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NPL_XENTR
ID   NPL_XENTR               Reviewed;         305 AA.
AC   Q5M905;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
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   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-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   -!- SIMILARITY: Belongs to the DapA family. NanA subfamily. {ECO:0000305}.
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DR   EMBL; BC087756; AAH87756.1; -; mRNA.
DR   RefSeq; NP_001011207.1; NM_001011207.1.
DR   RefSeq; XP_012816446.1; XM_012960992.2.
DR   AlphaFoldDB; Q5M905; -.
DR   SMR; Q5M905; -.
DR   STRING; 8364.ENSXETP00000032307; -.
DR   DNASU; 496638; -.
DR   GeneID; 496638; -.
DR   KEGG; xtr:496638; -.
DR   CTD; 80896; -.
DR   Xenbase; XB-GENE-978364; npl.
DR   InParanoid; Q5M905; -.
DR   OrthoDB; 1238597at2759; -.
DR   Reactome; R-XTR-4085001; Sialic acid metabolism.
DR   UniPathway; UPA00629; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000012514; Expressed in mesonephros and 17 other tissues.
DR   ExpressionAtlas; Q5M905; baseline.
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   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"
FT                   /id="PRO_0000273361"
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;  33777 MW;  6E8F51233FD013C8 CRC64;
     MEFAGKRLKG LIAATFTPMT SNSDINLPVI KQYVDYLVQK QHVRNIFVNG TTGEGMSLSV
     QERKCLAEEW VKQARGKMDN VIIHVGCLSL SDSKDLAAHA ASCGADAISI VCPSFLKPSS
     LDALVLYMKE VAFAAPSLPF YYYHIPRLTG TTYQICELLR KAKENIPSFR GVKFTDVNLM
     DFGLCVSQYK EFDCLYGVDE QLLGALAFGA HGAVGSTYNY LGKKNGDMMA AFEGGNLQEA
     RKIQCSLQEF LLFVFDMGWG LPEFKDIMSQ ISGIPLGPPR LPLYSSVKSD HHDSIRTKML
     KLDLI
 
 
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