DAPB_AROAE
ID DAPB_AROAE Reviewed; 276 AA.
AC Q5P1G6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=AZOSEA27230;
GN ORFNames=ebA4812;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(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 -!- 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; CR555306; CAI08848.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5P1G6; -.
DR SMR; Q5P1G6; -.
DR STRING; 76114.ebA4812; -.
DR EnsemblBacteria; CAI08848; CAI08848; ebA4812.
DR KEGG; eba:ebA4812; -.
DR eggNOG; COG0289; Bacteria.
DR HOGENOM; CLU_047479_2_1_4; -.
DR OMA; HHPNKAD; -.
DR UniPathway; UPA00034; UER00018.
DR Proteomes; UP000006552; 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; Reference proteome.
FT CHAIN 1..276
FT /note="4-hydroxy-tetrahydrodipicolinate reductase"
FT /id="PRO_0000228320"
FT ACT_SITE 164
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT ACT_SITE 168
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 18..23
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 107..109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 131..134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 165
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 174..175
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
SQ SEQUENCE 276 AA; 28962 MW; F2138D20D2FFF1B4 CRC64;
MSSKRNSLML PLRIAIAGAS GRMGRMLIEA TLKEEGAVLA SAFDRPGTTF IGRDAGELSG
SATGILITDD PRAAIAAADC VIDFTRPEGT LAHLALAREL GKAMVIGTTG FSTAEKEAIA
AAAQAIPIVF APNMAVGVNA VFKLLEVAAR ILDDGYDVEV IEAHHRFKVD APSGTALRMG
EVVACELGRD LETCAIYGRE GVTGERKAET IGFSTIRGGD VVGDHTVLFA GIGERIEITH
RSGSRMPYAS GSLRAARFLA GRSSGLFDMQ DVLGLR
