ID A0A7E5WQV0_TRINI Unreviewed; 366 AA.
AC A0A7E5WQV0;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 08-OCT-2025, entry version 20.
DE RecName: Full=N-acetylneuraminate lyase {ECO:0000256|ARBA:ARBA00012911};
DE EC=4.1.3.3 {ECO:0000256|ARBA:ARBA00012911};
GN Name=LOC113504859 {ECO:0000313|RefSeq:XP_026743140.1};
OS Trichoplusia ni (Cabbage looper).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Plusiinae; Trichoplusia.
OX NCBI_TaxID=7111 {ECO:0000313|Proteomes:UP000322000, ECO:0000313|RefSeq:XP_026743140.1};
RN [1] {ECO:0000313|RefSeq:XP_026743140.1}
RP IDENTIFICATION.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_026743140.1; XM_026887339.1.
DR AlphaFoldDB; A0A7E5WQV0; -.
DR GeneID; 113504859; -.
DR KEGG; tnl:113504859; -.
DR InParanoid; A0A7E5WQV0; -.
DR OrthoDB; 191315at2759; -.
DR Proteomes; UP000322000; Chromosome 23.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000322000};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..366
FT /note="N-acetylneuraminate lyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028925298"
FT REGION 326..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 366 AA; 40464 MW; 3DC4B27C853062B0 CRC64;
MALGILTLLF AIILAILPLG EAKDVQLKVK GIVASVFTPI DDYGYVNFNV IPQYAQSLKD
RGINGVLVGG YNGEGTKFSI WDRRQLLSTW IEAATPLGLF VLFQVGGIPL PDAQDLASFA
EQIGVSAILI YPDCIYKPKN PKELVYYVGI IASSAPNTPI LYYHIPQVTG VNVDMVKFFD
LASDQIDNFK GLKVETFDTA LKLRGRMEGD QRVFISNSVY LGPAALAGFD SFILSDATVF
PRLVDLIVRY GKSGDRRRVN SFSQRLIDLN EVISAQGNNL AALKATMSLV TDIDVGRIKD
PTLQLTAEQE NNLERRLKDE GIKVKQRQNN NQETYGRKRI YPPRPPVIYY DEAGRGSGPV
AEPVEN
//
