ID   NEUA_ECOLX              Reviewed;         419 AA.
AC   P13266;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=neuA;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 406-419, AND
RP   SUBUNIT.
RC   STRAIN=K1;
RX   PubMed=2549035; DOI=10.1016/s0021-9258(18)63765-2;
RA   Zapata G., Vann W.F., Aaronson W., Lewis M.S., Moos M.;
RT   "Sequence of the cloned Escherichia coli K1 CMP-N-acetylneuraminic acid
RT   synthetase gene.";
RL   J. Biol. Chem. 264:14769-14774(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-13, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   STRAIN=K1 / RS218 / O18:K1:H7;
RX   PubMed=2826425; DOI=10.1016/s0021-9258(18)45417-8;
RA   Vann W.F., Silver R.P., Abeijon C., Chang K., Aaronson W., Sutton A.,
RA   Finn C.W., Lindner W., Kotsatos M.;
RT   "Purification, properties, and genetic location of Escherichia coli
RT   cytidine 5'-monophosphate N-acetylneuraminic acid synthetase.";
RL   J. Biol. Chem. 262:17556-17562(1987).
CC   -!- FUNCTION: Catalyzes the formation of CMP-N-acetylneuraminic acid (CMP-
CC       NeuNAc), which is essential for the formation of the capsule.
CC       {ECO:0000269|PubMed:2826425}.
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:0000269|PubMed:2826425};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:2826425};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:2826425};
CC   -!- ACTIVITY REGULATION: Inhibited by the CTP analogs 5-mercuri-CTP and
CC       CTP-2',3'-dialdehyde. {ECO:0000269|PubMed:2826425}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4 mM for NeuNAc (at pH 9.0) {ECO:0000269|PubMed:2826425};
CC         KM=0.31 mM for CTP (at pH 9.0) {ECO:0000269|PubMed:2826425};
CC       pH dependence:
CC         Optimum pH is 9.0-10.0. {ECO:0000269|PubMed:2826425};
CC   -!- SUBUNIT: Monomer. May form aggregates. {ECO:0000269|PubMed:2549035}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2826425}.
CC   -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. {ECO:0000305}.
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DR   EMBL; J05023; AAA24210.1; -; Genomic_DNA.
DR   PIR; A36509; A36509.
DR   AlphaFoldDB; P13266; -.
DR   SMR; P13266; -.
DR   BioCyc; MetaCyc:MON-14544; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
DR   GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IEA:UniProtKB-EC.
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   1: Evidence at protein level;
KW   Capsule biogenesis/degradation; Cytoplasm; Direct protein sequencing;
KW   Magnesium; Manganese; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..419
FT                   /note="N-acylneuraminate cytidylyltransferase"
FT                   /id="PRO_0000213203"
SQ   SEQUENCE   419 AA;  48736 MW;  AB8E7793CDD74F19 CRC64;
     MRTKIIAIIP ARSGSKGLRN KNALMLIDKP LLAYTIEAAL QSEMFEKVIV TTDSEQYGAI
     AESYGADFLL RPEELATDKA SSFEFIKHAL SIYTDYESFA LLQPTSPFRD STHIIEAVKL
     YQTLEKYQCV VSVTRSNKPS QIIRPLDDYS TLSFFDLDYS KYNRNSIVEY HPNGAIFIAN
     KQHYLHTKHF FGRYSLAYIM DKESSLDIDD RMDFELAITI QQKKNRQKID LYQNIHNRIN
     EKRNEFDSVS DITLIGHSLF DYWDVKKIND IEVNNLGIAG INSKEYYEYI IEKELIVNFG
     EFVFIFFGTN DIVVSDWKKE DTLWYLKKTC QYIKKKNAAS KIYLLSVPPV FGRIDRDNRI
     INDLNSYLRE NVDFAKFISL DHVLKDSYGN LNKMYTYDGL HFNSNGYTVL ENEIAEIVK