ID   NPLA_XENLA              Reviewed;         305 AA.
AC   Q3B8E8;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=N-acetylneuraminate lyase A;
DE            Short=NALase A;
DE            EC=4.1.3.3;
DE   AltName: Full=N-acetylneuraminate pyruvate-lyase A;
DE   AltName: Full=N-acetylneuraminic acid aldolase A;
DE   AltName: Full=Sialate lyase A;
DE   AltName: Full=Sialate-pyruvate lyase A;
DE   AltName: Full=Sialic acid aldolase A;
DE   AltName: Full=Sialic acid lyase A;
GN   Name=npl-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the cleavage of N-acetylneuraminic acid (sialic
CC       acid) to form pyruvate and N-acetylmannosamine via a Schiff base
CC       intermediate. It prevents sialic acids from being recycled and
CC       returning to the cell surface. Involved in the N-glycolylneuraminic
CC       acid (Neu5Gc) degradation pathway (By similarity). {ECO:0000250}.
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;
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DapA family. NanA subfamily. {ECO:0000305}.
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; BC106506; AAI06507.1; -; mRNA.
DR   RefSeq; NP_001089763.1; NM_001096294.1.
DR   AlphaFoldDB; Q3B8E8; -.
DR   SMR; Q3B8E8; -.
DR   MaxQB; Q3B8E8; -.
DR   PRIDE; Q3B8E8; -.
DR   DNASU; 734827; -.
DR   GeneID; 734827; -.
DR   KEGG; xla:734827; -.
DR   CTD; 734827; -.
DR   Xenbase; XB-GENE-978369; npl.L.
DR   OrthoDB; 1238597at2759; -.
DR   UniPathway; UPA00629; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 734827; Expressed in spleen and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008747; F:N-acetylneuraminate lyase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   PANTHER; PTHR12128; PTHR12128; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cytoplasm; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..305
FT                   /note="N-acetylneuraminate lyase A"
FT                   /id="PRO_0000273359"
FT   ACT_SITE        173
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         51..52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            143
FT                   /note="Involved in proton transfer during cleavage"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  33725 MW;  293A04CCC286B3C8 CRC64;
     MAFAGKRLKG LIAATFTPMT SNSDINLAAI EQYVDYLVQK QHIRNIFVNG TTGEGMSLSV
     HERKSLAEEW VKQARGKMND VIVHVGCLSL SDSKDLAAHA ASCGADAIST VCPSFLKPSS
     LDALVLYLKE VASAAPNLPF YYYHIPRLTG ITYQIYELLG KVKKNIPSFR GVKFSDVNLM
     DFSLCVSEYK EFDCLYGVDE QLLGALAFGA HGAVGSTYNY LGKKNGDMMA AFEEGNLQKA
     RKIQCSLQEF LIFVFDMGWG LAEFKDIMSQ VSGIPLGPSR LPLYSSMKFD HHDNIKTKML
     KLDLI