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NANA_STAAC
ID   NANA_STAAC              Reviewed;         293 AA.
AC   Q5HJ53;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=SACOL0312;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW37519.1; -; Genomic_DNA.
DR   RefSeq; WP_001030738.1; NC_002951.2.
DR   AlphaFoldDB; Q5HJ53; -.
DR   SMR; Q5HJ53; -.
DR   EnsemblBacteria; AAW37519; AAW37519; SACOL0312.
DR   KEGG; sac:SACOL0312; -.
DR   HOGENOM; CLU_049343_5_1_9; -.
DR   OMA; VVPPVCT; -.
DR   UniPathway; UPA00629; UER00680.
DR   Proteomes; UP000000530; 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   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_0000103221"
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
 
 
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