ID A0A2Y9Q0B9_DELLE Unreviewed; 367 AA.
AC A0A2Y9Q0B9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 08-OCT-2025, entry version 27.
DE RecName: Full=N-acetylneuraminate lyase {ECO:0000256|ARBA:ARBA00039936};
DE EC=4.1.3.3 {ECO:0000256|ARBA:ARBA00012911};
DE AltName: Full=N-acetylneuraminate pyruvate-lyase {ECO:0000256|ARBA:ARBA00043127};
DE AltName: Full=N-acetylneuraminic acid aldolase {ECO:0000256|ARBA:ARBA00041211};
DE AltName: Full=Sialate lyase {ECO:0000256|ARBA:ARBA00042346};
DE AltName: Full=Sialate-pyruvate lyase {ECO:0000256|ARBA:ARBA00041376};
DE AltName: Full=Sialic acid aldolase {ECO:0000256|ARBA:ARBA00041560};
DE AltName: Full=Sialic acid lyase {ECO:0000256|ARBA:ARBA00042218};
GN Name=NPL {ECO:0000313|RefSeq:XP_022449017.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022449017.1};
RN [1] {ECO:0000313|RefSeq:XP_022449017.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022449017.1};
RG RefSeq;
RL Submitted (APR-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aceneuramate = aldehydo-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:ARBA00044906};
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 RefSeq; XP_022449017.1; XM_022593309.1.
DR AlphaFoldDB; A0A2Y9Q0B9; -.
DR FunCoup; A0A2Y9Q0B9; 104.
DR STRING; 9749.A0A2Y9Q0B9; -.
DR GeneID; 111184633; -.
DR KEGG; dle:111184633; -.
DR CTD; 80896; -.
DR InParanoid; A0A2Y9Q0B9; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008747; F:N-acetylneuraminate lyase activity; IEA:UniProtKB-ARBA.
DR FunFam; 3.20.20.70:FF:000133; N-acetylneuraminate pyruvate lyase; 1.
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 PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|RefSeq:XP_022449017.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ SEQUENCE 367 AA; 39755 MW; 1CC409D9ADAE4B91 CRC64;
MFIQAPAFGG PLKNRELHLC LTLWERGVAR GGATAPRPRG GAGTWCAAPA IKSAVGSAAR
SGGGGRAASG EINFSVIGRY VDYLVEEQGV KNIFVNGTTG EGLSLSISER CRVAEEWVTE
GRNKLDQIVI HVGALSLKES QELAQHAAKI GADGIAVIAP FFLKPWNKDV LINFLKEVAA
AAPALPFYYY HIPALTGVKI RAEELLDGIQ DKIPTFQGLK FSDTDLLDFG QCVDQNRQQQ
FAFLFGVDEQ LLSALVMGAT GAVGSTYNYL GKKTNQMLEA FERKDFSSAL NHQFCIQRFI
NFVVKLGFGV SQTKAIMTLV SGIPMGPPRL PLQKASREFT DNAEAKLKSL DFLSFTDLKD
GNLEACS
//
