ID   NEUA_STRA5              Reviewed;         413 AA.
AC   Q9AFG9;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 100.
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; OrderedLocusNames=SAG1158;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CNCTC 1/82 / Serotype V;
RA   McKinnon K., Chaffin D.O., Rubens C.E.;
RT   "Streptococcus agalactiae type V polysaccharide synthesis operon complete
RT   sequence.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
CC   -!- FUNCTION: Catalyzes the formation of CMP-N-acetylneuraminic acid (CMP-
CC       NeuNAc), which is essential for the formation of the capsule.
CC       {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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. {ECO:0000305}.
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DR   EMBL; AF349539; AAK29664.1; -; Genomic_DNA.
DR   EMBL; AE009948; AAN00040.1; -; Genomic_DNA.
DR   RefSeq; NP_688167.1; NC_004116.1.
DR   RefSeq; WP_000802362.1; NC_004116.1.
DR   AlphaFoldDB; Q9AFG9; -.
DR   SMR; Q9AFG9; -.
DR   STRING; 208435.SAG1158; -.
DR   EnsemblBacteria; AAN00040; AAN00040; SAG1158.
DR   KEGG; sag:SAG1158; -.
DR   PATRIC; fig|208435.3.peg.1164; -.
DR   HOGENOM; CLU_660110_0_0_9; -.
DR   OMA; LQWITEI; -.
DR   BRENDA; 2.7.7.43; 5917.
DR   Proteomes; UP000000821; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR003329; Cytidylyl_trans.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   Pfam; PF02348; CTP_transf_3; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Capsule biogenesis/degradation; Cytoplasm; Exopolysaccharide synthesis;
KW   Magnesium; Manganese; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..413
FT                   /note="N-acylneuraminate cytidylyltransferase"
FT                   /id="PRO_0000213209"
SQ   SEQUENCE   413 AA;  47644 MW;  0AB5C0554F44172D CRC64;
     MKPICIIPAR SGSKGLPDKN MLFLSGKPMI FHTIDAAIES GMFDKKDIFV STDSELYREI
     CLERGISVVM RKPELSTDQA TSYDMLKDFL SDYEDNQEFV LLQVTSPLRK SWHIKEAMEY
     YSSHDVDNVV SFSEVEKHPS LFTTLSDEGY AIDMVGADKG YRRQDLQPLY YPNGAIFISN
     KETYLREKSF FTSRTYAYQM AKEFSLDVDT RDDFIHVIGH LFFDYAIREK ENKVFYKEGY
     SRLFNREASK IILGDSKTIS TSLESYHNYS QGGVTLATML ENLPNFLTAN VTEAFVSIGV
     NDLITGYSVE EIFSNFQKLY SLLAENKIKM RLTTIAYTLF RETVNNADIE KINQWLTEFC
     YQNQIPLLDI NRFLSKDGNL NYHLTSDGLH FTQEANDLLQ SQYQLFVDEV KTL