ID S6EXR9_9CLOT Unreviewed; 289 AA.
AC S6EXR9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=CCH01_06370 {ECO:0000313|EMBL:SLK14344.1};
OS Clostridium chauvoei JF4335.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1351755 {ECO:0000313|EMBL:SLK14344.1, ECO:0000313|Proteomes:UP000190476};
RN [1] {ECO:0000313|Proteomes:UP000190476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Falquet L., Falquet L.;
RL Submitted (MAR-2017) 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}.
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DR EMBL; LT799839; SLK14344.1; -; Genomic_DNA.
DR RefSeq; WP_021874988.1; NZ_LT799839.1.
DR AlphaFoldDB; S6EXR9; -.
DR STRING; 1351755.CCH01_06370; -.
DR GeneID; 66300999; -.
DR OrthoDB; 9782828at2; -.
DR UniPathway; UPA00629; UER00680.
DR Proteomes; UP000190476; Chromosome i.
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:UP000190476};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_01237}.
FT ACT_SITE 133
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 161
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01237,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 44..45
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01237"
FT BINDING 45
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 202
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT SITE 133
FT /note="Involved in proton transfer during cleavage"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01237"
SQ SEQUENCE 289 AA; 32843 MW; 0F3C186B54C7E110 CRC64;
MKGIYSALLV SFDKEGNINE KGLRQIIRHN IDNCKVDGLY VGGSTGENFM LSTEEKKKIF
EIAKDEAKDQ VKLIAQVGSV NLKEAVELAK FTTDLGYNAI SAVTPFYYKF DFKEIKHYYE
TIINSVDNKL IIYSIPFLTG VNMSLDQFAE LFENDKIIGV KFTAADFYLL ERMRKTFPNK
LIFAGFDEMM LPATVLGVDG AIGSTFNVNG KRSKQIFEEA KKGNIEEALK IQHITNDFIT
DVLENGLYQT LKLLLEEFGV EAGYCRQPMK EATPEMRAKA KEIYNKYFK
//
