ID   NPL_RAT                 Reviewed;         320 AA.
AC   Q66H59;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=N-acetylneuraminate lyase {ECO:0000305};
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:0000312|RGD:1549702};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; BC082004; AAH82004.1; -; mRNA.
DR   RefSeq; NP_001014006.1; NM_001013984.1.
DR   AlphaFoldDB; Q66H59; -.
DR   SMR; Q66H59; -.
DR   STRING; 10116.ENSRNOP00000003713; -.
DR   iPTMnet; Q66H59; -.
DR   PhosphoSitePlus; Q66H59; -.
DR   PaxDb; Q66H59; -.
DR   Ensembl; ENSRNOT00000109291; ENSRNOP00000097337; ENSRNOG00000002775.
DR   GeneID; 304860; -.
DR   KEGG; rno:304860; -.
DR   UCSC; RGD:1549702; rat.
DR   CTD; 80896; -.
DR   RGD; 1549702; Npl.
DR   eggNOG; ENOG502QQA3; Eukaryota.
DR   GeneTree; ENSGT00530000063604; -.
DR   HOGENOM; CLU_049343_6_1_1; -.
DR   InParanoid; Q66H59; -.
DR   OMA; LPPMRYK; -.
DR   OrthoDB; 1238597at2759; -.
DR   PhylomeDB; Q66H59; -.
DR   TreeFam; TF353639; -.
DR   Reactome; R-RNO-4085001; Sialic acid metabolism.
DR   UniPathway; UPA00629; -.
DR   PRO; PR:Q66H59; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000002775; Expressed in adult mammalian kidney and 18 other tissues.
DR   Genevisible; Q66H59; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
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   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..320
FT                   /note="N-acetylneuraminate lyase"
FT                   /id="PRO_0000273356"
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;  35115 MW;  3674F314288D8B89 CRC64;
     MAFPKKKLQG LVAATITPMT ENGEINFPVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSI
     SERRQVAEEW VRQGKNKLDQ VVIHVGALNL KESQELAQHA AEIGADGIAV IAPFFFKSQN
     KDALISFLRE VAAAAPALPF YYYHIPSLTG VKIRAEELLD GIQDKIPSFQ GLKFSDTDLL
     DFGQCVDQNH QRQFALLFGV DEQLLSALVL GATGAVGSTY NYLGKKTNQM LEAFEQKDLA
     SALSYQFRIQ RFINYVIKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKATQ EFTANAEAKL
     KSLNFLSFPG LKDGNMEACS