ID Q3B0Q3_SYNS9 Unreviewed; 468 AA.
AC Q3B0Q3;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=N-acylneuraminate cytidylyltransferase {ECO:0000256|ARBA:ARBA00012491};
DE EC=2.7.7.43 {ECO:0000256|ARBA:ARBA00012491};
GN OrderedLocusNames=Syncc9902_0100 {ECO:0000313|EMBL:ABB25075.1};
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=316279 {ECO:0000313|EMBL:ABB25075.1, ECO:0000313|Proteomes:UP000002712};
RN [1] {ECO:0000313|Proteomes:UP000002712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902 {ECO:0000313|Proteomes:UP000002712};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family.
CC {ECO:0000256|ARBA:ARBA00010726}.
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DR EMBL; CP000097; ABB25075.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3B0Q3; -.
DR STRING; 316279.Syncc9902_0100; -.
DR KEGG; sye:Syncc9902_0100; -.
DR eggNOG; COG0546; Bacteria.
DR eggNOG; COG1083; Bacteria.
DR HOGENOM; CLU_583846_0_0_3; -.
DR UniPathway; UPA00628; -.
DR Proteomes; UP000002712; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR003329; Cytidylyl_trans.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR PANTHER; PTHR43434:SF3; GMP_IMP NUCLEOTIDASE YRFG; 1.
DR PANTHER; PTHR43434; PHOSPHOGLYCOLATE PHOSPHATASE; 1.
DR Pfam; PF02348; CTP_transf_3; 1.
DR Pfam; PF13419; HAD_2; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ABB25075.1}.
SQ SEQUENCE 468 AA; 54571 MW; 8DFE25BE04AB4CA5 CRC64;
MIMISHQYKN TDKEIMYKKI SAIVPIKFNS RRLPNKNFLN LNGRPLCSYI FQTLTQVEGI
HNIYCYASSS LPLNFLPKSV KYLQRPSYLD GDNIEATELF RYAIESIDTD IVIITHATSP
LIHSESIERG LQAVISGEYR SAYSVHKIQK YSWCDGKPVN FTPSKLEQTQ KISPVLYETS
GFYVFRKRDF LESNTRTTEP AFKVEIPISE AVDIDNPEDF ELATKLQYDN NITENELTSK
YFVDLIKRIS PESNLKESIS HICFDLDGVL IDSKIVMKIA WEECMRIFEL EQTFEEYFTH
LGIEFFEILK KIEIKKNLHD DIYKLYNEVS LNNSYKIKVY NNTREVLKRL KNAGFGLSIC
TSKSRKRTIE VLRRNNLIQY FDYISATEKE NKLRPKPAPD FLLECCTNLK VDPSQTIYIG
DTDYDHECAK RAHTAFIHAE WGYGRDNIRE KSIWLESIKD LDTLLIDE
//
