DAPA_PROMA
ID DAPA_PROMA Reviewed; 302 AA.
AC P49423; Q51920;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000255|HAMAP-Rule:MF_00418};
DE Short=HTPA synthase {ECO:0000255|HAMAP-Rule:MF_00418};
DE EC=4.3.3.7 {ECO:0000255|HAMAP-Rule:MF_00418};
GN Name=dapA {ECO:0000255|HAMAP-Rule:MF_00418}; OrderedLocusNames=Pro_1813;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RA Lorenz M., Boerner T., Hess W.R.;
RT "Molecular cloning and characterization of a dihydrodipicolinate synthase
RT (DHDPS) gene from the photoautotrophic prokaryote Prochlorococcus marinus
RT CCMP 1375 (Prochlorophyta).";
RL Endocyt. Cell Res. 11:59-68(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-302.
RC STRAIN=SARG / CCMP1375 / SS120;
RA Lorenz M., Partensky F., Boerner T., Hess W.R.;
RT "Sequencing and determination of copy numbers of RAPD fragments amplified
RT by repetitive primers in the prokaryote Prochlorococcus marinus.";
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde
CC [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
CC {ECO:0000255|HAMAP-Rule:MF_00418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-
CC 2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00418};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_00418}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00418}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00418}.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000255|HAMAP-
CC Rule:MF_00418}.
CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate synthase
CC (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde
CC [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was
CC shown in E.coli that the product of the enzymatic reaction is not
CC dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-
CC dipicolinic acid (HTPA), and that the consecutive dehydration reaction
CC leading to DHDP is not spontaneous but catalyzed by DapB.
CC {ECO:0000305}.
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DR EMBL; Z68126; CAA92211.1; -; Genomic_DNA.
DR EMBL; AE017126; AAQ00857.1; -; Genomic_DNA.
DR EMBL; Z37733; CAA85785.1; -; Genomic_DNA.
DR PIR; S51751; S51751.
DR RefSeq; NP_876204.1; NC_005042.1.
DR RefSeq; WP_011125962.1; NC_005042.1.
DR AlphaFoldDB; P49423; -.
DR SMR; P49423; -.
DR STRING; 167539.Pro_1813; -.
DR EnsemblBacteria; AAQ00857; AAQ00857; Pro_1813.
DR GeneID; 54201143; -.
DR KEGG; pma:Pro_1813; -.
DR PATRIC; fig|167539.5.peg.1915; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_7_1_3; -.
DR OMA; GMDACVP; -.
DR OrthoDB; 1438588at2; -.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000001420; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR CDD; cd00950; DHDPS; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00418; DapA; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005263; DapA.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR InterPro; IPR020624; Schiff_base-form_aldolases_CS.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR TIGRFAMs; TIGR00674; dapA; 1.
DR PROSITE; PS00665; DHDPS_1; 1.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Diaminopimelate biosynthesis; Lyase;
KW Lysine biosynthesis; Reference proteome; Schiff base.
FT CHAIN 1..302
FT /note="4-hydroxy-tetrahydrodipicolinate synthase"
FT /id="PRO_0000103135"
FT ACT_SITE 144
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT ACT_SITE 172
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT BINDING 55
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT BINDING 214
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT SITE 54
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT SITE 117
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT CONFLICT 3
FT /note="T -> P (in Ref. 1; CAA92211)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="A -> P (in Ref. 1; CAA92211)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="L -> P (in Ref. 1; CAA92211 and 3; CAA85785)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 31764 MW; 7C6B2871C7A2E0D6 CRC64;
MSTVPEISSA PFGRLLTAMV TPFDTAGAVD FALAARLARY LVDQGSDGLI VCGTTGESPT
LSWEEQYQLL ETVRNAVNGS AKVLAGTGSN STSEAIHATA KAAEAGADGA LVVVPYYNKP
PQAGLESHFR AVAQAAPDLP LMLYNIPGRT GCSISPITVQ RLMNCSNIVS FKAASGTTNE
VTDLRIRCGS RLAIYSGDDG LLLPMLSVGA VGVVSVASHI VGMRLKAMIE AYFAGENSLA
LSHHEQLQPL FKALFATTNP IPVKAALELI GWPVGAPRSP LLPLENQMKN ELMKTISALL
QT
