ID   NPL_DANRE               Reviewed;         307 AA.
AC   Q6NYR8;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 103.
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}; ORFNames=zgc:76930;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (FEB-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; BC066486; AAH66486.1; -; mRNA.
DR   AlphaFoldDB; Q6NYR8; -.
DR   SMR; Q6NYR8; -.
DR   STRING; 7955.ENSDARP00000148018; -.
DR   PaxDb; 7955-ENSDARP00000027094; -.
DR   AGR; ZFIN:ZDB-GENE-030131-926; -.
DR   ZFIN; ZDB-GENE-030131-926; npl.
DR   eggNOG; ENOG502QQA3; Eukaryota.
DR   InParanoid; Q6NYR8; -.
DR   PhylomeDB; Q6NYR8; -.
DR   Reactome; R-DRE-4085001; Sialic acid metabolism.
DR   UniPathway; UPA00629; -.
DR   PRO; PR:Q6NYR8; -.
DR   Proteomes; UP000000437; Genome assembly.
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; IMP:ZFIN.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR020624; Schiff_base-form_aldolases_CS.
DR   PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR   PANTHER; PTHR12128:SF21; N-ACETYLNEURAMINATE LYASE; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00665; DHDPS_1; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cytoplasm; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..307
FT                   /note="N-acetylneuraminate lyase"
FT                   /id="PRO_0000273358"
FT   ACT_SITE        143
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   ACT_SITE        173
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         51
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         52
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         175
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         199
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         201
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         202
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         218
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
SQ   SEQUENCE   307 AA;  33221 MW;  9E2222D36024CE5F CRC64;
     MSQRVKKLTG LVAATFTPLT AEGEINLSVI AAYVDYLIEK QNVKSVFVNG TTGEGCSLTV
     DERKHLAAAW CQHGKGKLEQ LIVHVGCMSI KDSQELARHA ASIGADGISV ISPSYFKPIN
     ADALRLFIKE VSASAPDLPM YYYHLPGMTG VALEAADVLN GIEREIPSFQ GVKYSGTDLR
     DLGQCVCYSQ SRDWSVLYGV DEQLLGALVL GVHGAVGSTY NYLGHIVNQM LSAFNNGNHT
     QTRDLQFGFM EVITFARTLG FDVSVNKQVM SEVSGLPMGP PRLPLLPCPV SKAQAIAQKI
     HNFTQGL
//