ID Q0FT89_SALBH Unreviewed; 293 AA.
AC Q0FT89;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Putative dihydrodipicolinate synthetase {ECO:0000313|EMBL:EAU47280.1};
GN ORFNames=R2601_20751 {ECO:0000313|EMBL:EAU47280.1};
OS Salipiger bermudensis (strain DSM 26914 / JCM 13377 / KCTC 12554 /
OS HTCC2601) (Pelagibaca bermudensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=314265 {ECO:0000313|EMBL:EAU47280.1, ECO:0000313|Proteomes:UP000006230};
RN [1] {ECO:0000313|EMBL:EAU47280.1, ECO:0000313|Proteomes:UP000006230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26914 / JCM 13377 / KCTC 12554 / HTCC2601
RC {ECO:0000313|Proteomes:UP000006230};
RX PubMed=20729358; DOI=10.1128/JB.00873-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT genera.";
RL J. Bacteriol. 192:5552-5553(2010).
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:EAU47280.1}.
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DR EMBL; AATQ01000007; EAU47280.1; -; Genomic_DNA.
DR RefSeq; WP_007799036.1; NZ_DS022276.1.
DR AlphaFoldDB; Q0FT89; -.
DR STRING; 314265.R2601_20751; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_5_0_5; -.
DR OrthoDB; 199953at2; -.
DR Proteomes; UP000006230; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; 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; PTHR12128:SF72; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000006230}.
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 46
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 205
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 293 AA; 31263 MW; 1958CEB2C5378F90 CRC64;
MSFEGVFPYL VSPLNQSGEV RGDVIEALVE RLITAGVHGL APLGSTGEFA YLDGRQRLAV
AKSVIKASRG RVPVIPGVAS TSTADAVSQT RAMVEAGADG ILAILEAYFP IDEDGVEAYF
TAIAEAAEGL PVVLYTNPNF QRSDLTLPVI ERLSHFENIR YIKDASSNTG RLLSIMERTK
GRLEVFAASA HIPTCVMMIG GKGWMAGPAC IVPEQSIALY EAAKAGDWGR AMELQRPLWR
INELFARHSL AACIKAALEL QGFEVGDPVA PQKPLGAAAR DEVASALRDL GAL
//
