ID   NPL_BOVIN               Reviewed;         320 AA.
AC   Q29RY9;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) 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   -!- SIMILARITY: Belongs to the DapA family. NanA subfamily. {ECO:0000305}.
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DR   EMBL; BC113332; AAI13333.1; -; mRNA.
DR   RefSeq; NP_001039443.1; NM_001045978.1.
DR   RefSeq; XP_015330739.1; XM_015475253.1.
DR   AlphaFoldDB; Q29RY9; -.
DR   SMR; Q29RY9; -.
DR   STRING; 9913.ENSBTAP00000002925; -.
DR   PaxDb; Q29RY9; -.
DR   PRIDE; Q29RY9; -.
DR   Ensembl; ENSBTAT00000002925; ENSBTAP00000002925; ENSBTAG00000002266.
DR   GeneID; 507597; -.
DR   KEGG; bta:507597; -.
DR   CTD; 80896; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002266; -.
DR   VGNC; VGNC:32205; NPL.
DR   eggNOG; ENOG502QQA3; Eukaryota.
DR   GeneTree; ENSGT00530000063604; -.
DR   HOGENOM; CLU_049343_6_1_1; -.
DR   InParanoid; Q29RY9; -.
DR   OMA; VVPPVCT; -.
DR   OrthoDB; 1238597at2759; -.
DR   TreeFam; TF353639; -.
DR   UniPathway; UPA00629; -.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000002266; Expressed in metanephros cortex and 85 other tissues.
DR   ExpressionAtlas; Q29RY9; baseline and differential.
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   Carbohydrate metabolism; Cytoplasm; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..320
FT                   /note="N-acetylneuraminate lyase"
FT                   /id="PRO_0000273351"
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   320 AA;  35166 MW;  D91F221361E56BA6 CRC64;
     MASPKKKLQG LVAATITPMT EHGEINFSVI GRYVDYLVEE QGVKNVFVNG TTGEGLSLSI
     SERCQVAEEW VTKGKNKLDQ IVIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWN
     KDVLINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GIQDKIPSFQ GLKFSDTDLL
     DFGQCVDQNR QRQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTKQM LEAFERKDFS
     SALNHQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDNAEAKL
     KSLDFLSCTD LKDGNMEACS