ID J5H499_9FIRM Unreviewed; 323 AA.
AC J5H499;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 ECO:0000313|EMBL:EJP25730.1};
GN ORFNames=HMPREF1142_0081 {ECO:0000313|EMBL:EJP25730.1};
OS Peptostreptococcaceae bacterium AS15.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX NCBI_TaxID=936556 {ECO:0000313|EMBL:EJP25730.1, ECO:0000313|Proteomes:UP000006605};
RN [1] {ECO:0000313|EMBL:EJP25730.1, ECO:0000313|Proteomes:UP000006605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS15 {ECO:0000313|EMBL:EJP25730.1,
RC ECO:0000313|Proteomes:UP000006605};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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:EJP25730.1}.
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; ALJM01000004; EJP25730.1; -; Genomic_DNA.
DR AlphaFoldDB; J5H499; -.
DR PATRIC; fig|936556.4.peg.300; -.
DR UniPathway; UPA00629; UER00680.
DR Proteomes; UP000006605; 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; IPR020625; Schiff_base-form_aldolases_AS.
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.
DR PROSITE; PS00666; DHDPS_2; 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:UP000006605};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_01237}.
FT ACT_SITE 167
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 195
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01237,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 78..79
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01237"
FT BINDING 79
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 236
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT SITE 167
FT /note="Involved in proton transfer during cleavage"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01237"
SQ SEQUENCE 323 AA; 36570 MW; 621D22990A924CC9 CRC64;
MGLIIFSKYD ARPCPDVSNF YGQLKEKKMG ANNELKGIYS ALLVSFNEDG SVNEKGTRQI
VRHNIDKMKV DGLYVGGSTG ENFLLSTDEK KKIFEIAKDE AKDEIKLIAQ IGSMNYYESL
ELAKFVTDLK YDAISAVTPF YYKFSFEEIK DYYNSIIDSV DNKLIIYSIP FLTGVNISVE
QFGELFENKK IIGVKFTAAD FYLLERVRNT YPDHLIYAGF DEMMLSASVL GVDGAIGSTF
NVNGPRARKI VDLVKQGKIE EAKKEQHITN DLITDVLNNG LYPTLKTILQ LQSVEGCYSR
KPMKSATEAQ KQRAKEIYEN YLK
//
