ID A0A2U3VP88_ODORO Unreviewed; 320 AA.
AC A0A2U3VP88;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=N-acetylneuraminate lyase {ECO:0000256|ARBA:ARBA00039936};
DE EC=4.1.3.3 {ECO:0000256|ARBA:ARBA00012911};
DE AltName: Full=N-acetylneuraminate pyruvate-lyase {ECO:0000256|ARBA:ARBA00043127};
DE AltName: Full=N-acetylneuraminic acid aldolase {ECO:0000256|ARBA:ARBA00041211};
DE AltName: Full=Sialate lyase {ECO:0000256|ARBA:ARBA00042346};
DE AltName: Full=Sialate-pyruvate lyase {ECO:0000256|ARBA:ARBA00041376};
DE AltName: Full=Sialic acid aldolase {ECO:0000256|ARBA:ARBA00041560};
DE AltName: Full=Sialic acid lyase {ECO:0000256|ARBA:ARBA00042218};
GN Name=NPL {ECO:0000313|RefSeq:XP_004396925.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004396925.1};
RN [1] {ECO:0000313|RefSeq:XP_004396925.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00024547};
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}.
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DR RefSeq; XP_004396925.1; XM_004396868.2.
DR AlphaFoldDB; A0A2U3VP88; -.
DR STRING; 9708.A0A2U3VP88; -.
DR GeneID; 101383174; -.
DR KEGG; oro:101383174; -.
DR CTD; 80896; -.
DR InParanoid; A0A2U3VP88; -.
DR OrthoDB; 101328at2759; -.
DR Proteomes; UP000245340; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008747; F:N-acetylneuraminate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd00954; NAL; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR005264; NanA.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR PANTHER; PTHR12128:SF21; N-ACETYLNEURAMINATE LYASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|PIRNR:PIRNR001365, ECO:0000313|RefSeq:XP_004396925.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245340}.
FT ACT_SITE 143
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 173
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 52
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 216
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 320 AA; 35080 MW; 0CF1B30E4AA494CC CRC64;
MASPKKKLQG LVAATITPMT EHGEINFSVI GQYVDYLVEE QGVKNIFVNG TTGEGLSLSV
SERRQVAEAW VAKGRNKLDQ VVIHVGALSL KDSQELARHA AEIGADGIAV IAPFFLKPWN
KDALINFLKE VAAAAPTLPF YYYHIPALTG VKIRAEELLD GIQDKIPTFQ GLKFSDTDLL
DFGQCVDQNR QQQFAFLFGV DEQLLSALVM GATGAVGSTY NYMGKKTNQM LEAFKRKDFS
SALNHQFCIQ RFINFVLKLG FGVSQTKAIM TLVSGIPVGP PRPPLQKASR EFIDNAKAKL
KSLDFLSSTD LKDGNLESCS
//
