DAPB_TRIV2
ID DAPB_TRIV2 Reviewed; 278 AA.
AC Q3MFY8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=Ava_0474;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA20098.1; -; Genomic_DNA.
DR PDB; 5KT0; X-ray; 2.83 A; A=2-278.
DR PDBsum; 5KT0; -.
DR AlphaFoldDB; Q3MFY8; -.
DR SMR; Q3MFY8; -.
DR STRING; 240292.Ava_0474; -.
DR EnsemblBacteria; ABA20098; ABA20098; Ava_0474.
DR KEGG; ava:Ava_0474; -.
DR eggNOG; COG0289; Bacteria.
DR HOGENOM; CLU_047479_0_1_3; -.
DR OMA; HHPNKAD; -.
DR BRENDA; 4.3.3.7; 322.
DR UniPathway; UPA00034; UER00018.
DR Proteomes; UP000002533; 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.
FT CHAIN 1..278
FT /note="4-hydroxy-tetrahydrodipicolinate reductase"
FT /id="PRO_1000057677"
FT ACT_SITE 167
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 13..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 111..113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 168
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT BINDING 177..178
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00102"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:5KT0"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:5KT0"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:5KT0"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:5KT0"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:5KT0"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:5KT0"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:5KT0"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:5KT0"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5KT0"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:5KT0"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:5KT0"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:5KT0"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:5KT0"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5KT0"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:5KT0"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:5KT0"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:5KT0"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:5KT0"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:5KT0"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:5KT0"
FT STRAND 239..250
FT /evidence="ECO:0007829|PDB:5KT0"
FT HELIX 254..264
FT /evidence="ECO:0007829|PDB:5KT0"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:5KT0"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:5KT0"
SQ SEQUENCE 278 AA; 29464 MW; F02D1FF0D93EBD6B CRC64;
MTNQAPIPVI VNGAAGKMGR EVVKAIAQAP DLNLLGAIDS SPEHQGKDAG ELAGLSEPLE
VPITNQLEPM LGYVAGERQG PPGVIVDFTH PDSVYDNVRS AIAYGIRPVV GTTGLSPAQI
QNLADFAEKA STGCLIIPNF SIGMVLLQQA AVTASQYFDH VEIIELHHNQ KADAPSGTAI
QTAELLAELG KTFNSAIVEE TEKIPGARGS LAGEGIRIHS VRLPGLIAHQ EVIFGAPGQI
YTLRHDTSDR ACYMPGVLLA IRKVLQLKSL VYGLEKIL
