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Entry: A0A087MMA9_9GAMM
LinkDB: A0A087MMA9_9GAMM
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ID   A0A087MMA9_9GAMM        Unreviewed;       245 AA.
AC   A0A087MMA9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   08-MAY-2019, entry version 29.
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=N788_02225 {ECO:0000313|EMBL:KFL38012.1};
OS   Arenimonas donghaensis DSM 18148 = HO3-R19.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Arenimonas.
OX   NCBI_TaxID=1121014 {ECO:0000313|EMBL:KFL38012.1, ECO:0000313|Proteomes:UP000029085};
RN   [1] {ECO:0000313|Proteomes:UP000029085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HO3-R19 {ECO:0000313|Proteomes:UP000029085};
RA   Chen F., Wang G.;
RT   "Genome sequencing of Arenimonas donghaensis.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KFL38012.1, ECO:0000313|Proteomes:UP000029085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HO3-R19 {ECO:0000313|EMBL:KFL38012.1,
RC   ECO:0000313|Proteomes:UP000029085};
RX   PubMed=26380644; DOI=10.1186/s40793-015-0055-4;
RA   Chen F., Wang H., Cao Y., Li X., Wang G.;
RT   "High quality draft genomic sequence of Arenimonas donghaensis DSM
RT   18148(T).";
RL   Stand. Genomic Sci. 10:59-59(2015).
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: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00102}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KFL38012.1}.
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; AVCJ01000001; KFL38012.1; -; Genomic_DNA.
DR   EnsemblBacteria; KFL38012; KFL38012; N788_02225.
DR   PATRIC; fig|1121014.3.peg.419; -.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000029085; 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; 1.
DR   Pfam; PF05173; DapB_C; 1.
DR   Pfam; PF01113; DapB_N; 1.
DR   PIRSF; PIRSF000161; DHPR; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00036; dapB; 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:UP000029085};
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:UP000029085}.
FT   DOMAIN        7    121       DapB_N. {ECO:0000259|Pfam:PF01113}.
FT   DOMAIN      124    239       DapB_C. {ECO:0000259|Pfam:PF05173}.
FT   NP_BIND      12     17       NAD(P). {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   NP_BIND      94     96       NAD(P). {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   NP_BIND     118    121       NAD(P). {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   REGION      160    161       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00102}.
FT   ACT_SITE    150    150       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00102}.
FT   ACT_SITE    154    154       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
FT   BINDING      39     39       NADP. {ECO:0000256|HAMAP-Rule:MF_00102}.
FT   BINDING     151    151       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00102}.
SQ   SEQUENCE   245 AA;  25574 MW;  1EF13374BE093534 CRC64;
     MDQAKPRLLI HGASGRMGRA LLRLAAERPE LQLVAAVSRS GEPLAEAPDG VPVLPVARLA
     EVPDFDVAVD FSLPEAFEPL VAACRAKGAA LVSGTTGLSP GQLEALDEAS ELMPVLWSAN
     FSVGVAVLRV LVHQAAAALP AWDADIVESH HVHKKDAPSG TALSLGAMVA LGRGSQPHYA
     SLRCGDVVGE HLVQFAGPGE RLELVHRATD RDIFARGALE AAVRLAGKGP GRYDFGELLL
     ASGRT
//
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