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 24-JAN-2024, entry version 103.
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; ENSPPYT00000005174.3; ENSPPYP00000004979.2; ENSPPYG00000004359.3.
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 OrthoDB; 5486419at2759; -.
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 CDD; cd02513; CMP-NeuAc_Synthase; 1.
DR CDD; cd01630; HAD_KDO-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR003329; Cytidylyl_trans.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR21485; HAD SUPERFAMILY MEMBERS CMAS AND KDSC; 1.
DR PANTHER; PTHR21485:SF3; N-ACYLNEURAMINATE CYTIDYLYLTRANSFERASE; 1.
DR Pfam; PF02348; CTP_transf_3; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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
//
