NPL_XENTR
ID NPL_XENTR Reviewed; 305 AA.
AC Q5M905;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
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};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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 EMBL; BC087756; AAH87756.1; -; mRNA.
DR RefSeq; NP_001011207.1; NM_001011207.1.
DR RefSeq; XP_012816446.1; XM_012960992.2.
DR AlphaFoldDB; Q5M905; -.
DR SMR; Q5M905; -.
DR STRING; 8364.ENSXETP00000032307; -.
DR DNASU; 496638; -.
DR GeneID; 496638; -.
DR KEGG; xtr:496638; -.
DR CTD; 80896; -.
DR Xenbase; XB-GENE-978364; npl.
DR InParanoid; Q5M905; -.
DR OrthoDB; 1238597at2759; -.
DR Reactome; R-XTR-4085001; Sialic acid metabolism.
DR UniPathway; UPA00629; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000012514; Expressed in mesonephros and 17 other tissues.
DR ExpressionAtlas; Q5M905; baseline.
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; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cytoplasm; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..305
FT /note="N-acetylneuraminate lyase"
FT /id="PRO_0000273361"
FT ACT_SITE 173
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 51..52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 143
FT /note="Involved in proton transfer during cleavage"
FT /evidence="ECO:0000250"
SQ SEQUENCE 305 AA; 33777 MW; 6E8F51233FD013C8 CRC64;
MEFAGKRLKG LIAATFTPMT SNSDINLPVI KQYVDYLVQK QHVRNIFVNG TTGEGMSLSV
QERKCLAEEW VKQARGKMDN VIIHVGCLSL SDSKDLAAHA ASCGADAISI VCPSFLKPSS
LDALVLYMKE VAFAAPSLPF YYYHIPRLTG TTYQICELLR KAKENIPSFR GVKFTDVNLM
DFGLCVSQYK EFDCLYGVDE QLLGALAFGA HGAVGSTYNY LGKKNGDMMA AFEGGNLQEA
RKIQCSLQEF LLFVFDMGWG LPEFKDIMSQ ISGIPLGPPR LPLYSSVKSD HHDSIRTKML
KLDLI