DAPB_PSEAE
ID DAPB_PSEAE Reviewed; 268 AA.
AC P38103;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 144.
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=PA4759;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-268.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8169201; DOI=10.1128/jb.176.9.2532-2542.1994;
RA Kwon D.-H., Lu C.-D., Walthall D.A., Brown T.M., Houghton J.E.,
RA Abdelal A.T.;
RT "Structure and regulation of the carAB operon in Pseudomonas aeruginosa and
RT Pseudomonas stutzeri: no untranslated region exists.";
RL J. Bacteriol. 176:2532-2542(1994).
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 -!- 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; AE004091; AAG08145.1; -; Genomic_DNA.
DR EMBL; U04992; AAA19045.1; -; Unassigned_DNA.
DR EMBL; U81259; AAB39249.1; -; Genomic_DNA.
DR PIR; A55580; A55580.
DR PIR; H83051; H83051.
DR RefSeq; NP_253447.1; NC_002516.2.
DR RefSeq; WP_003095210.1; NZ_QZGE01000018.1.
DR PDB; 4YWJ; X-ray; 1.80 A; A/B=1-268.
DR PDBsum; 4YWJ; -.
DR AlphaFoldDB; P38103; -.
DR SMR; P38103; -.
DR STRING; 287.DR97_2103; -.
DR PaxDb; P38103; -.
DR PRIDE; P38103; -.
DR EnsemblBacteria; AAG08145; AAG08145; PA4759.
DR GeneID; 881759; -.
DR KEGG; pae:PA4759; -.
DR PATRIC; fig|208964.12.peg.4985; -.
DR PseudoCAP; PA4759; -.
DR HOGENOM; CLU_047479_2_1_6; -.
DR InParanoid; P38103; -.
DR OMA; HHPNKAD; -.
DR PhylomeDB; P38103; -.
DR BioCyc; PAER208964:G1FZ6-4872-MON; -.
DR UniPathway; UPA00034; UER00018.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..268
FT /note="4-hydroxy-tetrahydrodipicolinate reductase"
FT /id="PRO_0000141468"
FT ACT_SITE 156
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 8..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 99..101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 123..126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 157
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 166..167
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..8
FT /evidence="ECO:0007829|PDB:4YWJ"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:4YWJ"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:4YWJ"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:4YWJ"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:4YWJ"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:4YWJ"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:4YWJ"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4YWJ"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:4YWJ"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:4YWJ"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:4YWJ"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:4YWJ"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:4YWJ"
FT HELIX 128..144
FT /evidence="ECO:0007829|PDB:4YWJ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:4YWJ"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:4YWJ"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:4YWJ"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:4YWJ"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:4YWJ"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:4YWJ"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:4YWJ"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:4YWJ"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:4YWJ"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:4YWJ"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:4YWJ"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:4YWJ"
SQ SEQUENCE 268 AA; 28324 MW; 0B37EAF688419254 CRC64;
MRRIAVVGAA GRMGKNLIEA VQQTGGAAGL TAAVDRPDST LVGADAGELA GLGRIGVPLS
GDLGKVCEEF DVLIDFTHPS VTLKNIEQCR KARRAMVIGT TGFSADEKLL LAEAAKDIPI
VFAANFSVGV NLCLKLLDTA ARVLGDEVDI EIIEAHHRHK VDAPSGTALR MGEVVAQALG
RDLQEVAVYG REGQTGARAR ETIGFATVRA GDVVGDHTVL FAAEGERVEI THKASSRMTF
ARGAVRAALW LEGKENGLYD MQDVLGLR
