ENOPH_CULQU
ID ENOPH_CULQU Reviewed; 723 AA.
AC B0WQG0;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Enolase-phosphatase E1;
DE EC=3.1.3.77;
DE AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase;
GN ORFNames=CPIJ009638;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB;
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the enolization of 2,3-
CC diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the
CC intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-
CC MTPenyl-1-P), which is then dephosphorylated to form the acireductone
CC 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-
CC dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate;
CC Xref=Rhea:RHEA:21700, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:49252, ChEBI:CHEBI:58828; EC=3.1.3.77;
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 3/6.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 4/6.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MasA/MtnC
CC family. {ECO:0000305}.
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DR EMBL; DS232039; EDS32831.1; -; Genomic_DNA.
DR RefSeq; XP_001850944.1; XM_001850892.1.
DR AlphaFoldDB; B0WQG0; -.
DR SMR; B0WQG0; -.
DR STRING; 7176.CPIJ009638-PA; -.
DR GeneID; 6041722; -.
DR KEGG; cqu:CpipJ_CPIJ009638; -.
DR VEuPathDB; VectorBase:CPIJ009638; -.
DR VEuPathDB; VectorBase:CQUJHB012676; -.
DR eggNOG; KOG2630; Eukaryota.
DR HOGENOM; CLU_382743_0_0_1; -.
DR InParanoid; B0WQG0; -.
DR OMA; IKAHVYE; -.
DR OrthoDB; 1475361at2759; -.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000002320; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043874; F:acireductone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023943; Enolase-ppase_E1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01691; enolase-ppase; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Hydrolase; Methionine biosynthesis;
KW Nucleus; Reference proteome.
FT CHAIN 1..723
FT /note="Enolase-phosphatase E1"
FT /id="PRO_0000393975"
FT REGION 239..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 126..127
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 723 AA; 77070 MW; 19C8F7670931B5B2 CRC64;
MRYQQDTLFP YALKNVEEYL KANWNEDATK TVVAALREQA DEDKKAEVEG ALTIPAGDSE
DIIPDIVKYV EWQTSRDAKT GSLKTLQGLV WAKGYKDGSI KGHVYDDVSK ALEQWTEGGR
KIYVYSSGSV DAQKMLFEHS EQGDLVKYLA GHYDTKIGAK TEKDSYEAIL KNIEATAEEA
LFLTDVVAEA KAAKEAGLNV VVLERPGNAE LSEDDRKEFT VVKSFADIPL ESIVESANGA
GAKRKIDEAQ EEDEAQPPTK VVKKDENGDA AAKKDETAKV DEPAAKATNG DAAAKEEAAA
PAEGKMEVDE AAAAAAPPAD AAEEKKETEE AKPETEKVTE KTESTAAEKK EEDKKEEVAE
SKEAAPKEVV AEEAKKEEEV KAAAPAEEVK KVEEPVPAEA KKVVEEEKME VDGGAEAVAE
EKEAEKKEED KAAEPAAEKK PAEEAVVTST EEPAKEEPKV ESSTAEAEPA KEKPAEAEAK
AAPAETTKAE VVEKPAETPA AESMETDSEP SADKEAEAKP EAKPVEEVKK AEAEKKVEAE
KKPAESEAEA KEVATKPVEE TKGEETTTAG PVEEIAVEAK EDAAKPEEKK SDADEVSTTT
TTTSTESKTE NGTHENGVSK EATPVNGKEE SRVPENGEAE PAAEAVVTSN GNGKHEEKGD
SDKENDTATS NTTEEPAANG NGVENGSTTS STTTPAPDAA AEIKSKKVID SSTTPTPPIE
AES
