ID F6CYY5_MARPP Unreviewed; 333 AA.
AC F6CYY5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:AEF53112.1};
DE EC=4.3.3.7 {ECO:0000313|EMBL:AEF53112.1};
GN OrderedLocusNames=Mar181_0043 {ECO:0000313|EMBL:AEF53112.1};
OS Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF53112.1, ECO:0000313|Proteomes:UP000009230};
RN [1] {ECO:0000313|EMBL:AEF53112.1, ECO:0000313|Proteomes:UP000009230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181
RC {ECO:0000313|Proteomes:UP000009230};
RX PubMed=23458837; DOI=10.4056/sigs.2976373;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Lu M., Bruce D., Detter C., Tapia R., Han S.,
RA Land M.L., Ivanova N., Mikhailova N., Johnston A.W., Sanchez-Amat A.;
RT "Complete genome sequence of Marinomonas posidonica type strain (IVIA-Po-
RT 181(T)).";
RL Stand. Genomic Sci. 7:31-43(2012).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; CP002771; AEF53112.1; -; Genomic_DNA.
DR RefSeq; WP_013794589.1; NC_015559.1.
DR AlphaFoldDB; F6CYY5; -.
DR STRING; 491952.Mar181_0043; -.
DR KEGG; mpc:Mar181_0043; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_075248_0_0_6; -.
DR OrthoDB; 6142028at2; -.
DR Proteomes; UP000009230; Chromosome.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-EC.
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:SF74; BLL4423 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}.
FT ACT_SITE 141
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 214
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 333 AA; 36139 MW; ED30E439AC995D27 CRC64;
MSNDVFDVSV FNGVMPALMT PCKPDRTPDF EALIKKGKEM MAAGMSAVVY CGSMGDWPLL
TDAERMEGVE RLVAAGVPVV VGTGAINTKS AVALAAHAQK VGAAGLMVIP RVLSRGSVIA
AQRHHFKAIL EAAPDVPAII YNSPVYGFAT RADLFFSLRA EHPNLVGFKE FGGVDDLRYA
AENITSQDDD VLLMVGVDTA VFHGFVNCGA VGAITGIGTA LPKEVLLLTN LSRKAAQGHA
EARKRAQELE EAFHVLASFD EGPDLVLFFK YLLVLNGEPA YRLHFNETDE LNDAQRHYCE
QQYALFKTWF ADWSQQGGIL SIIQLTDMQV TEC
//
