ID   NPLB_XENLA              Reviewed;         266 AA.
AC   Q5XGL8;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=N-acetylneuraminate lyase B;
DE            Short=NALase B;
DE            EC=4.1.3.3;
DE   AltName: Full=N-acetylneuraminate pyruvate-lyase B;
DE   AltName: Full=N-acetylneuraminic acid aldolase B;
DE   AltName: Full=Sialate lyase B;
DE   AltName: Full=Sialate-pyruvate lyase B;
DE   AltName: Full=Sialic acid aldolase B;
DE   AltName: Full=Sialic acid lyase B;
GN   Name=npl-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-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 (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DapA family. NanA subfamily. {ECO:0000305}.
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DR   EMBL; BC084419; AAH84419.1; -; mRNA.
DR   RefSeq; NP_001088349.1; NM_001094880.1.
DR   AlphaFoldDB; Q5XGL8; -.
DR   SMR; Q5XGL8; -.
DR   DNASU; 495191; -.
DR   GeneID; 495191; -.
DR   CTD; 495191; -.
DR   Xenbase; XB-GENE-6254295; npl.S.
DR   UniPathway; UPA00629; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 495191; Expressed in kidney and 18 other tissues.
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; IEA:UniProtKB-UniPathway.
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   SMART; SM01130; DHDPS; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cytoplasm; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..266
FT                   /note="N-acetylneuraminate lyase B"
FT                   /id="PRO_0000273360"
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   266 AA;  29313 MW;  9BF23C69FD7EF7D1 CRC64;
     MAFTGKRLKG LIAATFTPMT PNSDINLLVI EQYVDYLVQK QHIRNIFVNG TTGEGMSLSI
     CERKRLTEEW VKHARGKMDN VIVHVGCLGL SDSKDLAAHA ASCGADAISA VCPSFLKPAN
     LDALVLYLKD VASAAPSLPF YYYHIPKLTG ITYQIYELLG KVKENIPSFR GVKFSDVNLM
     DFSLCVSEYK EFDCLYGVDE QLLGALAFGA HGAVGSTYNY LGNKNGDMLE AFEAGNLQKA
     RKIQCSLQEF LYFVFDMAHF SGSKAN