NPL_PIG
ID NPL_PIG Reviewed; 319 AA.
AC Q9BEC7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=N-acetylneuraminate lyase {ECO:0000250|UniProtKB:Q9BXD5};
DE Short=NALase;
DE EC=4.1.3.3 {ECO:0000269|PubMed:11737202};
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC TISSUE=Kidney;
RX PubMed=11737202; DOI=10.1046/j.0014-2956.2001.02598.x;
RA Traving C., Bruse P., Waechter A., Schauer R.;
RT "The sialate-pyruvate lyase from pig kidney. Elucidation of the primary
RT structure and expression of recombinant enzyme activity.";
RL Eur. J. Biochem. 268:6473-6486(2001).
RN [2]
RP PROTEIN SEQUENCE OF 103-108; 122-127; 153-158; 166-171 AND 227-232,
RP SUBUNIT, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Kidney;
RX PubMed=10737328; DOI=10.1023/a:1007030627948;
RA Sommer U., Traving C., Schauer R.;
RT "The sialate pyruvate-lyase from pig kidney: purification, properties and
RT genetic relationship.";
RL Glycoconj. J. 16:425-435(1999).
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:0000269|PubMed:11737202}.
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:0000269|PubMed:11737202};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=2.3 umol/min/mg enzyme {ECO:0000269|PubMed:10737328};
CC pH dependence:
CC Optimum pH is 7.6-8.0. {ECO:0000269|PubMed:10737328};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC {ECO:0000305|PubMed:11737202}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:10737328}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10737328}.
CC -!- SIMILARITY: Belongs to the DapA family. NanA subfamily. {ECO:0000305}.
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DR EMBL; AJ271330; CAC27797.1; -; mRNA.
DR RefSeq; NP_999236.1; NM_214071.1.
DR RefSeq; XP_013846578.1; XM_013991124.1.
DR AlphaFoldDB; Q9BEC7; -.
DR SMR; Q9BEC7; -.
DR STRING; 9823.ENSSSCP00000027926; -.
DR PaxDb; Q9BEC7; -.
DR PeptideAtlas; Q9BEC7; -.
DR Ensembl; ENSSSCT00005061202; ENSSSCP00005037835; ENSSSCG00005038128.
DR Ensembl; ENSSSCT00060017262; ENSSSCP00060006864; ENSSSCG00060013130.
DR Ensembl; ENSSSCT00070025339; ENSSSCP00070020996; ENSSSCG00070012924.
DR GeneID; 397141; -.
DR KEGG; ssc:397141; -.
DR CTD; 80896; -.
DR eggNOG; ENOG502QQA3; Eukaryota.
DR HOGENOM; CLU_049343_6_1_1; -.
DR InParanoid; Q9BEC7; -.
DR OMA; LYEYNQC; -.
DR OrthoDB; 1238597at2759; -.
DR TreeFam; TF353639; -.
DR BRENDA; 4.1.3.3; 6170.
DR Reactome; R-SSC-4085001; Sialic acid metabolism.
DR UniPathway; UPA00629; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 9.
DR Genevisible; Q9BEC7; SS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008747; F:N-acetylneuraminate lyase activity; IDA:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IDA:UniProtKB.
DR CDD; cd00954; NAL; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR005264; NanA.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Direct protein sequencing; Lyase;
KW Reference proteome; Schiff base.
FT CHAIN 1..319
FT /note="N-acetylneuraminate lyase"
FT /id="PRO_0000273354"
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 319 AA; 35062 MW; C89894E9F68674A7 CRC64;
MASPKKKLQG LVAATITPMT EHGEINFSVI GQYVDYLVEV QGVKNIFVNG TTGEGLSLSI
SERCQVAEEW VTKGRNKLDQ IVIHVGALSL KESQELAQHA AKIGADGIAV IAPFFLKPWN
KDNLINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GIQDKIPTFQ GLKFSDTDLL
DFGQCVDQNH QRQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGRKTNQM LEAFERKDFS
SALNHQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDNAKAKL
KSLDVLSFTD LKDGNLEAC
