ID NANA_LACPL Reviewed; 292 AA. AC P59407; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 25-MAR-2003, sequence version 1. DT 20-JAN-2009, entry version 39. DE RecName: Full=N-acetylneuraminate lyase; DE EC=4.1.3.3; DE AltName: Full=N-acetylneuraminic acid aldolase; DE AltName: Full=N-acetylneuraminate pyruvate-lyase; DE AltName: Full=Sialic acid lyase; DE AltName: Full=Sialate lyase; DE AltName: Full=Sialic acid aldolase; GN Name=nanA; OrderedLocusNames=lp_3568; OS Lactobacillus plantarum. OC Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1590; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX MEDLINE=22480296; PubMed=12566566; DOI=10.1073/pnas.0337704100; RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., RA Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., RA Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., RA Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., RA De Vos W.M., Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). CC -!- FUNCTION: Catalyzes the cleavage of N-acetylneuraminic acid CC (sialic acid) to form pyruvate and N-acetylmannosamine via a CC Schiff base intermediate (By similarity). CC -!- CATALYTIC ACTIVITY: N-acetylneuraminate = N-acetyl-D-mannosamine + CC pyruvate. CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminic acid CC degradation; D-fructose 6-phosphate from N-acetylneuraminic acid: CC step 1/5. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the DHDPS family. NanA subfamily. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL935262; CAD65647.1; -; Genomic_DNA. DR RefSeq; NP_786769.1; -. DR HSSP; P44539; 1F73. DR GeneID; 1061995; -. DR GenomeReviews; AL935263_GR; lp_3568. DR KEGG; lpl:lp_3568; -. DR NMPDR; fig|220668.1.peg.2903; -. DR HOGENOM; P59407; -. DR BioCyc; LPLA220668:LP_3568-MON; -. DR BRENDA; 4.1.3.3; 593. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0008747; F:N-acetylneuraminate lyase activity; IEA:HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:HAMAP. DR HAMAP; MF_01237; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR002220; DHDPS. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR PANTHER; PTHR12128; DHDPS; 1. DR Pfam; PF00701; DHDPS; 1. DR PRINTS; PR00146; DHPICSNTHASE. DR ProDom; PD001859; DHDPS; 1. DR PROSITE; PS00665; DHDPS_1; 1. DR PROSITE; PS00666; DHDPS_2; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Lyase; KW Schiff base. FT CHAIN 1 292 N-acetylneuraminate lyase. FT /FTId=PRO_0000103215. FT REGION 46 47 Substrate binding (By similarity). FT ACT_SITE 163 163 Schiff-base intermediate with substrate FT (By similarity). FT SITE 135 135 Involved in proton transfer during FT cleavage (By similarity). SQ SEQUENCE 292 AA; 32708 MW; 4184967AE9C91747 CRC64; MSKKLLYAAQ MTAFDKDGNI NLDGIRALVR YNIDVNKVDG LYVCGSTGEA FMLNTDEKKQ VMETVYDEAN GAIDLVAQVG SLNLKEAKEL AKFATDLGYP KLSAVTPFYY NFTFEQIKDY YNEILKDVDN KLLIYSIPAL TGVALTTDQF AELFENPKII GIKYTNADFY LLERVRNAFP DKLILSGFDE MLLPALALNV DGCIGSTYNL NAPRVREEMD AFEAGDIDKA RQLQNISNDM ITDLIANDIY PTLKLVMKHM GVDAGYVKKP MSHPTPEMEA GATAIYEKYF KN //