ID   NEUA_PONAB              Reviewed;         434 AA.
AC   Q5R6R5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Has some activity
CC       toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-
CC       glycero-D-galacto-nononic acid (KDN) (By similarity). {ECO:0000250}.
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   -!- 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:0000250}.
CC   -!- DOMAIN: The BC2 (basic cluster 2) motif is necessary and sufficient for
CC       the nuclear localization and contains the catalytic active site. The
CC       localization in the nucleus is however not required for the enzyme
CC       activity (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. {ECO:0000305}.
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DR   EMBL; CR860420; CAH92545.1; -; mRNA.
DR   RefSeq; NP_001126489.1; NM_001133017.2.
DR   AlphaFoldDB; Q5R6R5; -.
DR   SMR; Q5R6R5; -.
DR   STRING; 9601.ENSPPYP00000004979; -.
DR   Ensembl; ENSPPYT00000005174; ENSPPYP00000004979; ENSPPYG00000004359.
DR   GeneID; 100173476; -.
DR   KEGG; pon:100173476; -.
DR   CTD; 55907; -.
DR   eggNOG; ENOG502QQH3; Eukaryota.
DR   GeneTree; ENSGT00390000004237; -.
DR   HOGENOM; CLU_042930_0_1_1; -.
DR   InParanoid; Q5R6R5; -.
DR   OMA; FHGFVWR; -.
DR   OrthoDB; 781897at2759; -.
DR   TreeFam; TF324840; -.
DR   UniPathway; UPA00628; -.
DR   Proteomes; UP000001595; Chromosome 12.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; ISS: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   Acetylation; Methylation; Nucleotidyltransferase; Nucleus;
KW   Reference proteome; Transferase.
FT   CHAIN           1..434
FT                   /note="N-acylneuraminate cytidylyltransferase"
FT                   /id="PRO_0000317034"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           15..31
FT                   /note="BC1 motif"
FT   MOTIF           200..206
FT                   /note="BC2 motif"
FT   MOTIF           269..276
FT                   /note="BC3 motif"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        201
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFW8"
FT   MOD_RES         37
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT   MOD_RES         52
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99KK2"
SQ   SEQUENCE   434 AA;  48423 MW;  B303B6647AA91A3A CRC64;
     MDSVEKGAAT SVSNPRGRPS RGRPPKLQRN SRGGQGRGVE KPPHLAALIL ARGGSKGIPL
     KNIKHLAGVP LIGWVLRAAL DSGAFQSVWV STDHDEIENV AKQFGAQVHR RSSEVSKDSS
     TSLDAIIEFL NYHNEVDIVG NIQATSPCLH PTDLQKVAEM IREEGYDSVF SVVRRHQFRW
     SEIQKGVREV TEPLNLNPAK RPRRQDWDGE LYENGSFYFA KRHLIEMGYL QGGKMAYYEM
     RAEHSVDIDV DIDWPIAEQR VLRYGYFGKE KLKEIKLLVC NIDGCLTNGH IYVSGDQKEI
     ISYDVKDAIG ISLLKKSGIE VRLISERACS KQTLSSLKLD CKMEVSVSDK LAVVDEWRKE
     MGLCWKEVAY LGNEVSDEEC LKRVGLSGAP ADACSTAQKA VGYICKCNGG RGAIREFAEH
     IFLLMEKVNN SCQK