ID   NPL_CHICK               Reviewed;         308 AA.
AC   Q5ZKD4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=RCJMB04_11j23;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720150; CAG31809.1; -; mRNA.
DR   RefSeq; NP_001026731.1; NM_001031560.2.
DR   AlphaFoldDB; Q5ZKD4; -.
DR   SMR; Q5ZKD4; -.
DR   STRING; 9031.ENSGALP00000007334; -.
DR   PaxDb; 9031-ENSGALP00000007334; -.
DR   GeneID; 429074; -.
DR   KEGG; gga:429074; -.
DR   CTD; 80896; -.
DR   VEuPathDB; HostDB:geneid_429074; -.
DR   eggNOG; ENOG502QQA3; Eukaryota.
DR   InParanoid; Q5ZKD4; -.
DR   PhylomeDB; Q5ZKD4; -.
DR   UniPathway; UPA00629; -.
DR   PRO; PR:Q5ZKD4; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
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; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
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.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cytoplasm; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..308
FT                   /note="N-acetylneuraminate lyase"
FT                   /id="PRO_0000273357"
FT   ACT_SITE        142
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   ACT_SITE        172
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         50
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
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         174
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         198
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         200
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         217
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
SQ   SEQUENCE   308 AA;  33646 MW;  FBA9375250252359 CRC64;
     MTPRKKLEGL VAATVTPMTP DGRINLSVIH QYVDYLVSEQ NVKNIFVNGT TGEGLSLSIQ
     ERKQLAEEWM CQGKGKLDHV IIHVGALSLL ESQELARHAA AIGASGIAVI APSFFKPTNK
     DELLGFLQKV ASEAPTVPFY YYHIPAMTGV KIRVEELLDG IREQIPTFQG VKFSDTDLLD
     LAQCINKKER EQFVFLYGVD EQLLSALAIG ANGAVGSTYN YLGRKTNLML QAFAKPDLAL
     ARKYQFLTGE FLSFVIKLGF GVAQTKAVMT SISGIPMGPP RLPLVGASEE FIAKAKAKLE
     SIVWPDGD
//