NANA_SALAR
ID NANA_SALAR Reviewed; 297 AA.
AC A9MNY6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=SARI_04285;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000880; ABX24068.1; -; Genomic_DNA.
DR RefSeq; WP_001029661.1; NC_010067.1.
DR AlphaFoldDB; A9MNY6; -.
DR SMR; A9MNY6; -.
DR STRING; 41514.SARI_04285; -.
DR EnsemblBacteria; ABX24068; ABX24068; SARI_04285.
DR KEGG; ses:SARI_04285; -.
DR HOGENOM; CLU_049343_6_0_6; -.
DR OMA; LPPMRYK; -.
DR OrthoDB; 1438588at2; -.
DR UniPathway; UPA00629; UER00680.
DR Proteomes; UP000002084; 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 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; Reference proteome; Schiff base.
FT CHAIN 1..297
FT /note="N-acetylneuraminate lyase"
FT /id="PRO_1000085738"
FT ACT_SITE 165
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT BINDING 47..48
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 297 AA; 32495 MW; 3F9484A670525D1A CRC64;
MAKALQGVMA ALLTPFDHQQ QLDSESLRRL VRFNIEQGID GLYVGGSTGE AFVQSLAERE
QVLEIVAEEA KGKITLIAHV GTVSTAGSQQ LASAAKRYGF DAVSAVTPFY YPFSFEEHCD
HYRAIIDSAD GLPMVVYNIP ALSGVKLTLD QINTLVTLPG VSALKQTSGD LFQMEQIRRA
HPDLVLYNGY DEIFASGLLA GADGGIGSTY NIMGWRYQGI VQALREGDVA KAQRLQTECN
KVIDLLIKTG VFRGLKTVLH YMDVVSVPLC RKPFAPVDEK YLPELKALAQ QLLEEKA