ID Q7UMJ1_RHOBA Unreviewed; 319 AA.
AC Q7UMJ1;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Dihydrodipicolinate synthase DapA {ECO:0000313|EMBL:CAD75926.1};
DE EC=4.2.1.52 {ECO:0000313|EMBL:CAD75926.1};
GN Name=dapA {ECO:0000313|EMBL:CAD75926.1};
GN OrderedLocusNames=RB8798 {ECO:0000313|EMBL:CAD75926.1};
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD75926.1, ECO:0000313|Proteomes:UP000001025};
RN [1] {ECO:0000313|EMBL:CAD75926.1, 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 -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; BX294148; CAD75926.1; -; Genomic_DNA.
DR RefSeq; NP_868549.1; NC_005027.1.
DR AlphaFoldDB; Q7UMJ1; -.
DR STRING; 243090.RB8798; -.
DR EnsemblBacteria; CAD75926; CAD75926; RB8798.
DR KEGG; rba:RB8798; -.
DR PATRIC; fig|243090.15.peg.4222; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_5_1_0; -.
DR InParanoid; Q7UMJ1; -.
DR OrthoDB; 9782828at2; -.
DR Proteomes; UP000001025; 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-KW.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
DR CDD; cd00408; DHDPS-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR PANTHER; PTHR42849; N-ACETYLNEURAMINATE LYASE; 1.
DR PANTHER; PTHR42849:SF1; 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; PS00666; DHDPS_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 154
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 182
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 66
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 227
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 319 AA; 34931 MW; AEA49856A321D747 CRC64;
MKSSSPIADA RDMSRLFTAG NRLQGIVPPL ITPLRARDEL DQEGWERLIE HVIDGGVSGI
FILGTTGEAP SLSYRLRREL ITATTHLVAK RVPVLVGVTD TAFVESVSIA HHAADAGADA
AVLTTPYYFP AGQTELTAYV QNIAPEIPLP LMLYNMPGLT KVWFEIETLK TLSEIQSIVG
VKDSSGDLDY FRRLCDLRNE VREDWSILIG PEAMLPEAHQ LGGDGGVAGG ANVMTRCFVD
CYEGLTANDS AKTEAAISKI RRFQDIYDVG KYASRHIKAT KCAASLLGIC SDLPADPFHR
FFEPERERVA AILRDLDIL
//
