ID   D0YYS9_PHODD            Unreviewed;       300 AA.
AC   D0YYS9;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=N-acetylneuraminate lyase {ECO:0000313|EMBL:EEZ41410.1};
DE            EC=4.1.3.3 {ECO:0000313|EMBL:EEZ41410.1};
GN   ORFNames=VDA_002442 {ECO:0000313|EMBL:EEZ41410.1};
OS   Photobacterium damselae subsp. damselae CIP 102761.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ41410.1, ECO:0000313|Proteomes:UP000003579};
RN   [1] {ECO:0000313|EMBL:EEZ41410.1, ECO:0000313|Proteomes:UP000003579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ41410.1,
RC   ECO:0000313|Proteomes:UP000003579};
RG   Los Alamos National Laboratory (LANL);
RG   National Microbial Pathogen Data Resource (NMPDR);
RA   Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA   Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA   Bartels D.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the DapA family.
CC       {ECO:0000256|PIRNR:PIRNR001365}.
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DR   EMBL; ADBS01000001; EEZ41410.1; -; Genomic_DNA.
DR   RefSeq; WP_005300099.1; NZ_ADBS01000001.1.
DR   AlphaFoldDB; D0YYS9; -.
DR   eggNOG; COG0329; Bacteria.
DR   Proteomes; UP000003579; Unassembled WGS sequence.
DR   GO; GO:0008747; F:N-acetylneuraminate lyase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR020624; Schiff_base-form_aldolases_CS.
DR   PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR   PANTHER; PTHR12128:SF21; 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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003579}.
FT   ACT_SITE        136
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        166
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         47
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT   BINDING         208
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   300 AA;  31984 MW;  32521662AC796AAC CRC64;
     MEKLTGLIAA PHTPFDTNGN VNFAAIDQIA AHLIKDGVKG VYVCGTTGEG IHCSVEERKA
     IAERWVSASQ GQLKITLHTG ALSIVDTLEL TRHAETLDIF ATSAIGPCFF KPGSVDDLVE
     YCATVAAAAP SKGFYYYHSG MSGVNLDMEQ FLIKADKKIP NLSGIKFNSG DLYEYQRCLR
     ACDGKYDIPF GVDEHLPGAL AVGAIGAVGS TYNYAAPHFT KMIEDFNNGD HAAVVKGMDN
     VIALIRVLVE FGGVAAGKAA MALHGIDCGD PRLPLRALTT EQKETVVAKM RDAGFLNAAK
//