ID   NANA1_ECOL6             Reviewed;         297 AA.
AC   Q8FD58;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=N-acetylneuraminate lyase 1;
DE            Short=NAL 1;
DE            Short=Neu5Ac lyase 1;
DE            EC=4.1.3.3;
DE   AltName: Full=N-acetylneuraminate pyruvate-lyase 1;
DE   AltName: Full=N-acetylneuraminic acid aldolase 1;
DE   AltName: Full=Sialate lyase 1;
DE   AltName: Full=Sialic acid aldolase 1;
DE   AltName: Full=Sialic acid lyase 1;
GN   Name=nanA1; Synonyms=nanA; OrderedLocusNames=c3979;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the reversible aldol cleavage of N-acetylneuraminic
CC       acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine
CC       (ManNAc) via a Schiff base intermediate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aceneuramate = N-acetyl-D-mannosamine + pyruvate;
CC         Xref=Rhea:RHEA:23296, ChEBI:CHEBI:15361, ChEBI:CHEBI:17122,
CC         ChEBI:CHEBI:173083; EC=4.1.3.3;
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC       fructose 6-phosphate from N-acetylneuraminate: step 1/5.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DapA family. NanA subfamily. {ECO:0000305}.
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DR   EMBL; AE014075; AAN82419.1; -; Genomic_DNA.
DR   RefSeq; WP_000224707.1; NC_004431.1.
DR   AlphaFoldDB; Q8FD58; -.
DR   SMR; Q8FD58; -.
DR   STRING; 199310.c3979; -.
DR   EnsemblBacteria; AAN82419; AAN82419; c3979.
DR   KEGG; ecc:c3979; -.
DR   eggNOG; COG0329; Bacteria.
DR   HOGENOM; CLU_049343_6_0_6; -.
DR   OMA; LPPMRYK; -.
DR   BioCyc; ECOL199310:C3979-MON; -.
DR   UniPathway; UPA00629; UER00680.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008747; F:N-acetylneuraminate lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00954; NAL; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01237; N_acetylneuram_lyase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR005264; NanA.
DR   InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR   InterPro; IPR020624; Schiff_base-form_aldolases_CS.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   TIGRFAMs; TIGR00683; nanA; 1.
DR   PROSITE; PS00665; DHDPS_1; 1.
DR   PROSITE; PS00666; DHDPS_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Lyase; Schiff base.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..297
FT                   /note="N-acetylneuraminate lyase 1"
FT                   /id="PRO_0000103210"
FT   ACT_SITE        165
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         47..48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            137
FT                   /note="Involved in proton transfer during cleavage"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   297 AA;  32594 MW;  E752F7D9C7624C0A CRC64;
     MATNLRGVMA ALLTPFDQQQ ALDKASLRRL VQFNIQQGID GLYVGGSTGE AFVQSLSERE
     QVLEIVAEEA KGKIKLIAHV GCVSTAESQQ LAASAKRYGF DAVSAVTPFY YPFSFEEHCD
     HYRAIIDSAD GLPMVVYNIP ALSGVKLTLD QIDTLVTLPG VGALKQTSGD LYQMEQIRRE
     HPDLVLYNGY DEIFASGLLA GADGGIGSTY NIMGWRYQGI VKALKEGDIQ TAQKLQTECN
     KVIDLLIKTG VFRGLKTVLH YMDVVSVPLC RKPFGPVDEK YLPELKALAQ QLMQERG