(data stored in SCRATCH zone)

SWISSPROT: C1ASP1_RHOOB

ID   C1ASP1_RHOOB            Unreviewed;       301 AA.
AC   C1ASP1;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 61.
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:BAH48490.1};
GN   OrderedLocusNames=ROP_02430 {ECO:0000313|EMBL:BAH48490.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48490.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48490.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48490.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) 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: 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; AP011115; BAH48490.1; -; Genomic_DNA.
DR   RefSeq; WP_012687498.1; NC_012522.1.
DR   ProteinModelPortal; C1ASP1; -.
DR   STRING; 632772.ROP_02430; -.
DR   EnsemblBacteria; BAH48490; BAH48490; ROP_02430.
DR   KEGG; rop:ROP_02430; -.
DR   PATRIC; fig|632772.20.peg.282; -.
DR   eggNOG; ENOG4105CDP; Bacteria.
DR   eggNOG; COG0329; LUCA.
DR   HOGENOM; HOG000173604; -.
DR   KO; K01714; -.
DR   OMA; MSWDEHV; -.
DR   OrthoDB; POG091H00C1; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000002212; Chromosome.
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   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; C1ASP1.
DR   SWISS-2DPAGE; C1ASP1.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00570585};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
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:BAH48490.1};
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:SAAS00543140}.
FT   ACT_SITE    142    142       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00418}.
FT   ACT_SITE    170    170       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00418}.
FT   BINDING      54     54       Pyruvate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00418}.
FT   BINDING     209    209       Pyruvate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00418}.
FT   SITE         53     53       Part of a proton relay during catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_00418}.
FT   SITE        116    116       Part of a proton relay during catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_00418}.
SQ   SEQUENCE   301 AA;  31441 MW;  35AD5B3D255A4EAA CRC64;
     MTVSSAPAAP FGRVLTAMAT AFTEDGELDE EATARIALHL VDHGHDGLVV SGTTGEAATT
     TTAEDGRILR VVKDAVGNRA KVVAGVGTND TRHTLELARQ AVVHGADGLL LVTPYYNKPS
     QGGVLQHFRY VVDAVDTPVM VYDIPSRAGT KLAPSTFEAM AGWPSVVAVK DAAGDPTQAI
     LLRELGFAVY SGDDSLTLGF LAYGACGVVS VLGHVAGDEI RAMIDAFFSG DVESAREINA
     RLQPALRAVM GVPNYGATTV KGALQLLGVL QDRTVRSPLL ALDDVEYEAL RAGLSASELL
     P
//

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