NANA_FUSNN
ID NANA_FUSNN Reviewed; 290 AA.
AC Q8RDN6;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=FN1475;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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; AE009951; AAL95668.1; -; Genomic_DNA.
DR RefSeq; NP_604369.1; NC_003454.1.
DR PDB; 5ZJM; X-ray; 2.32 A; A/B/C/D=1-289.
DR PDB; 5ZKA; X-ray; 1.76 A; A=1-290, B=1-289.
DR PDBsum; 5ZJM; -.
DR PDBsum; 5ZKA; -.
DR AlphaFoldDB; Q8RDN6; -.
DR SMR; Q8RDN6; -.
DR STRING; 190304.FN1475; -.
DR EnsemblBacteria; AAL95668; AAL95668; FN1475.
DR KEGG; fnu:FN1475; -.
DR PATRIC; fig|190304.8.peg.2035; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_6_0_0; -.
DR InParanoid; Q8RDN6; -.
DR OMA; VVPPVCT; -.
DR BioCyc; FNUC190304:G1FZS-2043-MON; -.
DR UniPathway; UPA00629; UER00680.
DR Proteomes; UP000002521; 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..290
FT /note="N-acetylneuraminate lyase"
FT /id="PRO_0000103213"
FT ACT_SITE 161
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT BINDING 44..45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT SITE 133
FT /note="Involved in proton transfer during cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:5ZKA"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:5ZKA"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:5ZKA"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:5ZKA"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:5ZKA"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:5ZKA"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:5ZKA"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:5ZKA"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:5ZKA"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:5ZKA"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5ZJM"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:5ZKA"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:5ZKA"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:5ZKA"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:5ZKA"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:5ZKA"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:5ZKA"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:5ZKA"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:5ZKA"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:5ZKA"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:5ZKA"
FT HELIX 206..220
FT /evidence="ECO:0007829|PDB:5ZKA"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:5ZKA"
FT HELIX 225..245
FT /evidence="ECO:0007829|PDB:5ZKA"
FT HELIX 247..257
FT /evidence="ECO:0007829|PDB:5ZKA"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:5ZKA"
SQ SEQUENCE 290 AA; 32803 MW; DEE469A25A4075FC CRC64;
MKGIYSALMV PYNEDGSINE KGLREIIRYN IDKMKVDGLY VGGSTGENFM ISTEEKKRVF
EIAIDEAKDS VNLIAQVGSI NLNEAVELGK YVTKLGYKCL SAVTPFYYKF DFSEIKDYYE
TIVRETGNYM IIYSIPFLTG VNMSLSQFGE LFENEKIIGV KFTAGDFYLL ERVRKAFPDK
LIFAGFDEML LPATVLGVDG AIGSTYNING IRAKQIFELA KNSKIDEALK IQHTTNDLIE
GILSNGLYQT IKEILKLEGV DAGYCRKPMK KISQKQIEFA KELHKKFLKN
