ID   NANA2_ECOL6             Reviewed;         305 AA.
AC   Q8FDU7;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=N-acetylneuraminate lyase 2;
DE            Short=NAL 2;
DE            Short=Neu5Ac lyase 2;
DE            EC=4.1.3.3;
DE   AltName: Full=N-acetylneuraminate pyruvate-lyase 2;
DE   AltName: Full=N-acetylneuraminic acid aldolase 2;
DE   AltName: Full=Sialate lyase 2;
DE   AltName: Full=Sialic acid aldolase 2;
DE   AltName: Full=Sialic acid lyase 2;
GN   Name=nanA2; OrderedLocusNames=c3639;
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; AAN82087.1; -; Genomic_DNA.
DR   RefSeq; WP_001149834.1; NC_004431.1.
DR   AlphaFoldDB; Q8FDU7; -.
DR   SMR; Q8FDU7; -.
DR   STRING; 199310.c3639; -.
DR   EnsemblBacteria; AAN82087; AAN82087; c3639.
DR   KEGG; ecc:c3639; -.
DR   eggNOG; COG0329; Bacteria.
DR   HOGENOM; CLU_049343_6_0_6; -.
DR   OMA; VVPPVCT; -.
DR   BioCyc; ECOL199310:C3639-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   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   CHAIN           1..305
FT                   /note="N-acetylneuraminate lyase 2"
FT                   /id="PRO_0000103211"
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   305 AA;  34098 MW;  50482F39B3C701A3 CRC64;
     MQCEFKGVIS ALPTPYDQSQ QIDMESLRKL IRFNIEQNIK GLYVGGSTGE AFLQNVAERE
     KILETVADES DGRLTLIAHV GGISTAESEV LAKAAKKYGY HAISAVTPFY YPFSFEEHCI
     HYRKIIDSAD GLPMVVYNIP ALSGVRFSLD QINELVTIPR VCALKQTSGD LFQMEQIKRN
     HPELVLYNGY DEIFASGLIA GADGGIGSTY NIMGWRYLEI FEAVKNNDVI KAKEMQVACN
     QVIDTLIQSG VLAGIKTLLY YMGIINTPVC RSPFSPVKEK NLDVLSKLAE RLFEEHDRNK
     KMKII