DAPB_COXBU
ID DAPB_COXBU Reviewed; 239 AA.
AC P24703;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 143.
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=CBU_1709;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hamilton;
RX PubMed=1500190; DOI=10.1128/iai.60.9.3814-3823.1992;
RA Heinzen R.A., Frazier M.E., Mallavia L.P.;
RT "Coxiella burnetii superoxide dismutase gene: cloning, sequencing, and
RT expression in Escherichia coli.";
RL Infect. Immun. 60:3814-3823(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M74242; AAA23312.1; -; Genomic_DNA.
DR EMBL; AE016828; AAO91204.1; -; Genomic_DNA.
DR PIR; B44791; B44791.
DR RefSeq; NP_820690.1; NC_002971.3.
DR RefSeq; WP_005770530.1; NC_002971.4.
DR PDB; 5WOL; X-ray; 1.70 A; A=1-239.
DR PDBsum; 5WOL; -.
DR AlphaFoldDB; P24703; -.
DR SMR; P24703; -.
DR STRING; 227377.CBU_1709; -.
DR EnsemblBacteria; AAO91204; AAO91204; CBU_1709.
DR GeneID; 1209620; -.
DR KEGG; cbu:CBU_1709; -.
DR PATRIC; fig|227377.7.peg.1695; -.
DR eggNOG; COG0289; Bacteria.
DR HOGENOM; CLU_047479_0_1_6; -.
DR OMA; TLCHSAH; -.
DR UniPathway; UPA00034; UER00018.
DR Proteomes; UP000002671; 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..239
FT /note="4-hydroxy-tetrahydrodipicolinate reductase"
FT /id="PRO_0000141436"
FT ACT_SITE 134
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT ACT_SITE 138
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 9..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 78..80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 104..107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 135
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 144..145
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT CONFLICT 56
FT /note="T -> S (in Ref. 1; AAA23312)"
FT /evidence="ECO:0000305"
FT CONFLICT 159..239
FT /note="SKKDEPFKDRARGEIKNGIPIHSIRLPGLFSHQSVIFGSNGETLTIRHDGMD
FT RNCTMPGIFMACRKVMELDYLVYGLENLL -> HPHQDAAEKSSR (in Ref. 1;
FT AAA23312)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:5WOL"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:5WOL"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:5WOL"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:5WOL"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:5WOL"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:5WOL"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:5WOL"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:5WOL"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:5WOL"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:5WOL"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:5WOL"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:5WOL"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:5WOL"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:5WOL"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5WOL"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:5WOL"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5WOL"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:5WOL"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:5WOL"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:5WOL"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:5WOL"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:5WOL"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:5WOL"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:5WOL"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:5WOL"
SQ SEQUENCE 239 AA; 26232 MW; CA2EC05270BE4CAD CRC64;
MAINVIINGI NGKMGRVVKE NITAQSDLEL VSGTGRQDDL AKTIQTTHAD VVIDFTTPQS
VFHNAEIIIQ SGARPVIGTT GLTLEQIALL DKQCRNKKLG AIVAPNFSVG AVLMMKYAKE
AAHYFPDVEI IEMHHSQKID APSGTAIKTA QMIGEMRSSK KDEPFKDRAR GEIKNGIPIH
SIRLPGLFSH QSVIFGSNGE TLTIRHDGMD RNCTMPGIFM ACRKVMELDY LVYGLENLL
