ID   NEUA_ONCMY              Reviewed;         432 AA.
AC   Q90WG6;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=N-acylneuraminate cytidylyltransferase;
DE            EC=2.7.7.43;
DE   AltName: Full=CMP-N-acetylneuraminic acid synthase;
DE            Short=CMP-NeuNAc synthase;
GN   Name=cmas;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=11479279; DOI=10.1093/glycob/11.8.685;
RA   Nakata D., Muenster A.-K., Gerardy-Schahn R., Aoki N., Matsuda T.,
RA   Kitajima K.;
RT   "Molecular cloning of a unique CMP-sialic acid synthetase that effectively
RT   utilizes both deaminoneuraminic acid (KDN) and N-acetylneuraminic acid
RT   (Neu5Ac) as substrates.";
RL   Glycobiology 11:685-692(2001).
CC   -!- FUNCTION: Catalyzes the activation of N-acetylneuraminic acid (NeuNAc)
CC       to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a
CC       substrate required for the addition of sialic acid.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylneuraminate + CTP = a CMP-N-acyl-beta-neuraminate +
CC         diphosphate; Xref=Rhea:RHEA:11344, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:60073, ChEBI:CHEBI:68671; EC=2.7.7.43;
CC         Evidence={ECO:0000269|PubMed:11479279};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate metabolism.
CC   -!- SUBUNIT: Homotetramer; the active enzyme is formed by a dimer of
CC       dimers. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:11479279}.
CC   -!- TISSUE SPECIFICITY: Expressed in testis, ovary and liver.
CC       {ECO:0000269|PubMed:11479279}.
CC   -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. {ECO:0000305}.
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DR   EMBL; AB027414; BAB47150.1; -; mRNA.
DR   RefSeq; NP_001117662.1; NM_001124190.1.
DR   AlphaFoldDB; Q90WG6; -.
DR   SMR; Q90WG6; -.
DR   GeneID; 100135794; -.
DR   KEGG; ag:BAB47150; -.
DR   KEGG; omy:100135794; -.
DR   CTD; 55907; -.
DR   OrthoDB; 1167540at2759; -.
DR   BioCyc; MetaCyc:MON-14551; -.
DR   BRENDA; 2.7.7.43; 4402.
DR   BRENDA; 2.7.7.92; 4402.
DR   SABIO-RK; Q90WG6; -.
DR   UniPathway; UPA00628; -.
DR   GO; GO:0005634; C:nucleus; IDA:AgBase.
DR   GO; GO:0090633; F:keto-deoxynonulosonic acid (KDN) cytidylyltransferase activity; IDA:AgBase.
DR   GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IDA:AgBase.
DR   GO; GO:0090632; F:N-glycolylneuraminic acid (Neu5Gc) cytidylyltransferase activity; IDA:AgBase.
DR   GO; GO:0006054; P:N-acetylneuraminate metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR003329; Cytidylyl_trans.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF02348; CTP_transf_3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
PE   2: Evidence at transcript level;
KW   Nucleotidyltransferase; Nucleus; Transferase.
FT   CHAIN           1..432
FT                   /note="N-acylneuraminate cytidylyltransferase"
FT                   /id="PRO_0000213202"
FT   ACT_SITE        188
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   432 AA;  48242 MW;  51947AC257B23382 CRC64;
     MAAAKKRTQS DIEDVRDRKA KVIKDSGEKR HIAALILARG GSKGIPLKNI KVLAGVPLIG
     WVLRAAVDSK QFDSVWVSTD HDDIEKVAKT WGAQVHRRSP EVSKDSSSSL DTIQEFARLN
     PEVDVICHIQ ATSPCLHPFH LKEALEMITK QGFTSVFSVV RRHHFRWQEV KKGGSVATQP
     LNLDPCNRPR RQDWDGELCE NGSFYIYTRA TIERGLQGGK WAYYEMLPEY SVDIDVDIDW
     PVAEQRVLRF GYFGLDKPEV VRLLLCNVSG CLTDGRVLIS VSGEEMVSVN TRDTMGIRML
     QREGVEVILI SSSEDLLTKA LADNLSQRTG CEVRQLGKDI QGEVIAMMDD KDLDWKEVAY
     MGNDAPDVDC LNLAGLSAVP RDAPVVAINA AKYSCHSAAG LGAVREFSEH ILLLKKKAKS
     QMEQDRIHRN TF