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Database: UniProt
Entry: NANA_ECO7I
LinkDB: NANA_ECO7I
Original site: NANA_ECO7I 
ID   NANA_ECO7I              Reviewed;         297 AA.
AC   B7NKT6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=N-acetylneuraminate lyase {ECO:0000255|HAMAP-Rule:MF_01237};
DE            Short=NAL {ECO:0000255|HAMAP-Rule:MF_01237};
DE            Short=Neu5Ac lyase {ECO:0000255|HAMAP-Rule:MF_01237};
DE            EC=4.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01237};
DE   AltName: Full=N-acetylneuraminate pyruvate-lyase {ECO:0000255|HAMAP-Rule:MF_01237};
DE   AltName: Full=N-acetylneuraminic acid aldolase {ECO:0000255|HAMAP-Rule:MF_01237};
DE   AltName: Full=Sialate lyase {ECO:0000255|HAMAP-Rule:MF_01237};
DE   AltName: Full=Sialic acid aldolase {ECO:0000255|HAMAP-Rule:MF_01237};
DE   AltName: Full=Sialic acid lyase {ECO:0000255|HAMAP-Rule:MF_01237};
GN   Name=nanA {ECO:0000255|HAMAP-Rule:MF_01237};
GN   OrderedLocusNames=ECIAI39_3714;
OS   Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI39 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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:0000255|HAMAP-
CC       Rule:MF_01237}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01237};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC       fructose 6-phosphate from N-acetylneuraminate: step 1/5.
CC       {ECO:0000255|HAMAP-Rule:MF_01237}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01237}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01237}.
CC   -!- SIMILARITY: Belongs to the DapA family. NanA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01237}.
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DR   EMBL; CU928164; CAR19830.1; -; Genomic_DNA.
DR   RefSeq; WP_000224706.1; NC_011750.1.
DR   RefSeq; YP_002409617.1; NC_011750.1.
DR   AlphaFoldDB; B7NKT6; -.
DR   SMR; B7NKT6; -.
DR   STRING; 585057.ECIAI39_3714; -.
DR   GeneID; 69474002; -.
DR   KEGG; ect:ECIAI39_3714; -.
DR   PATRIC; fig|585057.6.peg.3849; -.
DR   HOGENOM; CLU_049343_6_0_6; -.
DR   UniPathway; UPA00629; UER00680.
DR   Proteomes; UP000000749; 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; Aldolase class I; 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   NCBIfam; TIGR00683; nanA; 1.
DR   PANTHER; PTHR42849; N-ACETYLNEURAMINATE LYASE; 1.
DR   PANTHER; PTHR42849:SF1; N-ACETYLNEURAMINATE LYASE; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   SUPFAM; SSF51569; Aldolase; 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..297
FT                   /note="N-acetylneuraminate lyase"
FT                   /id="PRO_1000139732"
FT   ACT_SITE        137
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT   ACT_SITE        165
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT   BINDING         47
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT   BINDING         48
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT   BINDING         167
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT   BINDING         189
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT   BINDING         191
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT   BINDING         192
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT   BINDING         208
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
SQ   SEQUENCE   297 AA;  32579 MW;  BAE830B3D7173145 CRC64;
     MATNLRGVMA ALLTPFDQQQ ALDKASLRRL VQFNIQQGID GLYVGGSTGE AFVQSLSERE
     QVLEIVAEEA KGKIKLIAHV GCVSTAESQQ LAASAKRYGF DAVSAVTPFY YPFSFEEHCD
     HYRAIIDSAD GLPMVVYNIP ALSGVKLSLD QINTLVTLPG VGALKQTSGD LYQMEQIRRE
     HPDLVLYNGY DEIFASGLLA GADGGIGSTY NIMGWRYQGI VKALKEGDIQ TAQKLQTECN
     KVIDLLIKTG VFRGLKTVLH YMDVVSVPLC RKPFGPVDEK YLPELKALAQ QLMQERG
//
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