ID NANA_CITK8 Reviewed; 297 AA.
AC A8AQB6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
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=CKO_04629;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-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; CP000822; ABV15679.1; -; Genomic_DNA.
DR RefSeq; WP_012135358.1; NC_009792.1.
DR AlphaFoldDB; A8AQB6; -.
DR SMR; A8AQB6; -.
DR STRING; 290338.CKO_04629; -.
DR GeneID; 45138162; -.
DR KEGG; cko:CKO_04629; -.
DR HOGENOM; CLU_049343_6_0_6; -.
DR OrthoDB; 199953at2; -.
DR UniPathway; UPA00629; UER00680.
DR Proteomes; UP000008148; 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; Reference proteome; Schiff base.
FT CHAIN 1..297
FT /note="N-acetylneuraminate lyase"
FT /id="PRO_1000066920"
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; 32706 MW; D2F7129AD2C16AC0 CRC64;
MAKDLRGVMP ALLTPFDNQQ KLDIESLRRL VRFNIAQGID GLYVGGSTGE AFVQSRAERE
QVLEIVAEEA KGKVTLIAHV GTVSTEESQQ LASAAHRYGF DAVSAVTPFY YPFSFEEHCD
HYRAIIDSAE GLPMVVYNIP ALSGVKLTLD QINTLVTLPG VGALKQTSGD LYQMEQIRRA
HPDLVLYNGY DEIFASGLLA GADGGIGSTY NIMGWRYQGI VKALQEGDVA KAQHLQTECN
KVIDLLIKTG VFRGLKTVLH YMDVVSVPLC RKPFSPVDEK YLPELKALAQ QLMQERG
//
