FRAAVPSGAS TGIHEALELR DNDKAVNHGK
GVLQAVRNVN EQIGPALVAK NFCPTQQREI DLFMLQLDGT ENKAKLGANA ILGVSLAVCK
AGAVHKGMPL YKYIAELAGT RQIVLPVPAM NVINGGSHAG NKLAMQEFMI MPVGASSFSE
AMRMGSEIYH YLKAEIKKRY GLDATAVGDE GGFAPNIQDN KEGLDLLNTA IATAGYTGKV
SIAMDCAASE YYKEADKLYD LDFKNPNSDK TQWKTGDQMM EIYQSFIKEY PVVSIEDWFD
QDDWDNWTKG LAKTNIQIVG DDLTVTNPKR IALAAEKKAC NCLLLKVNQI GSVTESIDAA
NLARKNGWGV MVSHRSGETE DTFIADLVVG LATGQIKTGA PCRSERLAKY NQILRIEEEL
GSAAVYAGQK FRNPQA
//
