(data stored in SCRATCH zone)

SWISSPROT: Q13DE3_RHOPS

ID   Q13DE3_RHOPS            Unreviewed;       315 AA.
AC   Q13DE3;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 96.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000256|HAMAP-Rule:MF_00418, ECO:0000256|SAAS:SAAS00767708};
DE            Short=HTPA synthase {ECO:0000256|HAMAP-Rule:MF_00418};
DE            EC=4.3.3.7 {ECO:0000256|HAMAP-Rule:MF_00418};
GN   Name=dapA {ECO:0000256|HAMAP-Rule:MF_00418};
GN   OrderedLocusNames=RPD_0658 {ECO:0000313|EMBL:ABE37896.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37896.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37896.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37896.1,
RC   ECO:0000313|Proteomes:UP000001818};
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., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-
CC       semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-
CC       tetrahydrodipicolinate (HTPA). {ECO:0000256|HAMAP-Rule:MF_00418,
CC       ECO:0000256|SAAS:SAAS00570606}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-
CC         hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O;
CC         Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519;
CC         EC=4.3.3.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00418,
CC         ECO:0000256|SAAS:SAAS01124461};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
CC       {ECO:0000256|HAMAP-Rule:MF_00418, ECO:0000256|SAAS:SAAS00570584}.
CC   -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_00418}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00418,
CC       ECO:0000256|SAAS:SAAS00767691}.
CC   -!- SIMILARITY: Belongs to the DapA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00418, ECO:0000256|PIRNR:PIRNR001365,
CC       ECO:0000256|SAAS:SAAS00579284}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00418}.
CC   -!- CAUTION: Was originally thought to be a dihydrodipicolinate
CC       synthase (DHDPS), catalyzing the condensation of (S)-aspartate-
CC       beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate
CC       (DHDP). However, it was shown in E.coli that the product of the
CC       enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-
CC       hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that
CC       the consecutive dehydration reaction leading to DHDP is not
CC       spontaneous but catalyzed by DapB. {ECO:0000256|HAMAP-
CC       Rule:MF_00418}.
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DR   EMBL; CP000283; ABE37896.1; -; Genomic_DNA.
DR   RefSeq; WP_011501083.1; NC_007958.1.
DR   STRING; 316057.RPD_0658; -.
DR   EnsemblBacteria; ABE37896; ABE37896; RPD_0658.
DR   KEGG; rpd:RPD_0658; -.
DR   eggNOG; ENOG4105CDP; Bacteria.
DR   eggNOG; COG0329; LUCA.
DR   HOGENOM; HOG000173604; -.
DR   KO; K01714; -.
DR   OMA; GDEMKAM; -.
DR   OrthoDB; 1438588at2; -.
DR   BioCyc; RPAL316057:RPD_RS03370-MONOMER; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase; 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   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.
PE   3: Inferred from homology;
DR   PRODOM; Q13DE3.
DR   SWISS-2DPAGE; Q13DE3.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00570585};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00767706};
KW   Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00570604};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00418, ECO:0000256|PIRNR:PIRNR001365,
KW   ECO:0000256|SAAS:SAAS00579236, ECO:0000313|EMBL:ABE37896.1};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00570598};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00570587}.
FT   ACT_SITE    171    171       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00418}.
FT   BINDING     213    213       Pyruvate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00418}.
FT   SITE         54     54       Part of a proton relay during catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_00418}.
FT   SITE        117    117       Part of a proton relay during catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_00418}.
SQ   SEQUENCE   315 AA;  33116 MW;  F4B1EED415353529 CRC64;
     MTNPINSSTP WLTGFIADLP TPFDANDRID WGSFEMLCEQ QIRSGARAVL VAETMGEAST
     LTLTEHDALI GAAVAISCGR VAVIAGAGSN STSQAIDLTR RAEANGADAV MSVVPYYNKP
     MQSGIVAHFS AIAQATALPI ILHDAPGRTA RELSDETMQR LADIPRFAGA KDATGDIARL
     VRLRSKLPPD FHLLSGDDST AGAYLAAGGD GCVSILSNIA PDLCRSIYQY CRQADLVSSR
     TLAAHLAPLG QAVLPDATPA ALKYALCLLG LAAPWVRLPL VELDQSAKMA VAKAVAGVFL
     SYRGYGGEHR DLIAV
//

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