NANA_LACPL
ID NANA_LACPL Reviewed; 292 AA.
AC P59407; F9ULC3;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=N-acetylneuraminate lyase {ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000303|PubMed:21317263};
DE Short=NAL {ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000303|PubMed:21317263};
DE Short=Neu5Ac lyase {ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000303|PubMed:21317263};
DE EC=4.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000269|PubMed:21317263};
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, ECO:0000303|PubMed:21317263};
DE AltName: Full=Sialic acid lyase {ECO:0000255|HAMAP-Rule:MF_01237};
GN Name=nanA {ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000303|PubMed:21317263};
GN OrderedLocusNames=lp_3568;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP BIOTECHNOLOGY, AND 3D-STRUCTURE MODELING.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=21317263; DOI=10.1128/aem.02927-10;
RA Sanchez-Carron G., Garcia-Garcia M.I., Lopez-Rodriguez A.B.,
RA Jimenez-Garcia S., Sola-Carvajal A., Garcia-Carmona F., Sanchez-Ferrer A.;
RT "Molecular characterization of a novel N-acetylneuraminate lyase from
RT Lactobacillus plantarum WCFS1.";
RL Appl. Environ. Microbiol. 77:2471-2478(2011).
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:21317263}.
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:21317263};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 mM for N-acetylneuraminate {ECO:0000269|PubMed:21317263};
CC KM=160 mM for N-acetyl-D-mannosamine {ECO:0000269|PubMed:21317263};
CC KM=19.9 mM for pyruvate {ECO:0000269|PubMed:21317263};
CC Note=kcat is 10.08 sec(-1) for the cleavage of Neu5Ac and 4.8 sec(-1)
CC for the synthetic reaction. {ECO:0000269|PubMed:21317263};
CC pH dependence:
CC Optimum pH is 7-7.3 in both synthetic and cleavage directions. Is
CC active over a broad pH range, from pH 5.0 to 9.0, in both directions.
CC Maintains 5 to 10% activity in the synthetic direction above pH 11.0.
CC The enzyme is also stable at basic pHs, where it maintains around 80%
CC residual synthetic activity after 15 days of incubation.
CC {ECO:0000269|PubMed:21317263};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius for synthetic activity and
CC up to 70 degrees Celsius for the cleavage reaction. Is very
CC thermostable, maintaining 80% of cleavage activity after 48 hours at
CC 60 degrees Celsius. However, at higher temperatures (70 degrees
CC Celsius), activity decreases to less than 10% in 8 hours. Temperature
CC stability is further improved by the presence of stabilizing
CC additives. {ECO:0000269|PubMed:21317263};
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 ECO:0000269|PubMed:21317263}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01237}.
CC -!- BIOTECHNOLOGY: The good synthetic activity of this enzyme at basic pHs,
CC together with its thermostability and pH stability at such pHs,
CC underlines the potential biotechnological application of this new NAL
CC for the chemo-enzymatic synthesis of sialic acid and its derivatives.
CC Thus, these characteristics make this enzyme a promising biocatalyst.
CC {ECO:0000303|PubMed:21317263}.
CC -!- SIMILARITY: Belongs to the DapA family. NanA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01237}.
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DR EMBL; AL935263; CCC80530.1; -; Genomic_DNA.
DR RefSeq; WP_003646215.1; NC_004567.2.
DR RefSeq; YP_004891044.1; NC_004567.2.
DR AlphaFoldDB; P59407; -.
DR SMR; P59407; -.
DR STRING; 220668.lp_3568; -.
DR EnsemblBacteria; CCC80530; CCC80530; lp_3568.
DR GeneID; 57026766; -.
DR KEGG; lpl:lp_3568; -.
DR PATRIC; fig|220668.9.peg.2977; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_6_0_9; -.
DR OMA; VVPPVCT; -.
DR PhylomeDB; P59407; -.
DR BioCyc; LPLA220668:G1GW0-3018-MON; -.
DR UniPathway; UPA00629; UER00680.
DR Proteomes; UP000000432; 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 PROSITE; PS00665; DHDPS_1; 1.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..292
FT /note="N-acetylneuraminate lyase"
FT /id="PRO_0000103215"
FT ACT_SITE 163
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT BINDING 46..47
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT SITE 135
FT /note="Involved in proton transfer during cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
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
