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DAPB_MYCTO
ID   DAPB_MYCTO              Reviewed;         245 AA.
AC   P9WP22; L0TDI3; O33315; P72024;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000255|HAMAP-Rule:MF_00102};
DE            Short=HTPA reductase {ECO:0000255|HAMAP-Rule:MF_00102};
DE            EC=1.17.1.8 {ECO:0000255|HAMAP-Rule:MF_00102};
GN   Name=dapB {ECO:0000255|HAMAP-Rule:MF_00102}; OrderedLocusNames=MT2843;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate
CC       (HTPA) to tetrahydrodipicolinate. {ECO:0000255|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; Evidence={ECO:0000255|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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00102}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00102}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00102}.
CC   -!- SIMILARITY: Belongs to the DapB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00102}.
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DR   EMBL; AE000516; AAK47162.1; -; Genomic_DNA.
DR   PIR; D70882; D70882.
DR   RefSeq; WP_003414099.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WP22; -.
DR   SMR; P9WP22; -.
DR   EnsemblBacteria; AAK47162; AAK47162; MT2843.
DR   GeneID; 45426762; -.
DR   KEGG; mtc:MT2843; -.
DR   PATRIC; fig|83331.31.peg.3066; -.
DR   HOGENOM; CLU_047479_0_1_11; -.
DR   UniPathway; UPA00034; UER00018.
DR   Proteomes; UP000001020; 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   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; Cytoplasm; Diaminopimelate biosynthesis;
KW   Lysine biosynthesis; NAD; NADP; Oxidoreductase.
FT   CHAIN           1..245
FT                   /note="4-hydroxy-tetrahydrodipicolinate reductase"
FT                   /id="PRO_0000427027"
FT   ACT_SITE        132
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   ACT_SITE        136
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         7..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         75..77
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         102..105
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         133
FT                   /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT                   /ligand_id="ChEBI:CHEBI:16845"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT   BINDING         142..143
FT                   /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT                   /ligand_id="ChEBI:CHEBI:16845"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
SQ   SEQUENCE   245 AA;  25733 MW;  CDB8273AFFD4C095 CRC64;
     MRVGVLGAKG KVGATMVRAV AAADDLTLSA ELDAGDPLSL LTDGNTEVVI DFTHPDVVMG
     NLEFLIDNGI HAVVGTTGFT AERFQQVESW LVAKPNTSVL IAPNFAIGAV LSMHFAKQAA
     RFFDSAEVIE LHHPHKADAP SGTAARTAKL IAEARKGLPP NPDATSTSLP GARGADVDGI
     PVHAVRLAGL VAHQEVLFGT EGETLTIRHD SLDRTSFVPG VLLAVRRIAE RPGLTVGLEP
     LLDLH
 
 
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