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4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8)

 A0A1M3L5T4_9BACT        Unreviewed;       250 AA.
A0A1M3L5T4;
15-MAR-2017, integrated into UniProtKB/TrEMBL.
15-MAR-2017, sequence version 1.
10-MAY-2017, entry version 3.
RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|HAMAP-Rule:MF_00102};
Short=HTPA reductase {ECO:0000256|HAMAP-Rule:MF_00102};
EC=1.17.1.8 {ECO:0000256|HAMAP-Rule:MF_00102};
Name=dapB {ECO:0000256|HAMAP-Rule:MF_00102};
ORFNames=BGO89_04710 {ECO:0000313|EMBL:OJX60869.1};
Candidatus Kapabacteria sp. 59-99.
Bacteria; Candidatus Kapabacteria.
NCBI_TaxID=1895771 {ECO:0000313|EMBL:OJX60869.1, ECO:0000313|Proteomes:UP000184233};
[1] {ECO:0000313|EMBL:OJX60869.1, ECO:0000313|Proteomes:UP000184233}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=59-99 {ECO:0000313|EMBL:OJX60869.1};
Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T.,
Anantharaman K., Tringe S., Hettich R.L., Harrison S.T.,
Banfield J.F.;
"Genome-resolved meta-omics ties microbial dynamics to process
performance in biotechnology for thiocyanate degradation.";
Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the conversion of 4-hydroxy-
tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
{ECO:0000256|HAMAP-Rule:MF_00102}.
-!- CATALYTIC ACTIVITY: (S)-2,3,4,5-tetrahydropyridine-2,6-
dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5-
tetrahydrodipicolinate + NAD(P)H. {ECO:0000256|HAMAP-
Rule:MF_00102}.
-!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
{ECO:0000256|HAMAP-Rule:MF_00102}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00102}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102}.
-!- SIMILARITY: Belongs to the DapB family. {ECO:0000256|HAMAP-
Rule:MF_00102, ECO:0000256|SAAS:SAAS00671951}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00102}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:OJX60869.1}.
-!- CAUTION: Was originally thought to be a dihydrodipicolinate
reductase (DHDPR), catalyzing the conversion of
dihydrodipicolinate to tetrahydrodipicolinate. However, it was
shown in E.coli that the substrate of the enzymatic reaction is
not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-
2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by
the DapA-catalyzed reaction. {ECO:0000256|HAMAP-Rule:MF_00102}.
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EMBL; MKVH01000003; OJX60869.1; -; Genomic_DNA.
UniPathway; UPA00034; UER00018.
Proteomes; UP000184233; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:UniProtKB-EC.
GO; GO:0051287; F:NAD binding; IEA:UniProtKB-HAMAP.
GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP.
GO; GO:0016726; F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor; IEA:UniProtKB-HAMAP.
GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP.
GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP.
HAMAP; MF_00102; DapB; 1.
InterPro; IPR022663; DapB_C.
InterPro; IPR000846; DapB_N.
InterPro; IPR023940; DHDPR_bac.
InterPro; IPR016040; NAD(P)-bd_dom.
PANTHER; PTHR20836; PTHR20836; 1.
Pfam; PF05173; DapB_C; 1.
Pfam; PF01113; DapB_N; 1.
PIRSF; PIRSF000161; DHPR; 1.
SUPFAM; SSF51735; SSF51735; 2.
TIGRFAMs; TIGR00036; dapB; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
ECO:0000256|SAAS:SAAS00018109};
Complete proteome {ECO:0000313|Proteomes:UP000184233};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102};
Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
ECO:0000256|SAAS:SAAS00018031};
Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
ECO:0000256|SAAS:SAAS00018109};
NAD {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00018069};
NADP {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00484099};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00102,
ECO:0000256|SAAS:SAAS00484120};
Reference proteome {ECO:0000313|Proteomes:UP000184233}.
DOMAIN 6 106 DapB_N. {ECO:0000259|Pfam:PF01113}.
DOMAIN 109 242 DapB_C. {ECO:0000259|Pfam:PF05173}.
NP_BIND 78 80 NAD(P). {ECO:0000256|HAMAP-
Rule:MF_00102}.
NP_BIND 103 106 NAD(P). {ECO:0000256|HAMAP-
Rule:MF_00102}.
REGION 148 149 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00102}.
ACT_SITE 138 138 Proton donor/acceptor.
{ECO:0000256|HAMAP-Rule:MF_00102}.
ACT_SITE 142 142 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00102}.
BINDING 38 38 NADP. {ECO:0000256|HAMAP-Rule:MF_00102}.
BINDING 139 139 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00102}.
SEQUENCE 250 AA; 27455 MW; 18909F337A0595A3 CRC64;
MPTPTRIALV GHGAMGREIE RLAPQTPCAI TRIYDEARPF DAATVNDDID VVIDFTQPDA
VLATVETAAR HGIDVVIGTT GWMQHMDRVK GICDRHGVGL IHGSNFSVGV QLFFRLVRAA
SILVQDVTEY DVMIHEWHHR RKKDSPSGTA LTMAGIVLDE LDRKTRIVTD AINDTPIAAD
MLHVSSTRGG EIVGRHVLTL DSAADRIELT HDARNRSGFA LGALLAAEWI HGKTGVYDFT
DVFPEIMSQR


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