NANA_PASMU
ID NANA_PASMU Reviewed; 293 AA.
AC Q9CKB0;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=N-acetylneuraminate lyase {ECO:0000255|HAMAP-Rule:MF_01237};
DE Short=NAL {ECO:0000255|HAMAP-Rule:MF_01237};
DE Short=Neu5Ac lyase {ECO:0000255|HAMAP-Rule:MF_01237};
DE EC=4.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01237};
DE AltName: Full=N-acetylneuraminate pyruvate-lyase {ECO:0000255|HAMAP-Rule:MF_01237};
DE AltName: Full=N-acetylneuraminic acid aldolase {ECO:0000255|HAMAP-Rule:MF_01237};
DE AltName: Full=Sialate lyase {ECO:0000255|HAMAP-Rule:MF_01237};
DE AltName: Full=Sialic acid aldolase {ECO:0000255|HAMAP-Rule:MF_01237};
DE AltName: Full=Sialic acid lyase {ECO:0000255|HAMAP-Rule:MF_01237};
GN Name=nanA {ECO:0000255|HAMAP-Rule:MF_01237}; OrderedLocusNames=PM1715;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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:0000255|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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01237}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01237}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01237}.
CC -!- SIMILARITY: Belongs to the DapA family. NanA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01237}.
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DR EMBL; AE004439; AAK03799.1; -; Genomic_DNA.
DR RefSeq; WP_005718701.1; NC_002663.1.
DR PDB; 4IMC; X-ray; 1.85 A; A/B/C/D=1-293.
DR PDB; 4IMD; X-ray; 2.10 A; A/B/C/D=1-293.
DR PDB; 4IME; X-ray; 1.75 A; A/B/C/D/E/F/G/H=1-293.
DR PDB; 4IMF; X-ray; 1.90 A; A/B=1-293.
DR PDB; 4IMG; X-ray; 1.85 A; A/B=1-293.
DR PDBsum; 4IMC; -.
DR PDBsum; 4IMD; -.
DR PDBsum; 4IME; -.
DR PDBsum; 4IMF; -.
DR PDBsum; 4IMG; -.
DR AlphaFoldDB; Q9CKB0; -.
DR SMR; Q9CKB0; -.
DR STRING; 747.DR93_646; -.
DR EnsemblBacteria; AAK03799; AAK03799; PM1715.
DR KEGG; pmu:PM1715; -.
DR HOGENOM; CLU_049343_6_0_6; -.
DR OMA; VVPPVCT; -.
DR BRENDA; 4.1.3.3; 4558.
DR UniPathway; UPA00629; UER00680.
DR Proteomes; UP000000809; Chromosome.
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; -; 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 Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR TIGRFAMs; TIGR00683; nanA; 1.
DR PROSITE; PS00665; DHDPS_1; 1.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Lyase;
KW Reference proteome; Schiff base.
FT CHAIN 1..293
FT /note="N-acetylneuraminate lyase"
FT /id="PRO_0000103216"
FT ACT_SITE 164
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT BINDING 47..48
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT SITE 136
FT /note="Involved in proton transfer during cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:4IME"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:4IME"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:4IME"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:4IME"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:4IME"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:4IME"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:4IME"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 209..224
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 228..248
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:4IME"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:4IME"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:4IME"
SQ SEQUENCE 293 AA; 32608 MW; 69AE7B7729340545 CRC64;
MKNLKGIFSA LLVSFNADGS INEKGLRQIV RYNIDKMKVD GLYVGGSTGE NFMLSTEEKK
EIFRIAKDEA KDEIALIAQV GSVNLQEAIE LGKYATELGY DSLSAVTPFY YKFSFPEIKH
YYDSIIEATG NYMIVYSIPF LTGVNIGVEQ FGELYKNPKV LGVKFTAGDF YLLERLKKAY
PNHLIWAGFD EMMLPAASLG VDGAIGSTFN VNGVRARQIF ELTQAGKLKE ALEIQHVTND
LIEGILANGL YLTIKELLKL DGVEAGYCRE PMTKELSPEK VAFAKELKAK YLS
