ID   A0A667XUW4_9TELE        Unreviewed;       307 AA.
AC   A0A667XUW4;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=N-acetylneuraminate lyase {ECO:0000256|ARBA:ARBA00012911};
DE            EC=4.1.3.3 {ECO:0000256|ARBA:ARBA00012911};
GN   Name=npl {ECO:0000313|Ensembl:ENSMMDP00005013026.1};
OS   Myripristis murdjan (pinecone soldierfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Holocentriformes; Holocentridae; Myripristis.
OX   NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005013026.1, ECO:0000313|Proteomes:UP000472263};
RN   [1] {ECO:0000313|Ensembl:ENSMMDP00005013026.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00024547};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC       {ECO:0000256|ARBA:ARBA00004878}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the DapA family. NanA subfamily.
CC       {ECO:0000256|ARBA:ARBA00006324}.
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DR   AlphaFoldDB; A0A667XUW4; -.
DR   Ensembl; ENSMMDT00005013398.1; ENSMMDP00005013026.1; ENSMMDG00005006824.1.
DR   GeneTree; ENSGT00530000063604; -.
DR   InParanoid; A0A667XUW4; -.
DR   OrthoDB; 101328at2759; -.
DR   Proteomes; UP000472263; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Lyase {ECO:0000256|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472263}.
FT   ACT_SITE        144
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        174
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         53
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT   BINDING         216
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   307 AA;  33384 MW;  959862AC10FF044D CRC64;
     MDPAVDRKVS GIVAATFTPF NPDGHINPAV IGPYVDYLTK KQGVTNVFVN GTTGESVSLS
     MEERKVLAEV WCREGKGKLD QLIVHVGCMS LKDTQELARH AEEIGADGIA VISPSFFKPS
     TADALREYLK QVAKVAPTLP FYYYHIPAMT GINVNARDVV EGIEQLIPSF RGLKFSGTDL
     MDFGQCVRLS QPNWSLLYGV DEQLLAGLAM GAEGAVGSTF NYMGCHTKQL ITAFKAGDLS
     QARAIEFKVQ ELLCFAIKKG FNLGVNKQLM IEVSGLSLGP PRLPLLQCPA DNSQAIAKKY
     HSLFPDP
//