NANA_STAAR
ID NANA_STAAR Reviewed; 293 AA.
AC Q6GK01;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=N-acetylneuraminate lyase {ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000303|PubMed:23519810};
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, ECO:0000269|PubMed:23519810};
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, ECO:0000303|PubMed:23519810};
GN OrderedLocusNames=SAR0312;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND PATHWAY.
RC STRAIN=MRSA252;
RX PubMed=23519810; DOI=10.1107/s1744309113003060;
RA North R.A., Kessans S.A., Atkinson S.C., Suzuki H., Watson A.J.,
RA Burgess B.R., Angley L.M., Hudson A.O., Varsani A., Griffin M.D.,
RA Fairbanks A.J., Dobson R.C.;
RT "Cloning, expression, purification, crystallization and preliminary X-ray
RT diffraction studies of N-acetylneuraminate lyase from methicillin-resistant
RT Staphylococcus aureus.";
RL Acta Crystallogr. F 69:306-312(2013).
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, ECO:0000269|PubMed:23519810}.
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, ECO:0000269|PubMed:23519810};
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, ECO:0000303|PubMed:23519810}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01237,
CC ECO:0000303|PubMed:23519810}.
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; BX571856; CAG39336.1; -; Genomic_DNA.
DR RefSeq; WP_001030738.1; NC_002952.2.
DR AlphaFoldDB; Q6GK01; -.
DR SMR; Q6GK01; -.
DR KEGG; sar:SAR0312; -.
DR HOGENOM; CLU_049343_5_1_9; -.
DR OMA; VVPPVCT; -.
DR OrthoDB; 1438588at2; -.
DR BRENDA; 4.1.3.3; 3352.
DR UniPathway; UPA00629; UER00680.
DR Proteomes; UP000000596; 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 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Lyase; Schiff base.
FT CHAIN 1..293
FT /note="N-acetylneuraminate lyase"
FT /id="PRO_0000103224"
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
