DAPB_STAAC
ID DAPB_STAAC Reviewed; 240 AA.
AC Q5HG24;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=SACOL1431;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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 -!- INTERACTION:
CC Q5HG24; Q5HG24: dapB; NbExp=3; IntAct=EBI-7045745, EBI-7045745;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00102}.
CC -!- SIMILARITY: Belongs to the DapB family. {ECO:0000255|HAMAP-
CC 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:0000305}.
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DR EMBL; CP000046; AAW38176.1; -; Genomic_DNA.
DR RefSeq; WP_000698235.1; NC_002951.2.
DR PDB; 3QY9; X-ray; 1.80 A; A/B/C/D=1-240.
DR PDBsum; 3QY9; -.
DR AlphaFoldDB; Q5HG24; -.
DR SMR; Q5HG24; -.
DR MINT; Q5HG24; -.
DR EnsemblBacteria; AAW38176; AAW38176; SACOL1431.
DR KEGG; sac:SACOL1431; -.
DR HOGENOM; CLU_047479_2_2_9; -.
DR OMA; ALKACEY; -.
DR BRENDA; 1.17.1.8; 3352.
DR UniPathway; UPA00034; UER00018.
DR Proteomes; UP000000530; 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:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm;
KW Diaminopimelate biosynthesis; Lysine biosynthesis; NAD; NADP;
KW Oxidoreductase.
FT CHAIN 1..240
FT /note="4-hydroxy-tetrahydrodipicolinate reductase"
FT /id="PRO_0000141485"
FT ACT_SITE 135
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT ACT_SITE 139
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 79..81
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 103..106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 136
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 145..146
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3QY9"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:3QY9"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3QY9"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3QY9"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:3QY9"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:3QY9"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:3QY9"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:3QY9"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:3QY9"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:3QY9"
FT HELIX 108..123
FT /evidence="ECO:0007829|PDB:3QY9"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3QY9"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:3QY9"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3QY9"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:3QY9"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3QY9"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:3QY9"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:3QY9"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:3QY9"
FT STRAND 200..211
FT /evidence="ECO:0007829|PDB:3QY9"
FT HELIX 214..227
FT /evidence="ECO:0007829|PDB:3QY9"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:3QY9"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:3QY9"
SQ SEQUENCE 240 AA; 26654 MW; 23051DECF75B8D8D CRC64;
MKILLIGYGA MNQRVARLAE EKGHEIVGVI ENTPKATTPY QQYQHIADVK GADVAIDFSN
PNLLFPLLDE DFHLPLVVAT TGEKEKLLNK LDELSQNMPV FFSANMSYGV HALTKILAAA
VPLLDDFDIE LTEAHHNKKV DAPSGTLEKL YDVIVSLKEN VTPVYDRHEL NEKRQPQDIG
IHSIRGGTIV GEHEVLFAGT DETIQITHRA QSKDIFANGA IQAAERLVNK PNGFYTFDNL
