(data stored in SCRATCH zone)

SWISSPROT: Q3IJ34_PSEHT

ID   Q3IJ34_PSEHT            Unreviewed;       294 AA.
AC   Q3IJ34;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 95.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000256|HAMAP-Rule:MF_00418};
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   ECO:0000313|EMBL:CAI85283.1};
GN   OrderedLocusNames=PSHAa0180 {ECO:0000313|EMBL:CAI85283.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85283.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85283.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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: Pyruvate + L-aspartate-4-semialdehyde = (4S)-
CC       4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O.
CC       {ECO:0000256|HAMAP-Rule:MF_00418, ECO:0000256|SAAS:SAAS00570589}.
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:SAAS00543063}.
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: 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; CR954246; CAI85283.1; -; Genomic_DNA.
DR   RefSeq; WP_011326898.1; NC_007481.1.
DR   ProteinModelPortal; Q3IJ34; -.
DR   STRING; 326442.PSHAa0180; -.
DR   EnsemblBacteria; CAI85283; CAI85283; PSHAa0180.
DR   GeneID; 32566680; -.
DR   KEGG; pha:PSHAa0180; -.
DR   eggNOG; ENOG4105CDP; Bacteria.
DR   eggNOG; COG0329; LUCA.
DR   HOGENOM; HOG000034708; -.
DR   KO; K01714; -.
DR   OMA; MSWDEHV; -.
DR   OrthoDB; POG091H00C1; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
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; Q3IJ34.
DR   SWISS-2DPAGE; Q3IJ34.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00570585};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00543067};
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:CAI85283.1};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00570598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00543140}.
FT   ACT_SITE    138    138       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00418}.
FT   ACT_SITE    166    166       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00418}.
FT   BINDING      51     51       Pyruvate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00418}.
FT   BINDING     207    207       Pyruvate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00418}.
FT   SITE         50     50       Part of a proton relay during catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_00418}.
FT   SITE        112    112       Part of a proton relay during catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_00418}.
SQ   SEQUENCE   294 AA;  32261 MW;  57F9FF4D6FD0F04F CRC64;
     MIKNFNLDDY SVWTALVTPF NQNGTIDYGT LTTLVAEQAA ANNAILLLGS TGEGLALTLK
     EQQAIVEHVC QLSPNVPLMV AVGGMNLKQQ LAWVEYCNHL PIHSFLLGSP LYAKPGVIGQ
     THWFESLLNI SKHPCMLYNV PGRSAVDIPV ATIQNLQQHK NLWALKEASG NIAQFEAYRQ
     AAPNLAIFSG DDALMPYFAQ AGAKGLVSVA ANAWPLQTHE FVQRSLSGQY PNLFTQWSSA
     ISSLFTVANP IPVKVLMHLQ GRLTSSYLRP PLTHLELTQT TCIEQANNTI LSWH
//

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