ID A0A369Y1Y1_9FUSO Unreviewed; 292 AA.
AC A0A369Y1Y1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=N-acetylneuraminate lyase {ECO:0000256|ARBA:ARBA00012911, ECO:0000256|HAMAP-Rule:MF_01237};
DE Short=NAL {ECO:0000256|HAMAP-Rule:MF_01237};
DE Short=Neu5Ac lyase {ECO:0000256|HAMAP-Rule:MF_01237};
DE EC=4.1.3.3 {ECO:0000256|ARBA:ARBA00012911, ECO:0000256|HAMAP-Rule:MF_01237};
DE AltName: Full=N-acetylneuraminate pyruvate-lyase {ECO:0000256|HAMAP-Rule:MF_01237};
DE AltName: Full=N-acetylneuraminic acid aldolase {ECO:0000256|HAMAP-Rule:MF_01237};
DE AltName: Full=Sialate lyase {ECO:0000256|HAMAP-Rule:MF_01237};
DE AltName: Full=Sialic acid aldolase {ECO:0000256|HAMAP-Rule:MF_01237};
DE AltName: Full=Sialic acid lyase {ECO:0000256|HAMAP-Rule:MF_01237};
GN Name=nanA {ECO:0000256|HAMAP-Rule:MF_01237};
GN ORFNames=DV867_04700 {ECO:0000313|EMBL:RDE63681.1};
OS Psychrilyobacter sp. S5.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Psychrilyobacter.
OX NCBI_TaxID=2283384 {ECO:0000313|EMBL:RDE63681.1, ECO:0000313|Proteomes:UP000253914};
RN [1] {ECO:0000313|EMBL:RDE63681.1, ECO:0000313|Proteomes:UP000253914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S5 {ECO:0000313|EMBL:RDE63681.1,
RC ECO:0000313|Proteomes:UP000253914};
RA Yadav S., Villanueva L., Damste J.S.S.;
RT "Draft genome sequence of Psychrilyobacter sp. strain S5.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible aldol cleavage of N-acetylneuraminic
CC acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine
CC (ManNAc) via a Schiff base intermediate. {ECO:0000256|HAMAP-
CC Rule:MF_01237}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01237};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 1/5.
CC {ECO:0000256|HAMAP-Rule:MF_01237}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|HAMAP-Rule:MF_01237}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01237}.
CC -!- SIMILARITY: Belongs to the DapA family. NanA subfamily.
CC {ECO:0000256|ARBA:ARBA00006324, ECO:0000256|HAMAP-Rule:MF_01237}.
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:RDE63681.1}.
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DR EMBL; QQOU01000006; RDE63681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369Y1Y1; -.
DR UniPathway; UPA00629; UER00680.
DR Proteomes; UP000253914; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008747; F:N-acetylneuraminate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00954; NAL; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01237; N_acetylneuram_lyase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR005264; NanA.
DR InterPro; IPR020624; Schiff_base-form_aldolases_CS.
DR NCBIfam; TIGR00683; nanA; 1.
DR PANTHER; PTHR42849; N-ACETYLNEURAMINATE LYASE; 1.
DR PANTHER; PTHR42849:SF1; 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.
DR PROSITE; PS00665; DHDPS_1; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01237};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01237};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01237};
KW Reference proteome {ECO:0000313|Proteomes:UP000253914};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_01237}.
FT ACT_SITE 137
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 165
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01237,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 48..49
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01237"
FT BINDING 49
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 206
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT SITE 137
FT /note="Involved in proton transfer during cleavage"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01237"
SQ SEQUENCE 292 AA; 32680 MW; 8AF8FE2AAFE97D14 CRC64;
MKTKLGGIYS ALMVAYDEDG NINENGTREI IRHNIHKMEV DGLYVGGSTG ENFMISTEEK
KRILYIAMDE GRGQVKLMAQ VGSVNLKEAV ELGKYATDLG YDALSAVTPF YYKFDFEEIK
NYYNTIIEAT GNYMVIYFIP SLTGVNLSLD QFGELFENEK IIGVKFSHGD FFLLERLRKA
YPDHLIYAGL DEMMLSAAVL HVDGGIGSTY NVNGIRAKQI YTLAKGGKIK EARELQHTTN
DLIEGILANG LYQTIKEIMK TQGVDAGYCR QPTKRLSEEG IIAAKELAEK YL
//
