ID   A0A068NEZ4_9ACTO        Unreviewed;       302 AA.
AC   A0A068NEZ4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JUN-2015, entry version 8.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000256|HAMAP-Rule:MF_00418, ECO:0000256|SAAS:SAAS00086421};
DE            Short=HTPA synthase {ECO:0000256|HAMAP-Rule:MF_00418};
DE            EC=4.3.3.7 {ECO:0000256|HAMAP-Rule:MF_00418, ECO:0000256|SAAS:SAAS00086421};
GN   Name=dapA {ECO:0000256|HAMAP-Rule:MF_00418};
GN   ORFNames=FB03_00765 {ECO:0000313|EMBL:AIE82046.1};
OS   Actinotignum schaalii.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
OC   Actinotignum.
OX   NCBI_TaxID=59505 {ECO:0000313|EMBL:AIE82046.1};
RN   [1] {ECO:0000313|EMBL:AIE82046.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCUG 27420 {ECO:0000313|EMBL:AIE82046.1};
RX   PubMed=25189588;
RA   Kristiansen R., Dueholm M.S., Bank S., Nielsen P.H., Karst S.M.,
RA   Cattoir V., Lienhard R., Grisold A.J., Olsen A.B., Reinhard M.,
RA   Soby K.M., Christensen J.J., Prag J., Thomsen T.R.;
RT   "Complete Genome Sequence of Actinobaculum schaalii Strain CCUG
RT   27420.";
RL   Genome Announc. 2:e00880-14(2014).
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:SAAS00086388}.
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:SAAS00086378}.
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:SAAS00086376}.
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:SAAS00020921}.
CC   -!- SIMILARITY: Belongs to the DapA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00418, ECO:0000256|PIRNR:PIRNR001365}.
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; CP008802; AIE82046.1; -; Genomic_DNA.
DR   EnsemblBacteria; AIE82046; AIE82046; FB03_00765.
DR   UniPathway; UPA00034; UER00017.
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   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 {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00086393};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00020940};
KW   Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00086370};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|PIRNR:PIRNR001365};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00086416};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00418,
KW   ECO:0000256|SAAS:SAAS00021621}.
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     210    210       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   302 AA;  31422 MW;  52935AA17130DB21 CRC64;
     MDEHTLPSRS FGSVSVAMVT PFHADGSLDV DAAVALATTL VDQGCDALLL SGTTGESPTT
     HQPEKDVLVR EVCAAVRNRA MVIAGAGSND TAHAVRIARG AEKSGAQGLL VVAPYYNRPS
     QEGVYQHILN VTEATDLPVM VYDIPGRTGV RLELDTLLRL AEHPRILAVK DATGDVAGGF
     VKMARTGLEY YSGDDALNFA WLAHGASGVI SVAGHVIAAR LRALVEQVDA GDLPAARREA
     AAQRHIISAI MGSGQGAVMA KEALKLLGVI PSATLRLPLV GASAVQIAEL AEALRAEGLL
     AD
//