NEUA_NEIMB
ID NEUA_NEIMB Reviewed; 228 AA.
AC P0A0Z7; Q57385;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
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;
DE AltName: Full=CMP-sialic acid synthase;
GN Name=neuA; Synonyms=siaB, synB; OrderedLocusNames=NMB0069;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B1940 / Serogroup B;
RX PubMed=1398032; DOI=10.1016/0378-1097(92)90397-7;
RA Edwards U., Frosch M.;
RT "Sequence and functional analysis of the cloned Neisseria meningitidis CMP-
RT NeuNAc synthetase.";
RL FEMS Microbiol. Lett. 75:161-166(1992).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=7830552; DOI=10.1111/j.1365-2958.1994.tb01274.x;
RA Edwards U., Mueller A., Hammerschmidt S., Gerardy-Schahn R., Frosch M.;
RT "Molecular analysis of the biosynthesis pathway of the alpha-2,8 polysialic
RT acid capsule by Neisseria meningitidis serogroup B.";
RL Mol. Microbiol. 14:141-149(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NMB / Serogroup B;
RX PubMed=8113198; DOI=10.1128/jb.176.5.1530-1534.1994;
RA Swartley J.S., Stephens D.S.;
RT "Identification of a genetic locus involved in the biosynthesis of N-
RT acetyl-D-mannosamine, a precursor of the (alpha 2-->8)-linked polysialic
RT acid capsule of serogroup B Neisseria meningitidis.";
RL J. Bacteriol. 176:1530-1534(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=NCTC 8249 / Serogroup B;
RX PubMed=8045888; DOI=10.1128/jb.176.15.4583-4589.1994;
RA Ganguli S., Zapata G., Wallis T., Reid C., Boulnois G.J., Vann W.F.,
RA Roberts I.S.;
RT "Molecular cloning and analysis of genes for sialic acid synthesis in
RT Neisseria meningitidis group B and purification of the meningococcal CMP-
RT NeuNAc synthetase enzyme.";
RL J. Bacteriol. 176:4583-4589(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. {ECO:0000305}.
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DR EMBL; M95053; AAA20476.1; -; Genomic_DNA.
DR EMBL; U04328; AAA17655.1; -; Unassigned_DNA.
DR EMBL; X78068; CAA54983.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF40536.1; -; Genomic_DNA.
DR PIR; B53384; B53384.
DR RefSeq; NP_273133.1; NC_003112.2.
DR RefSeq; WP_002215295.1; NC_003112.2.
DR AlphaFoldDB; P0A0Z7; -.
DR SMR; P0A0Z7; -.
DR STRING; 122586.NMB0069; -.
DR PaxDb; P0A0Z7; -.
DR EnsemblBacteria; AAF40536; AAF40536; NMB0069.
DR GeneID; 61282335; -.
DR KEGG; nme:NMB0069; -.
DR PATRIC; fig|122586.8.peg.103; -.
DR HOGENOM; CLU_042930_1_0_4; -.
DR OMA; AYHMKEL; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IBA:GO_Central.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR003329; Cytidylyl_trans.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF02348; CTP_transf_3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..228
FT /note="N-acylneuraminate cytidylyltransferase"
FT /id="PRO_0000213205"
SQ SEQUENCE 228 AA; 24892 MW; F2510733EE1C3A31 CRC64;
MEKQNIAVIL ARQNSKGLPL KNLRKMNGIS LLGHTINAAI SSKCFDRIIV STDGGLIAEE
AKNFGVEVVL RPAELASDTA SSISGVIHAL ETIGSNSGTV TLLQPTSPLR TGAHIREAFS
LFDEKIKGSV VSACPMEHHP LKTLLQINNG EYAPMRHLSD LEQPRQQLPQ AFRPNGAIYI
NDTASLIANN CFFIAPTKLY IMSHQDSIDI DTELDLQQAE NILNHKES