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Entry: A0A1G6MYH5_9BACT
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ID   A0A1G6MYH5_9BACT        Unreviewed;       216 AA.
AC   A0A1G6MYH5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   08-MAY-2019, entry version 8.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081423};
DE            Short=HTPA reductase {ECO:0000256|HAMAP-Rule:MF_00102};
DE            EC=1.17.1.8 {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081445};
GN   Name=dapB {ECO:0000256|HAMAP-Rule:MF_00102};
GN   ORFNames=SAMN04488588_1422 {ECO:0000313|EMBL:SDC60247.1};
OS   Geotoga petraea.
OC   Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Geotoga.
OX   NCBI_TaxID=28234 {ECO:0000313|EMBL:SDC60247.1, ECO:0000313|Proteomes:UP000199322};
RN   [1] {ECO:0000313|EMBL:SDC60247.1, ECO:0000313|Proteomes:UP000199322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WG14 {ECO:0000313|EMBL:SDC60247.1,
RC   ECO:0000313|Proteomes:UP000199322};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-
CC       tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
CC       {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081415}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) =
CC         (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH;
CC         Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00102, ECO:0000256|SAAS:SAAS01117954};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) =
CC         (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00102, ECO:0000256|SAAS:SAAS01117970};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
CC       {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081412}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00102}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102,
CC       ECO:0000256|SAAS:SAAS01081435}.
CC   -!- SIMILARITY: Belongs to the DapB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00102, ECO:0000256|SAAS:SAAS01081404}.
CC   -!- CAUTION: Was originally thought to be a dihydrodipicolinate
CC       reductase (DHDPR), catalyzing the conversion of
CC       dihydrodipicolinate to tetrahydrodipicolinate. However, it was
CC       shown in E.coli that the substrate of the enzymatic reaction is
CC       not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-
CC       2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by
CC       the DapA-catalyzed reaction. {ECO:0000256|HAMAP-Rule:MF_00102}.
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DR   EMBL; FMYV01000005; SDC60247.1; -; Genomic_DNA.
DR   BioCyc; GCF_900102615:BLS00_RS07025-MONOMER; -.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000199322; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016726; F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor; 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-UniRule.
DR   HAMAP; MF_00102; DapB; 1.
DR   InterPro; IPR022663; DapB_C.
DR   InterPro; IPR000846; DapB_N.
DR   InterPro; IPR022664; DapB_N_CS.
DR   InterPro; IPR023940; DHDPR_bac.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR20836; PTHR20836; 2.
DR   Pfam; PF05173; DapB_C; 1.
DR   Pfam; PF01113; DapB_N; 1.
DR   PIRSF; PIRSF000161; DHPR; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS01298; DAPB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS01081390};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199322};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS01081408};
KW   Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS01081418};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS01081406};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS01081420};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00333002};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00102,
KW   ECO:0000256|SAAS:SAAS00333034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199322}.
FT   DOMAIN        1     98       DapB_N. {ECO:0000259|Pfam:PF01113}.
FT   DOMAIN      101    214       DapB_C. {ECO:0000259|Pfam:PF05173}.
FT   NP_BIND       7     12       NAD(P). {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   NP_BIND      71     73       NAD(P). {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   NP_BIND      95     98       NAD(P). {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   REGION      138    139       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00102}.
FT   ACT_SITE    128    128       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00102}.
FT   ACT_SITE    132    132       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   BINDING      34     34       NAD. {ECO:0000256|HAMAP-Rule:MF_00102}.
FT   BINDING      35     35       NADP. {ECO:0000256|HAMAP-Rule:MF_00102}.
FT   BINDING     129    129       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
SQ   SEQUENCE   216 AA;  24990 MW;  F4BF8276CD202ED5 CRC64;
     MKYGLIGYSG KMGKAIKELF DKNGHKLVYW KDSEKEEEIE KPEIIIDFSI KSAFLETLRI
     IEEKEVPLII GTTGLDENDF EKLREISKKV PVIQSFNFSI GINIMTELLK KMNDFIDDSY
     DIEITETHHR FKKDKPSGTA ILLKNIIDKE VEEIHSKRLG SEFGEHEIEF ATTGEIIKLT
     HRAYSREAFT KGVLLSAKRI NNLENGLYTF KEILMR
//
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