ID NANA_LACPL STANDARD; PRT; 292 AA. AC P59407; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE N-acetylneuraminate lyase (EC 4.1.3.3) (N-acetylneuraminic acid DE aldolase) (N-acetylneuraminate pyruvate-lyase) (Sialic acid lyase) DE (Sialate lyase) (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 SEQUENCE FROM N.A. RC STRAIN=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: N-acetylneuraminic acid (sialic acid) utilization. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic (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; -. DR HSSP; P44539; 1F73. DR HAMAP; MF_01237; -; 1. DR InterPro; IPR002220; DHDPS. DR Pfam; PF00701; DHDPS; 1. DR PRINTS; PR00146; DHPICSNTHASE. DR PROSITE; PS00665; DHDPS_1; 1. DR PROSITE; PS00666; DHDPS_2; FALSE_NEG. KW Carbohydrate metabolism; Complete proteome; Lyase; Schiff base. FT ACT_SITE 135 135 Involved in proton transfer during FT cleavage (By similarity). FT ACT_SITE 163 163 Schiff-base with N-acetylneuraminate (By FT 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 //