ID A0AAD4PP68_9MUSC Unreviewed; 361 AA.
AC A0AAD4PP68;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 08-OCT-2025, entry version 7.
DE RecName: Full=N-acetylneuraminate lyase {ECO:0000256|ARBA:ARBA00012911};
DE EC=4.1.3.3 {ECO:0000256|ARBA:ARBA00012911};
GN ORFNames=KR093_002231 {ECO:0000313|EMBL:KAH8385458.1};
OS Drosophila rubida.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30044 {ECO:0000313|EMBL:KAH8385458.1, ECO:0000313|Proteomes:UP001200034};
RN [1] {ECO:0000313|EMBL:KAH8385458.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BGI-SZ-2011g {ECO:0000313|EMBL:KAH8385458.1};
RX PubMed=34839580;
RA Li F., Rane R.V., Luria V., Xiong Z., Chen J., Li Z., Catullo R.A.,
RA Griffin P.C., Schiffer M., Pearce S., Lee S.F., McElroy K., Stocker A.,
RA Shirriffs J., Cockerell F., Coppin C., Sgro C.M., Karger A., Cain J.W.,
RA Weber J.A., Santpere G., Kirschner M.W., Hoffmann A.A., Oakeshott J.G.,
RA Zhang G.;
RT "Phylogenomic analyses of the genus Drosophila reveals genomic signals of
RT climate adaptation.";
RL Mol. Ecol. Resour. 0:0-0(2021).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAH8385458.1}.
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DR EMBL; JAJJHW010000454; KAH8385458.1; -; Genomic_DNA.
DR Proteomes; UP001200034; Unassembled WGS sequence.
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:UP001200034};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..13
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 361 AA; 40583 MW; 8C97AF7D2484ABE8 CRC64;
MAWFRRDTDK SVESTKTPIL QETPDDGKTH VCNAYALLNC TFTAPVVKHS REEVRHQDER
PSLPTLSKDA ELITPKFKGL LAPVFTCFTD DDRRSLDVRP INRYAEWLKH QLIAGVLVNG
VVGEGPIMRV RERKANAEYW QRAAVRHNLL ILVQVGGAPL PDVLSLAAHA EELHVSGVVV
LPDLFYRPRT VDQLVGYCKH VASRCRTRPL LYYHMPSMTG VDLDMVEFCT KAERAIPNFM
GLHYSSGDLE MGQRCLRLGR VILLASPSLL ASGLMSGFSC CSLAVINIRP DLVRRICDAF
DGNELQHVRD YQRELNQLID IHTQLGGSLE KWVVCMKSWL NKEFSSRASG PFIAGPARTV
F
//
