ID Q28JT1_JANSC Unreviewed; 299 AA.
AC Q28JT1;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Dihydrodipicolinate synthetase {ECO:0000313|EMBL:ABD57031.1};
GN OrderedLocusNames=Jann_4114 {ECO:0000313|EMBL:ABD57031.1};
OS Jannaschia sp. (strain CCS1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=290400 {ECO:0000313|EMBL:ABD57031.1, ECO:0000313|Proteomes:UP000008326};
RN [1] {ECO:0000313|Proteomes:UP000008326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1 {ECO:0000313|Proteomes:UP000008326};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABD57031.1, ECO:0000313|Proteomes:UP000008326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1 {ECO:0000313|EMBL:ABD57031.1,
RC ECO:0000313|Proteomes:UP000008326};
RX PubMed=17526795; DOI=10.1128/AEM.02580-06;
RA Moran M.A., Belas R., Schell M.A., Gonzalez J.M., Sun F., Sun S.,
RA Binder B.J., Edmonds J., Ye W., Orcutt B., Howard E.C., Meile C.,
RA Palefsky W., Goesmann A., Ren Q., Paulsen I., Ulrich L.E., Thompson L.S.,
RA Saunders E., Buchan A.;
RT "Ecological genomics of marine Roseobacters.";
RL Appl. Environ. Microbiol. 73:4559-4569(2007).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; CP000264; ABD57031.1; -; Genomic_DNA.
DR RefSeq; WP_011457227.1; NC_007802.1.
DR AlphaFoldDB; Q28JT1; -.
DR STRING; 290400.Jann_4114; -.
DR KEGG; jan:Jann_4114; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_5_1_5; -.
DR OrthoDB; 9782828at2; -.
DR Proteomes; UP000008326; Chromosome.
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:SF67; BLR3884 PROTEIN; 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:UP000008326}.
FT ACT_SITE 139
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 169
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 48
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 210
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 299 AA; 31004 MW; F85ED1246338528A CRC64;
MMSRKIELFV PAITPFAADL SVDTPAFVAR ATGLLNAGAH GLAPFGTTSE ANSLTVAERV
AALEALVDSG IDPAQLIPGT GCCAIADTIT LSSHATGLGC RGVLMLPPFY YKGVSDEGVF
RAFAQVIEAV GPDLRIYLYH IPQMSGVPIT LPLIQRLIEA FGDQIAGLKD SSGKWDNTAA
VIKAFPQIDT YSASESLIPE NVAAGGAGCI SASSNVNPRG IRALIDGLNG ADHDALHEQV
SAVRTIFEGV PLIPAIKAAV AAQAGREGLA RVRPPFTELG ADHSDAIAEA VRLAGPQTR
//
