(data stored in ACNUC7421 zone)

SWISSPROT: DAPA_SYNFM

ID   DAPA_SYNFM              Reviewed;         291 AA.
AC   A0LEA7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 81.
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};
GN   OrderedLocusNames=Sfum_0056;
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB;
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., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-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:0000255|HAMAP-Rule:MF_00418}.
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: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
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:0000305}.
DR   EMBL; CP000478; ABK15759.1; -; Genomic_DNA.
DR   RefSeq; WP_011696932.1; NC_008554.1.
DR   SMR; A0LEA7; -.
DR   STRING; 335543.Sfum_0056; -.
DR   PRIDE; A0LEA7; -.
DR   EnsemblBacteria; ABK15759; ABK15759; Sfum_0056.
DR   KEGG; sfu:Sfum_0056; -.
DR   eggNOG; ENOG4105CDP; Bacteria.
DR   eggNOG; COG0329; LUCA.
DR   HOGENOM; HOG000173604; -.
DR   KO; K01714; -.
DR   OMA; GMDACVP; -.
DR   OrthoDB; 1438588at2; -.
DR   BioCyc; SFUM335543:G1G7I-58-MONOMER; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000001784; 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   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;
DR   PRODOM; A0LEA7.
DR   SWISS-2DPAGE; A0LEA7.
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Diaminopimelate biosynthesis; Lyase; Lysine biosynthesis;
KW   Reference proteome; Schiff base.
FT   CHAIN         1    291       4-hydroxy-tetrahydrodipicolinate
FT                                synthase.
FT                                /FTId=PRO_1000050285.
FT   ACT_SITE    132    132       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00418}.
FT   ACT_SITE    160    160       Schiff-base intermediate with substrate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00418}.
FT   BINDING      44     44       Pyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00418}.
FT   BINDING     202    202       Pyruvate; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00418}.
FT   SITE         43     43       Part of a proton relay during catalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_00418}.
FT   SITE        106    106       Part of a proton relay during catalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_00418}.
SQ   SEQUENCE   291 AA;  31580 MW;  E48FBBF468DC3498 CRC64;
     MFQGAMVAIV TPFKAGQVDE ETFRNLIEFQ IANGTHGIVP CGTTGESATL SFNEHERVIE
     IAVEQVDKRV PVIAGTGSNN TEEAIRLTKH AKNAGADGAL LISPYYNKPT QEGLYRHYEK
     IAKAVDIPLV PYNIPGRTAV NMEPDTIARL AKIDNIVAIK EAAGSMKQIT DIIARCGDEL
     VVLSGEDFLT FPLLCVGGKG VISVVSNIAP ADMANLCNLF LGGDFDAARK LYYRLLPLCH
     GLFYETNPAP VKAALAMMNK IPSDELRLPL APMSPANRLR LRQDLQAYGL I
//

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