NEUA_NEIME
ID NEUA_NEIME Reviewed; 228 AA.
AC P0A0Z8; Q57385;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 62.
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;
OS Neisseria meningitidis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=487;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NRCC 4030 / 406Y / Serogroup Y;
RA Gilbert M., Watson D.C., Wakarchuk W.W.;
RT "Purification and characterization of the recombinant CMP-sialic acid
RT synthetase from Neisseria meningitidis.";
RL Biotechnol. Lett. 19:417-420(1997).
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; U60146; AAB60780.1; -; Genomic_DNA.
DR RefSeq; WP_002215295.1; NZ_WSOH01000068.1.
DR PDB; 1EYR; X-ray; 2.20 A; A/B=1-228.
DR PDB; 1EZI; X-ray; 2.00 A; A/B=1-228.
DR PDB; 6CKJ; X-ray; 1.75 A; A=1-228.
DR PDB; 6CKK; X-ray; 1.80 A; A/B=1-228.
DR PDB; 6CKL; X-ray; 2.68 A; A/B/C=1-228.
DR PDB; 6CKM; X-ray; 1.54 A; A=1-228.
DR PDBsum; 1EYR; -.
DR PDBsum; 1EZI; -.
DR PDBsum; 6CKJ; -.
DR PDBsum; 6CKK; -.
DR PDBsum; 6CKL; -.
DR PDBsum; 6CKM; -.
DR AlphaFoldDB; P0A0Z8; -.
DR SMR; P0A0Z8; -.
DR DrugBank; DB04555; Cytidine-5'-Diphosphate.
DR GeneID; 61282335; -.
DR OMA; AYHMKEL; -.
DR BRENDA; 2.7.7.43; 3593.
DR EvolutionaryTrace; P0A0Z8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IEA:UniProtKB-EC.
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 3D-structure; Cytoplasm; Nucleotidyltransferase; Transferase.
FT CHAIN 1..228
FT /note="N-acylneuraminate cytidylyltransferase"
FT /id="PRO_0000213206"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:6CKM"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:6CKM"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:6CKM"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:6CKM"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:6CKM"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:6CKM"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:6CKM"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:6CKM"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:6CKM"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:6CKM"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:6CKM"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:6CKM"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:6CKM"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:6CKM"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:6CKM"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:6CKM"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:6CKM"
FT STRAND 172..182
FT /evidence="ECO:0007829|PDB:6CKM"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:6CKM"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:6CKM"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:6CKM"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:6CKM"
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