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Database: UniProt
Entry: A3K8S9_9RHOB
LinkDB: A3K8S9_9RHOB
Original site: A3K8S9_9RHOB 
ID   A3K8S9_9RHOB            Unreviewed;       299 AA.
AC   A3K8S9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Dihydrodipicolinate synthase protein {ECO:0000313|EMBL:EBA06517.1};
GN   ORFNames=SSE37_14979 {ECO:0000313|EMBL:EBA06517.1};
OS   Sagittula stellata E-37.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sagittula.
OX   NCBI_TaxID=388399 {ECO:0000313|EMBL:EBA06517.1, ECO:0000313|Proteomes:UP000005713};
RN   [1] {ECO:0000313|EMBL:EBA06517.1, ECO:0000313|Proteomes:UP000005713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E-37 {ECO:0000313|EMBL:EBA06517.1,
RC   ECO:0000313|Proteomes:UP000005713};
RA   Moran M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-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:EBA06517.1}.
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DR   EMBL; AAYA01000015; EBA06517.1; -; Genomic_DNA.
DR   RefSeq; WP_005862554.1; NZ_AAYA01000015.1.
DR   AlphaFoldDB; A3K8S9; -.
DR   eggNOG; COG0329; Bacteria.
DR   OrthoDB; 9778880at2; -.
DR   Proteomes; UP000005713; Unassembled WGS sequence.
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   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   SMART; SM01130; DHDPS; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005713}.
FT   ACT_SITE        140
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        164
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         52
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   299 AA;  31594 MW;  EF31B4EB97D93349 CRC64;
     MSSDLHKSLT GVSGILVTPF DEAGEIAPDL QRPIVERAIE AGVHILTANG NTGEFYGLTL
     EEAQAMVHAA GQHIDDRVPM VAGVGRGIRD AQALAEASGL AGASALMIHQ PPDPFVSPRG
     LVRYVEAVRE AGDGLPIVLY LRNDTIGTEA IRAMCLVEGV IGVKWATPNP MKLKAAIAAC
     PDDIVWTGGL AEVWAPTFYA VGARGFTSGL INVWPERSVA INTALENGDY EEARALIAGM
     QVFEDIRAEE QGGANVPGVK GALQMMGEDC GAARPPAAWP LSDSQRLRLE TFMTTNGLI
//
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