NEUA_BOVIN
ID NEUA_BOVIN Reviewed; 434 AA.
AC Q3SZM5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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; BC102786; AAI02787.1; -; mRNA.
DR RefSeq; NP_001030475.1; NM_001035398.1.
DR AlphaFoldDB; Q3SZM5; -.
DR SMR; Q3SZM5; -.
DR STRING; 9913.ENSBTAP00000013373; -.
DR PaxDb; Q3SZM5; -.
DR PRIDE; Q3SZM5; -.
DR Ensembl; ENSBTAT00000013373; ENSBTAP00000013373; ENSBTAG00000010136.
DR GeneID; 100336710; -.
DR KEGG; bta:100336710; -.
DR CTD; 55907; -.
DR VEuPathDB; HostDB:ENSBTAG00000010136; -.
DR VGNC; VGNC:27476; CMAS.
DR eggNOG; ENOG502QQH3; Eukaryota.
DR GeneTree; ENSGT00390000004237; -.
DR InParanoid; Q3SZM5; -.
DR OMA; FHGFVWR; -.
DR OrthoDB; 781897at2759; -.
DR UniPathway; UPA00628; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000010136; Expressed in spermatocyte and 104 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 Acetylation; Methylation; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..434
FT /note="N-acylneuraminate cytidylyltransferase"
FT /id="PRO_0000317033"
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; 48438 MW; 7B5A3C9A3B194412 CRC64;
MDSVEKGAAT SVSNPRGRPS RGRPPKLQRN SRGGQGRGVE KPPHMAALIL ARGGSKGIPL
KNIKHLAGVP LIGWVLRAAL DSGVFQSIWV STDHDEIENV AKQFGAQVHR RSSEASKDSS
TSLDAIIEFL NYHNEVDIVG NIQATSPCLH PTDLQKVAEM IREEGYDSVF SVVRRHQFRW
GEIQKGVREM TEPLNLNPAK RPRRQDWDGE LYENGSFYFA KRHLIEMGYL QGGKMAYYEM
RAEHSVDIDV DIDWPIAEQR VLRYGYFGKE KLKEIKLFVC NIDGCLTNGH IYVSGDQKEI
ISYDVKDAIG ISLLKKSGIE VRLISERACS KQTLSSLKLD CKMEVNVPDK LAVVDEWRKE
MGLCWKEVAY LGNEVSDEEC LKKVGLSGVP ADACAAAQKA VGYICKSSGG RGALREFAEH
IFLLMEKVIN SCQK
