ID A0A3Q7RZ86_VULVU Unreviewed; 434 AA.
AC A0A3Q7RZ86;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=N-acylneuraminate cytidylyltransferase {ECO:0000256|ARBA:ARBA00020893};
DE EC=2.7.7.43 {ECO:0000256|ARBA:ARBA00012491};
DE AltName: Full=CMP-N-acetylneuraminic acid synthase {ECO:0000256|ARBA:ARBA00032878};
GN Name=CMAS {ECO:0000313|RefSeq:XP_025850899.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025850899.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025850899.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025850899.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025850899.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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). {ECO:0000256|ARBA:ARBA00024902}.
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:0000256|ARBA:ARBA00001862};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate metabolism.
CC {ECO:0000256|ARBA:ARBA00005141}.
CC -!- SUBUNIT: Homotetramer; the active enzyme is formed by a dimer of
CC dimers. {ECO:0000256|ARBA:ARBA00011658}.
CC -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family.
CC {ECO:0000256|ARBA:ARBA00010726}.
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DR RefSeq; XP_025850899.1; XM_025995114.1.
DR AlphaFoldDB; A0A3Q7RZ86; -.
DR SMR; A0A3Q7RZ86; -.
DR STRING; 9627.ENSVVUP00000000957; -.
DR Ensembl; ENSVVUT00000001454; ENSVVUP00000000957; ENSVVUG00000000839.
DR KEGG; vvp:112917221; -.
DR OMA; FHGFVWR; -.
DR OrthoDB; 5486419at2759; -.
DR UniPathway; UPA00628; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Nucleotidyltransferase {ECO:0000313|RefSeq:XP_025850899.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Transferase {ECO:0000313|RefSeq:XP_025850899.1}.
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 48487 MW; F37D887A4ADCB201 CRC64;
MDSVEKGAAT SVSNPRGRPS RGRPPKLQRN SRGGQGRGVE KPPHLAALVL ARGGSKGIPL
KNIKHLAGVP LIGWVLRAAL DSGVFQSVWV 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 CKMEVNVPDK LAVLDEWRKE
MGLCWKEVAY LGNEVSDEEC LKKVGLSGVP ADACSTAQKA VGYICKCNGG RGALREFAEH
IFLLMEKVIN SCQK
//
