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

 A5CCS0_ORITB            Unreviewed;       283 AA.
A5CCS0;
12-JUN-2007, integrated into UniProtKB/TrEMBL.
12-JUN-2007, sequence version 1.
25-OCT-2017, entry version 89.
RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00018068};
Short=HTPA reductase {ECO:0000256|HAMAP-Rule:MF_00102};
EC=1.17.1.8 {ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00018030};
Name=dapB {ECO:0000256|HAMAP-Rule:MF_00102,
ECO:0000313|EMBL:CAM79512.1};
OrderedLocusNames=OTBS_0446 {ECO:0000313|EMBL:CAM79512.1};
Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Rickettsiaceae; Rickettsieae; Orientia.
NCBI_TaxID=357244 {ECO:0000313|EMBL:CAM79512.1, ECO:0000313|Proteomes:UP000001565};
[1] {ECO:0000313|EMBL:CAM79512.1, ECO:0000313|Proteomes:UP000001565}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Boryong {ECO:0000313|EMBL:CAM79512.1,
ECO:0000313|Proteomes:UP000001565};
PubMed=17483455; DOI=10.1073/pnas.0611553104;
Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J.,
Koh Y.-S., Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S.,
Kim I.-S.;
"The Orientia tsutsugamushi genome reveals massive proliferation of
conjugative type IV secretion system and host-cell interaction
genes.";
Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(2007).
-!- FUNCTION: Catalyzes the conversion of 4-hydroxy-
tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
{ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00011094}.
-!- 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, ECO:0000256|SAAS:SAAS00018108}.
-!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
{ECO:0000256|HAMAP-Rule:MF_00102, ECO:0000256|SAAS:SAAS00018087}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00102}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102,
ECO:0000256|SAAS:SAAS00018118}.
-!- 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: 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; AM494475; CAM79512.1; -; Genomic_DNA.
RefSeq; WP_011944488.1; NC_009488.1.
STRING; 357244.OTBS_0446; -.
EnsemblBacteria; CAM79512; CAM79512; OTBS_0446.
GeneID; 29642316; -.
KEGG; ots:OTBS_0446; -.
eggNOG; ENOG4105DUK; Bacteria.
eggNOG; COG0289; LUCA.
HOGENOM; HOG000227155; -.
KO; K00215; -.
OMA; RESFMPG; -.
OrthoDB; POG091H01P6; -.
UniPathway; UPA00034; UER00018.
Proteomes; UP000001565; Chromosome.
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-UniRule.
GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
GO; GO:0016726; F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor; IEA:UniProtKB-UniRule.
GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
HAMAP; MF_00102; DapB; 1.
InterPro; IPR022663; DapB_C.
InterPro; IPR000846; DapB_N.
InterPro; IPR022664; DapB_N_CS.
InterPro; IPR023940; DHDPR_bac.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR20836; PTHR20836; 1.
Pfam; PF05173; DapB_C; 1.
Pfam; PF01113; DapB_N; 1.
PIRSF; PIRSF000161; DHPR; 2.
SUPFAM; SSF51735; SSF51735; 2.
PROSITE; PS01298; DAPB; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00102,
ECO:0000256|SAAS:SAAS00018109};
Complete proteome {ECO:0000313|Proteomes:UP000001565};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102,
ECO:0000256|SAAS:SAAS00018059};
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, ECO:0000313|EMBL:CAM79512.1};
Reference proteome {ECO:0000313|Proteomes:UP000001565}.
DOMAIN 8 111 DapB_N. {ECO:0000259|Pfam:PF01113}.
DOMAIN 115 278 DapB_C. {ECO:0000259|Pfam:PF05173}.
NP_BIND 14 19 NAD(P). {ECO:0000256|HAMAP-
Rule:MF_00102}.
NP_BIND 84 86 NAD(P). {ECO:0000256|HAMAP-
Rule:MF_00102}.
NP_BIND 108 111 NAD(P). {ECO:0000256|HAMAP-
Rule:MF_00102}.
REGION 151 152 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00102}.
ACT_SITE 141 141 Proton donor/acceptor.
{ECO:0000256|HAMAP-Rule:MF_00102}.
ACT_SITE 145 145 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00102}.
BINDING 142 142 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00102}.
SEQUENCE 283 AA; 31449 MW; D79757EDD2DB18FD CRC64;
MIENSAVIRV GVCGASGRMG QEVTKIINNQ AQYQLSATHS SQDDEGNLSL LCQKSDVVID
FSAIDVLPQL LHHAKKNMVP LVIGTTGLSK EHEYLMRETS NSVPIFYSPN MSLAANVMNI
MIEKIARLLN PGYDVEIIEM HHKSKVDIPS GTAIMLGKAV AKGRNIKQNH AAYFEQNAEL
QQNENDNDFQ LTENSAHNFT IDKQKKNCTT KKNDIGFSSI RAGEMPCRHE VMFIGQDDIL
SVQHQSMNRS LFAKGALTAA EWLLGRNKIG LYSFIDLLNS NLE


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