DAPB_CORGL
ID DAPB_CORGL Reviewed; 248 AA.
AC P40110; P42462;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 146.
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};
GN OrderedLocusNames=Cgl1973, cg2163;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RA Eikmanns B.J., Eggeling L., Thum-Schmitz N., Krumbach K.;
RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=8478336; DOI=10.1128/jb.175.9.2743-2749.1993;
RA Pisabarro A., Malumbres M., Mateos L.M., Oguiza J.A., Martin J.F.;
RT "A cluster of three genes (dapA, orf2, and dapB) of Brevibacterium
RT lactofermentum encodes dihydrodipicolinate synthase, dihydrodipicolinate
RT reductase, and a third polypeptide of unknown function.";
RL J. Bacteriol. 175:2743-2749(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(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}.
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DR EMBL; X67737; CAA47968.1; -; Genomic_DNA.
DR EMBL; Z21502; CAA79712.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99366.1; -; Genomic_DNA.
DR EMBL; BX927153; CAF20314.1; -; Genomic_DNA.
DR PIR; A40626; A40626.
DR RefSeq; NP_601179.1; NC_003450.3.
DR RefSeq; WP_011014794.1; NC_006958.1.
DR PDB; 5EER; X-ray; 2.50 A; A=2-248.
DR PDB; 5EES; X-ray; 2.15 A; A=2-248.
DR PDBsum; 5EER; -.
DR PDBsum; 5EES; -.
DR AlphaFoldDB; P40110; -.
DR SMR; P40110; -.
DR STRING; 196627.cg2163; -.
DR KEGG; cgb:cg2163; -.
DR KEGG; cgl:Cgl1973; -.
DR PATRIC; fig|196627.13.peg.1910; -.
DR eggNOG; COG0289; Bacteria.
DR HOGENOM; CLU_047479_0_1_11; -.
DR OMA; HHPNKAD; -.
DR BioCyc; MetaCyc:MON-6445; -.
DR BRENDA; 1.17.1.8; 960.
DR UniPathway; UPA00034; UER00018.
DR Proteomes; UP000000582; 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 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..248
FT /note="4-hydroxy-tetrahydrodipicolinate reductase"
FT /id="PRO_0000141435"
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 77..79
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 91
FT /note="D -> A (in Ref. 2; CAA79712)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:5EES"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:5EES"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:5EES"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:5EES"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5EER"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:5EES"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:5EES"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:5EES"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:5EES"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:5EES"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:5EES"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:5EES"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:5EES"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:5EES"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5EES"
FT HELIX 144..159
FT /evidence="ECO:0007829|PDB:5EES"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:5EES"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5EES"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:5EES"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:5EES"
FT STRAND 207..218
FT /evidence="ECO:0007829|PDB:5EES"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:5EES"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:5EES"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:5EES"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:5EES"
SQ SEQUENCE 248 AA; 26024 MW; A0B143F478D12414 CRC64;
MGIKVGVLGA KGRVGQTIVA AVNESDDLEL VAEIGVDDDL SLLVDNGAEV VVDFTTPNAV
MGNLEFCINN GISAVVGTTG FDDARLEQVR DWLEGKDNVG VLIAPNFAIS AVLTMVFSKQ
AARFFESAEV IELHHPNKLD APSGTAIHTA QGIAAARKEA GMDAQPDATE QALEGSRGAS
VDGIPVHAVR MSGMVAHEQV IFGTQGQTLT IKQDSYDRNS FAPGVLVGVR NIAQHPGLVV
GLEHYLGL
