NANA_HISS2
ID NANA_HISS2 Reviewed; 292 AA.
AC B0UTI7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=HSM_1106;
OS Histophilus somni (strain 2336) (Haemophilus somnus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=228400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2336;
RG US DOE Joint Genome Institute;
RA Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA Dyer D.W., Inzana T.J.;
RT "Complete sequence of Haemophilus somnus 2336.";
RL Submitted (FEB-2008) 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: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; CP000947; ACA30825.1; -; Genomic_DNA.
DR RefSeq; WP_011608851.1; NC_010519.1.
DR AlphaFoldDB; B0UTI7; -.
DR SMR; B0UTI7; -.
DR STRING; 228400.HSM_1106; -.
DR EnsemblBacteria; ACA30825; ACA30825; HSM_1106.
DR KEGG; hsm:HSM_1106; -.
DR HOGENOM; CLU_049343_6_0_6; -.
DR OMA; VVPPVCT; -.
DR OrthoDB; 1438588at2; -.
DR UniPathway; UPA00629; UER00680.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Lyase; Schiff base.
FT CHAIN 1..292
FT /note="N-acetylneuraminate lyase"
FT /id="PRO_1000085737"
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"
SQ SEQUENCE 292 AA; 32321 MW; 8E32D8F3C26511CE CRC64;
MKNLKGIFSA LLVSFNEDGS INEKGLREIV RYNIDKMKID GLYVGGSTGE NFMLSTAEKK
EIFRIAKEEA KDQVALIAQV GSVNLHEAVE LGKYATELGY DSLSAVTPFY YKFSFAEIKH
YYETIIAETG NNMIVYSIPF LTGVNMGVEQ FGELYANPKV LGVKFTAGDF YLLERLKKAY
PNHLVWAGFD EMMLPAVSLG VDGAIGSTFN VNGLRARQIF ELAKAGKVAE ALEIQHVTND
LIEGILANGL YLTIKEILKL QGVNAGYCRE PMTAKATEKQ LAVAKELKEK FL