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Database: UniProt
Entry: A0A0Q5QSJ8_9FLAO
LinkDB: A0A0Q5QSJ8_9FLAO
Original site: A0A0Q5QSJ8_9FLAO 
ID   A0A0Q5QSJ8_9FLAO        Unreviewed;       266 AA.
AC   A0A0Q5QSJ8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|ARBA:ARBA00038983};
DE            EC=1.17.1.8 {ECO:0000256|ARBA:ARBA00038983};
GN   ORFNames=ASG01_00025 {ECO:0000313|EMBL:KQR95621.1};
OS   Chryseobacterium sp. Leaf180.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1736289 {ECO:0000313|EMBL:KQR95621.1, ECO:0000313|Proteomes:UP000051405};
RN   [1] {ECO:0000313|EMBL:KQR95621.1, ECO:0000313|Proteomes:UP000051405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf180 {ECO:0000313|EMBL:KQR95621.1,
RC   ECO:0000313|Proteomes:UP000051405};
RX   PubMed=26633631; DOI=.1038/nature16192;
RA   Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA   Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA   McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL   Nature 528:364-369(2015).
RN   [2] {ECO:0000313|Proteomes:UP000051405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf180 {ECO:0000313|Proteomes:UP000051405};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000051405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf180 {ECO:0000313|Proteomes:UP000051405};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-
CC         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;
CC         Evidence={ECO:0000256|ARBA:ARBA00036290};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-
CC         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;
CC         Evidence={ECO:0000256|ARBA:ARBA00036097};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00037922}.
CC   -!- SIMILARITY: Belongs to the DapB family.
CC       {ECO:0000256|ARBA:ARBA00006642}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQR95621.1}.
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DR   EMBL; LMPJ01000001; KQR95621.1; -; Genomic_DNA.
DR   RefSeq; WP_055861967.1; NZ_LMPJ01000001.1.
DR   AlphaFoldDB; A0A0Q5QSJ8; -.
DR   STRING; 1736289.ASG01_00025; -.
DR   OrthoDB; 9790352at2; -.
DR   Proteomes; UP000051405; Unassembled WGS sequence.
DR   GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR022663; DapB_C.
DR   InterPro; IPR000846; DapB_N.
DR   InterPro; IPR023940; DHDPR_bac.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00036; dapB; 1.
DR   PANTHER; PTHR20836:SF0; 4-HYDROXY-TETRAHYDRODIPICOLINATE REDUCTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR20836; DIHYDRODIPICOLINATE REDUCTASE; 1.
DR   Pfam; PF05173; DapB_C; 1.
DR   Pfam; PF01113; DapB_N; 1.
DR   PIRSF; PIRSF000161; DHPR; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051405}.
FT   DOMAIN          2..126
FT                   /note="Dihydrodipicolinate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01113"
FT   DOMAIN          130..255
FT                   /note="Dihydrodipicolinate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05173"
SQ   SEQUENCE   266 AA;  29060 MW;  BCFB372C494A2D97 CRC64;
     MIKVCIAGGT GWAGSELSKG VFKHPNMELV GAISRKHKGE NLGNVLKLGY ADIPIFGDIE
     TALKEIDFDV LVEYTKPDIA KKNIVSCLKK GKNVVIGTSG LTDEDYSEIE KTTDENNASV
     LAVGNFAITV VLLQKFSEMA AKYIPNFEII DYAQEDKIDA PSGTARELAY RLSKVQKPNQ
     YVTEEDLIGE KASRGAKLNE VQVHSVRLPG HVISIETIFG LKDERLSIRH DSGSSAEPYV
     KGGLLAIEKV GTFKGLRRGL DSVMEF
//
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