SIAS_DROME
ID SIAS_DROME Reviewed; 372 AA.
AC Q9VG74; B3DMY1; Q95VY1;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Sialic acid synthase {ECO:0000303|PubMed:11886840};
DE AltName: Full=N-acetylneuraminate synthase {ECO:0000303|PubMed:11886840};
DE EC=2.5.1.56 {ECO:0000269|PubMed:11886840, ECO:0000269|PubMed:21919466};
DE AltName: Full=N-acetylneuraminate-9-phosphate synthase {ECO:0000303|PubMed:11886840};
DE EC=2.5.1.57 {ECO:0000269|PubMed:11886840};
GN Name=NANS {ECO:0000312|FlyBase:FBgn0038045};
GN Synonyms=Sas {ECO:0000303|PubMed:11886840};
GN ORFNames=CG5232 {ECO:0000312|FlyBase:FBgn0038045};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAK92125.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Oregon-R {ECO:0000312|EMBL:AAK92125.1};
RX PubMed=11886840; DOI=10.1093/glycob/12.2.73;
RA Kim K., Lawrence S.M., Park J., Pitts L., Vann W.F., Betenbaugh M.J.,
RA Palter K.B.;
RT "Expression of a functional Drosophila melanogaster N-acetylneuraminic acid
RT (Neu5Ac) phosphate synthase gene: evidence for endogenous sialic acid
RT biosynthetic ability in insects.";
RL Glycobiology 12:73-83(2002).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:ACD81783.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21919466; DOI=10.1021/cb200238k;
RA Granell A.E., Palter K.B., Akan I., Aich U., Yarema K.J., Betenbaugh M.J.,
RA Thornhill W.B., Recio-Pinto E.;
RT "DmSAS is required for sialic acid biosynthesis in cultured Drosophila
RT third instar larvae CNS neurons.";
RL ACS Chem. Biol. 6:1287-1295(2011).
CC -!- FUNCTION: Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-
CC D-glycero-D-galacto-nononic acid (KDN) (PubMed:11886840,
CC PubMed:21919466). Can also use N-acetylmannosamine 6-phosphate and
CC mannose 6-phosphate as substrates to generate phosphorylated forms of
CC Neu5Ac and KDN, respectively (PubMed:11886840). Essential for
CC biosynthesis of sialic acids in neurons of the central nervous system
CC (PubMed:21919466). {ECO:0000269|PubMed:11886840,
CC ECO:0000269|PubMed:21919466}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-mannosamine + phosphoenolpyruvate = N-
CC acetylneuraminate + phosphate; Xref=Rhea:RHEA:19273,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17122, ChEBI:CHEBI:35418,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=2.5.1.56;
CC Evidence={ECO:0000269|PubMed:11886840, ECO:0000269|PubMed:21919466};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-D-mannosamine 6-phosphate + H2O +
CC phosphoenolpyruvate = an N-acylneuraminate 9-phosphate + phosphate;
CC Xref=Rhea:RHEA:13421, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57537, ChEBI:CHEBI:57666, ChEBI:CHEBI:58702; EC=2.5.1.57;
CC Evidence={ECO:0000269|PubMed:11886840};
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of development.
CC {ECO:0000269|PubMed:11886840}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACD81783.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF397531; AAK92125.1; -; mRNA.
DR EMBL; AE014297; AAF54811.2; -; Genomic_DNA.
DR EMBL; BT032769; ACD81783.1; ALT_INIT; mRNA.
DR RefSeq; NP_650195.1; NM_141938.1.
DR AlphaFoldDB; Q9VG74; -.
DR SMR; Q9VG74; -.
DR IntAct; Q9VG74; 1.
DR STRING; 7227.FBpp0082060; -.
DR PaxDb; Q9VG74; -.
DR EnsemblMetazoa; FBtr0082588; FBpp0082060; FBgn0038045.
DR GeneID; 41528; -.
DR KEGG; dme:Dmel_CG5232; -.
DR UCSC; CG5232-RA; d. melanogaster.
DR CTD; 54187; -.
DR FlyBase; FBgn0038045; NANS.
DR VEuPathDB; VectorBase:FBgn0038045; -.
DR eggNOG; ENOG502QR5J; Eukaryota.
DR GeneTree; ENSGT00390000011081; -.
DR HOGENOM; CLU_040465_1_0_1; -.
DR InParanoid; Q9VG74; -.
DR OMA; YRHRVEF; -.
DR OrthoDB; 1117607at2759; -.
DR PhylomeDB; Q9VG74; -.
DR BRENDA; 2.5.1.57; 1994.
DR Reactome; R-DME-4085001; Sialic acid metabolism.
DR BioGRID-ORCS; 41528; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41528; -.
DR PRO; PR:Q9VG74; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038045; Expressed in central nervous system and 6 other tissues.
DR GO; GO:0050462; F:N-acetylneuraminate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0047444; F:N-acylneuraminate-9-phosphate synthase activity; IDA:FlyBase.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR GO; GO:0070085; P:glycosylation; IMP:FlyBase.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR006190; AFP_Neu5c_C.
DR InterPro; IPR036732; AFP_Neu5c_C_sf.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013132; Neu5Ac_N.
DR InterPro; IPR013974; SAF.
DR Pfam; PF03102; NeuB; 1.
DR Pfam; PF08666; SAF; 1.
DR SMART; SM00858; SAF; 1.
DR SUPFAM; SSF51269; SSF51269; 1.
DR PROSITE; PS50844; AFP_LIKE; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..372
FT /note="Sialic acid synthase"
FT /id="PRO_0000438525"
FT DOMAIN 314..372
FT /note="AFP-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00021"
SQ SEQUENCE 372 AA; 41218 MW; 9C7ADB0567422F3E CRC64;
MLLNDIISGK LVDSVYIIAE IGQNHQGCVE TAKKMIWEAK KAGCHCVKFQ KSDLPAKFTR
SALDREYISD HAWGKTYGEH KEYLEFSKDQ YLQLQAHCKE LNVDFTASAM DERSLEFLSA
LNVPFIKIGS GDANNFPLLK KAANLNLPLV ISTGMQTMQT VERIVQTMRE SGKEDYALMH
CVSSYPTDPK DCSLQLISVL RTRFPNVAIG YSGHELGVII SQAAVLLGAR IVERHFTLDK
SQKGSDHRCS LEPQELKALT TAITNFKLSS VPMPPQEIVK KLNGDEELEA ALQHVESKTI
LPCELPCRNK LGKSIVAARN LNKGYRLQLA DMAIKVSEPS GLTAEDFLDL VGKELADNIG
EDEPILGNSI IN
