ID A3ZUS3_9BACT Unreviewed; 303 AA.
AC A3ZUS3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Dihydrodipicolinate synthase DapA {ECO:0000313|EMBL:EAQ79659.1};
GN ORFNames=DSM3645_24160 {ECO:0000313|EMBL:EAQ79659.1};
OS Blastopirellula marina DSM 3645.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Blastopirellula.
OX NCBI_TaxID=314230 {ECO:0000313|EMBL:EAQ79659.1, ECO:0000313|Proteomes:UP000004358};
RN [1] {ECO:0000313|EMBL:EAQ79659.1, ECO:0000313|Proteomes:UP000004358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3645 {ECO:0000313|EMBL:EAQ79659.1,
RC ECO:0000313|Proteomes:UP000004358};
RA Amann R., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAQ79659.1}.
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DR EMBL; AANZ01000013; EAQ79659.1; -; Genomic_DNA.
DR RefSeq; WP_002652729.1; NZ_CH672376.1.
DR AlphaFoldDB; A3ZUS3; -.
DR STRING; 314230.DSM3645_24160; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_5_1_0; -.
DR OrthoDB; 9782828at2; -.
DR Proteomes; UP000004358; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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 Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 135
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 163
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 207
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 303 AA; 33511 MW; 54F3540EA6773E42 CRC64;
MSTFHGIVPP LVTPLLGRDQ LDHEGLERLI EHVLEGGVHG LFILGSTGEA PSLSYRLRRE
VIAAVCRQTD NRVPVLVGVT DTAFVESIAL AQYAADAGAA AVVLSTPYYF PAGQTELRTY
VRNIVSELPL PLMLYNMPAL TKVWFEIETL QKLTDLDGIV GLKDSSGDLD YFAKATRLKE
QRPDWSILIG PEAMLPAAMR LGGDGGVNGG ANILPRLFVE CYDSIITQDE VKLAELHRRI
VDFQRIYDVG KYASKYIKAT KCCLSLLNIC DDFMAEPFHS FHPPEREQLA QILQELDIPV
VQG
//
