ID   Q7UUE0_RHOBA            Unreviewed;       322 AA.
AC   Q7UUE0;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=N-acetylneuraminate lyase {ECO:0000256|ARBA:ARBA00012911};
DE            EC=4.1.3.3 {ECO:0000256|ARBA:ARBA00012911};
GN   Name=nanA {ECO:0000313|EMBL:CAD73140.1};
GN   OrderedLocusNames=RB3352 {ECO:0000313|EMBL:CAD73140.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD73140.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD73140.1, ECO:0000313|Proteomes:UP000001025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC   {ECO:0000313|Proteomes:UP000001025};
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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         Evidence={ECO:0000256|ARBA:ARBA00024547};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the DapA family. NanA subfamily.
CC       {ECO:0000256|ARBA:ARBA00006324}.
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DR   EMBL; BX294138; CAD73140.1; -; Genomic_DNA.
DR   RefSeq; NP_865456.1; NC_005027.1.
DR   AlphaFoldDB; Q7UUE0; -.
DR   STRING; 243090.RB3352; -.
DR   EnsemblBacteria; CAD73140; CAD73140; RB3352.
DR   KEGG; rba:RB3352; -.
DR   PATRIC; fig|243090.15.peg.1546; -.
DR   eggNOG; COG0329; Bacteria.
DR   HOGENOM; CLU_049343_6_1_0; -.
DR   InParanoid; Q7UUE0; -.
DR   OrthoDB; 9771791at2; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008747; F:N-acetylneuraminate lyase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
DR   CDD; cd00954; NAL; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR005264; NanA.
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:UP000001025}.
FT   ACT_SITE        150
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        180
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         60
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT   BINDING         222
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   322 AA;  34857 MW;  02BAC02AB21AA68C CRC64;
     MMVDESLLMQ RMAGRKLSGL IAATYTPMKA CGDLNLDVVP AMVEKLLLDG VSGLYVCGST
     GEGMSLTTRE RQLVASAFVN ATAGRVPVIV QVGHNSLREA QELAKHAQQI GASAISATCP
     SYFKVASVQS LTLCMQELAA AAPETPFYYY HIPVLTGSSI DMVEFLTHAD EAIPTLVGLK
     YTDTMLFEFQ RCLELSNRKF DVVWGCDEML LGATATGARA AIGSTYNLAA KIYRKMTLAL
     ASGQLETARQ WQSKSIEMIC TIGRYPFHPA MKAILAMQGL DVGPCRLPLE SLSQSQVESL
     RESLDAIGFF EWSGDTSKPS DA
//