ID   NANA_STAAS              Reviewed;         293 AA.
AC   Q6GCF6;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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}; OrderedLocusNames=SAS0292;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG42063.1; -; Genomic_DNA.
DR   RefSeq; WP_001030738.1; NC_002953.3.
DR   AlphaFoldDB; Q6GCF6; -.
DR   SMR; Q6GCF6; -.
DR   KEGG; sas:SAS0292; -.
DR   HOGENOM; CLU_049343_5_1_9; -.
DR   OMA; VVPPVCT; -.
DR   UniPathway; UPA00629; UER00680.
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   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   PROSITE; PS00666; DHDPS_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Lyase; Schiff base.
FT   CHAIN           1..293
FT                   /note="N-acetylneuraminate lyase"
FT                   /id="PRO_0000103225"
FT   ACT_SITE        165
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT   BINDING         48..49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT   SITE            137
FT                   /note="Involved in proton transfer during cleavage"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
SQ   SEQUENCE   293 AA;  33043 MW;  62D7DEFFDC1AF431 CRC64;
     MNKDLKGLYA ALLVPFDENG QVNEQGLKQI AQNAIETEEL DGLYVNGSSG ENFLLNTEQK
     KQVFKVAKEA VGDKVKLIAQ VGSLDLNEAI ELGKYATELG YDALSAVTPF YYPFTFEEIR
     DYYFDIIEAT QNNMIIYAIP DLTGVNISIE QFSELFNHEK IVGVKYTAPN FFLLERIRKA
     FPDKLILSGF DEMLVQATIS GVDGAIGSTY NVNGRRARKI FDLARQGQIQ EAYQLQHDSN
     DIIETVLSMG IYPTLKEILR HRGIDAGLPK RPFKPFNEAH RQTLDQLIAK YDL