ID A0A0R2D6X4_9LACO Unreviewed; 289 AA.
AC A0A0R2D6X4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=FC24_GL000363 {ECO:0000313|EMBL:KRM99397.1};
OS Loigolactobacillus rennini DSM 20253.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=1423796 {ECO:0000313|EMBL:KRM99397.1, ECO:0000313|Proteomes:UP000051638};
RN [1] {ECO:0000313|EMBL:KRM99397.1, ECO:0000313|Proteomes:UP000051638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20253 {ECO:0000313|EMBL:KRM99397.1,
RC ECO:0000313|Proteomes:UP000051638};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM99397.1}.
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DR EMBL; AYYI01000015; KRM99397.1; -; Genomic_DNA.
DR RefSeq; WP_057873279.1; NZ_AYYI01000015.1.
DR AlphaFoldDB; A0A0R2D6X4; -.
DR STRING; 1423796.FC24_GL000363; -.
DR PATRIC; fig|1423796.3.peg.375; -.
DR OrthoDB; 9782828at2; -.
DR UniPathway; UPA00629; UER00680.
DR Proteomes; UP000051638; 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 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:UP000051638};
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; 32407 MW; E550757F21E58D22 CRC64;
MKKLYSALMT AFNEDGTVNS QGIREMVRYN IDVNHIDGLY VGGSTGEAFM LSTEEKKLIF
KTAFDEANGA IDLIAQVGSL NLLEAKALAK YVTDLGYKKI SAVTPFYYNF KFDEIKHYYD
EIVKDVDNKL IIYSIPALTG VALTTDQFAE LFENPKIIGI KYTNADFYLL ERVRNRFPDK
LILSGFDEML LPALALNVDG AIGSTYNLNA KRAKAEMNAF EAGDIAKARQ LQKDSNDLIT
ALIQNDIYPS LKLVMEEMGI HAGYTKEPMS HPTPEMKAGA KEIYQKYLK
//
