ID   NPL_PONAB               Reviewed;         320 AA.
AC   Q5RDY1; Q5RFA4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=N-acetylneuraminate lyase {ECO:0000250|UniProtKB:Q9BXD5};
DE            Short=NALase;
DE            EC=4.1.3.3 {ECO:0000250|UniProtKB:Q9BXD5};
DE   AltName: Full=N-acetylneuraminate pyruvate-lyase;
DE   AltName: Full=N-acetylneuraminic acid aldolase;
DE   AltName: Full=Sialate lyase;
DE   AltName: Full=Sialate-pyruvate lyase;
DE   AltName: Full=Sialic acid aldolase;
DE   AltName: Full=Sialic acid lyase;
GN   Name=NPL {ECO:0000250|UniProtKB:Q9BXD5};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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. {ECO:0000250|UniProtKB:Q9BXD5}.
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         Evidence={ECO:0000250|UniProtKB:Q9BXD5};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC       {ECO:0000250|UniProtKB:Q9BXD5}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9BXD5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5RDY1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5RDY1-2; Sequence=VSP_022523;
CC   -!- SIMILARITY: Belongs to the DapA family. NanA subfamily. {ECO:0000305}.
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DR   EMBL; CR857257; CAH89553.1; -; mRNA.
DR   EMBL; CR857761; CAH90026.1; -; mRNA.
DR   RefSeq; NP_001124676.1; NM_001131204.2.
DR   AlphaFoldDB; Q5RDY1; -.
DR   SMR; Q5RDY1; -.
DR   STRING; 9601.ENSPPYP00000000491; -.
DR   Ensembl; ENSPPYT00000055971; ENSPPYP00000034792; ENSPPYG00000000432. [Q5RDY1-2]
DR   GeneID; 100171523; -.
DR   KEGG; pon:100171523; -.
DR   CTD; 80896; -.
DR   eggNOG; ENOG502QQA3; Eukaryota.
DR   GeneTree; ENSGT00530000063604; -.
DR   InParanoid; Q5RDY1; -.
DR   UniPathway; UPA00629; -.
DR   Proteomes; UP000001595; Chromosome 1.
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; ISS:UniProtKB.
DR   CDD; cd00954; NAL; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR005264; NanA.
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   Alternative splicing; Carbohydrate metabolism; Cytoplasm; Lyase;
KW   Reference proteome; Schiff base.
FT   CHAIN           1..320
FT                   /note="N-acetylneuraminate lyase"
FT                   /id="PRO_0000273355"
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"
FT   VAR_SEQ         1..77
FT                   /note="MAFPKKKLQGLVAATITPMTEDGEINFSVIGQYVDYLVKEQGVKNIFVNGTT
FT                   GEGLSLSISERRQVAEEWVTKGKDK -> MSRAPGILAAWRRAPSLSVQKGSQTARHTC
FT                   HPEVPLGNCFLPVYKANPLTVTRPWAER (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_022523"
FT   CONFLICT        117
FT                   /note="K -> N (in Ref. 1; CAH89553)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   320 AA;  35196 MW;  1C7331BA522A8363 CRC64;
     MAFPKKKLQG LVAATITPMT EDGEINFSVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSI
     SERRQVAEEW VTKGKDKLDQ VIIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWT
     KDILINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GILDKIPTFQ GLKFSDTDLL
     DFGQCVDQNR QQQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFERKDFS
     LALNYQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGISMGP PRLPLQKASR EFTDSAEAKL
     KSLDFLSFTD LKDGNLEAGS