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Entry: A0A1Z4UZ96_9CYAN
LinkDB: A0A1Z4UZ96_9CYAN
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ID   A0A1Z4UZ96_9CYAN        Unreviewed;       278 AA.
AC   A0A1Z4UZ96;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|ARBA:ARBA00038983, ECO:0000256|HAMAP-Rule:MF_00102};
DE            Short=HTPA reductase {ECO:0000256|HAMAP-Rule:MF_00102};
DE            EC=1.17.1.8 {ECO:0000256|ARBA:ARBA00038983, ECO:0000256|HAMAP-Rule:MF_00102};
GN   Name=dapB {ECO:0000256|HAMAP-Rule:MF_00102};
GN   ORFNames=NIES806_07670 {ECO:0000313|EMBL:BAZ84577.1};
OS   Dolichospermum compactum NIES-806.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC   Dolichospermum; Dolichospermum compactum.
OX   NCBI_TaxID=1973481 {ECO:0000313|EMBL:BAZ84577.1, ECO:0000313|Proteomes:UP000218702};
RN   [1] {ECO:0000313|EMBL:BAZ84577.1, ECO:0000313|Proteomes:UP000218702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-806 {ECO:0000313|EMBL:BAZ84577.1,
RC   ECO:0000313|Proteomes:UP000218702};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate
CC       (HTPA) to tetrahydrodipicolinate. {ECO:0000256|HAMAP-Rule:MF_00102}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00102};
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, ECO:0000256|HAMAP-
CC         Rule:MF_00102};
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, ECO:0000256|HAMAP-Rule:MF_00102}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00102}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102}.
CC   -!- SIMILARITY: Belongs to the DapB family. {ECO:0000256|ARBA:ARBA00006642,
CC       ECO:0000256|HAMAP-Rule:MF_00102}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00102}.
CC   -!- CAUTION: Was originally thought to be a dihydrodipicolinate reductase
CC       (DHDPR), catalyzing the conversion of dihydrodipicolinate to
CC       tetrahydrodipicolinate. However, it was shown in E.coli that the
CC       substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP)
CC       but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid
CC       (HTPA), the product released by the DapA-catalyzed reaction.
CC       {ECO:0000256|HAMAP-Rule:MF_00102}.
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DR   EMBL; AP018316; BAZ84577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z4UZ96; -.
DR   OrthoDB; 9790352at2; -.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000218702; Chromosome.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   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.
DR   PROSITE; PS01298; DAPB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00102};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00102};
KW   Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915,
KW   ECO:0000256|HAMAP-Rule:MF_00102};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW   Rule:MF_00102};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00102};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00102};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00102}.
FT   DOMAIN          7..140
FT                   /note="Dihydrodipicolinate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01113"
FT   DOMAIN          143..278
FT                   /note="Dihydrodipicolinate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05173"
FT   ACT_SITE        167
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT   ACT_SITE        171
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT   BINDING         13..18
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT   BINDING         111..113
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT   BINDING         168
FT                   /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT                   /ligand_id="ChEBI:CHEBI:16845"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT   BINDING         177..178
FT                   /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT                   /ligand_id="ChEBI:CHEBI:16845"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
SQ   SEQUENCE   278 AA;  29716 MW;  5406C7DA7875758D CRC64;
     MSNQTSIPVI VNGAAGKMGR EVIKAVAEAS DLTLMGAIDT TPEHQGKDAG ELAGLSEPLE
     VPITNQLEPM LAYVAGERQM QPGVLVDFTH PDAVYNNIRS AIAYGIRPVV GTTGLSPAQL
     EELADFAEKA STGCLVIPNF SIGMVLLQEA ALRASQYFDH VEIIELHHNQ KADAPSGTAI
     QTAQLLAEMG KTFNTAIVVE TEKIPGARGS LADEGIRIHS VRLPGLIAHQ EVIFGAAGQI
     YTLRHDTSDR ACYMPGVILA IRKVNQLKSL VYGLEKIL
//
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