NANA_HAEIN
ID NANA_HAEIN Reviewed; 293 AA.
AC P44539;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=N-acetylneuraminate lyase;
DE Short=NAL;
DE Short=Neu5Ac lyase;
DE EC=4.1.3.3;
DE AltName: Full=N-acetylneuraminate pyruvate-lyase;
DE AltName: Full=N-acetylneuraminic acid aldolase;
DE AltName: Full=Sialate lyase;
DE AltName: Full=Sialic acid aldolase;
DE AltName: Full=Sialic acid lyase;
GN Name=nanA; OrderedLocusNames=HI_0142;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH
RP SIALIC ACID ALDITOL; 4-DEOXY-SIALIC ACID AND 4-OXO-SIALIC ACID.
RX PubMed=11031117; DOI=10.1006/jmbi.2000.4138;
RA Barbosa J.A.R.G., Smith B.J., DeGori R., Ooi H.C., Marcuccio S.M.,
RA Campi E.M., Jackson W.R., Brossmer R., Sommer M., Lawrence M.C.;
RT "Active site modulation in the N-acetylneuraminate lyase sub-family as
RT revealed by the structure of the inhibitor-complexed Haemophilus influenzae
RT enzyme.";
RL J. Mol. Biol. 303:405-421(2000).
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.
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 -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the DapA family. NanA subfamily. {ECO:0000305}.
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DR EMBL; L42023; AAC21814.1; -; Genomic_DNA.
DR PIR; G64050; G64050.
DR RefSeq; NP_438311.1; NC_000907.1.
DR RefSeq; WP_005694428.1; NC_000907.1.
DR PDB; 1F5Z; X-ray; 1.88 A; A/B/C/D=1-293.
DR PDB; 1F6K; X-ray; 1.60 A; A/C=1-293.
DR PDB; 1F6P; X-ray; 2.25 A; A/B/C/D=1-293.
DR PDB; 1F73; X-ray; 1.95 A; A/B/C/D=1-293.
DR PDB; 1F74; X-ray; 1.60 A; A/C=1-293.
DR PDB; 1F7B; X-ray; 1.80 A; A/C=1-293.
DR PDBsum; 1F5Z; -.
DR PDBsum; 1F6K; -.
DR PDBsum; 1F6P; -.
DR PDBsum; 1F73; -.
DR PDBsum; 1F74; -.
DR PDBsum; 1F7B; -.
DR AlphaFoldDB; P44539; -.
DR SMR; P44539; -.
DR STRING; 71421.HI_0142; -.
DR EnsemblBacteria; AAC21814; AAC21814; HI_0142.
DR KEGG; hin:HI_0142; -.
DR PATRIC; fig|71421.8.peg.144; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_6_0_6; -.
DR OMA; VVPPVCT; -.
DR PhylomeDB; P44539; -.
DR BioCyc; HINF71421:G1GJ1-154-MON; -.
DR EvolutionaryTrace; P44539; -.
DR PRO; PR:P44539; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008747; F:N-acetylneuraminate lyase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
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_0000103214"
FT ACT_SITE 164
FT /note="Schiff-base intermediate with substrate"
FT BINDING 47..48
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 136
FT /note="Involved in proton transfer during cleavage"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1F6K"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1F7B"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:1F6K"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1F6K"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1F6K"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1F6K"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:1F6K"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:1F6K"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:1F6K"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1F6K"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:1F6K"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1F6K"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:1F6K"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:1F6K"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1F6K"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:1F6K"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1F6K"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1F6K"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:1F6K"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:1F6K"
FT HELIX 209..224
FT /evidence="ECO:0007829|PDB:1F6K"
FT HELIX 228..248
FT /evidence="ECO:0007829|PDB:1F6K"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:1F6K"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:1F6K"
SQ SEQUENCE 293 AA; 32565 MW; ACA755D0A5D93D33 CRC64;
MRDLKGIFSA LLVSFNEDGT INEKGLRQII RHNIDKMKVD GLYVGGSTGE NFMLSTEEKK
EIFRIAKDEA KDQIALIAQV GSVNLKEAVE LGKYATELGY DCLSAVTPFY YKFSFPEIKH
YYDTIIAETG NNMIVYSIPF LTGVNMGIEQ FGELYKNPKV LGVKFTAGDF YLLERLKKAY
PNHLIWAGFD EMMLPAASLG VDGAIGSTFN VNGVRARQIF ELTKAGKLAE ALEIQHVTND
LIEGILANGL YLTIKELLKL EGVDAGYCRE PMTSKATEEQ LAKAKDLKAK FLS
