ID D4MZG3_ANAHA Unreviewed; 251 AA.
AC D4MZG3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|HAMAP-Rule:MF_00102};
DE Short=HTPA reductase {ECO:0000256|HAMAP-Rule:MF_00102};
DE EC=1.17.1.8 {ECO:0000256|HAMAP-Rule:MF_00102};
GN Name=dapB {ECO:0000256|HAMAP-Rule:MF_00102,
GN ECO:0000313|EMBL:CUM79325.1};
GN ORFNames=CL2_10030 {ECO:0000313|EMBL:CBL38008.1}, DO83_12675
GN {ECO:0000313|EMBL:AQP40347.1}, ERS852425_00910
GN {ECO:0000313|EMBL:CUM83368.1}, ERS852520_03122
GN {ECO:0000313|EMBL:CUQ12578.1}, ERS852571_00603
GN {ECO:0000313|EMBL:CUM79325.1};
OS Anaerostipes hadrus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL38008.1, ECO:0000313|Proteomes:UP000008960};
RN [1] {ECO:0000313|EMBL:CBL38008.1, ECO:0000313|Proteomes:UP000008960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38008.1,
RC ECO:0000313|Proteomes:UP000008960};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SSC/2.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL38008.1, ECO:0000313|Proteomes:UP000008960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38008.1,
RC ECO:0000313|Proteomes:UP000008960};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000095553, ECO:0000313|Proteomes:UP000095564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608868 {ECO:0000313|EMBL:CUM83368.1,
RC ECO:0000313|Proteomes:UP000095598}, 2789STDY5834908
RC {ECO:0000313|EMBL:CUQ12578.1, ECO:0000313|Proteomes:UP000095564}, and
RC 2789STDY5834959 {ECO:0000313|EMBL:CUM79325.1,
RC ECO:0000313|Proteomes:UP000095553};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AQP40347.1, ECO:0000313|Proteomes:UP000188159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPB5 {ECO:0000313|EMBL:AQP40347.1,
RC ECO:0000313|Proteomes:UP000188159};
RX PubMed=27264309; DOI=10.1038/srep27572;
RA Zhang Q., Wu Y., Wang J., Wu G., Long W., Xue Z., Wang L., Zhang X.,
RA Pang X., Zhao Y., Zhao L., Zhang C.;
RT "Accelerated dysbiosis of gut microbiota during aggravation of DSS-induced
RT colitis by a butyrate-producing bacterium.";
RL Sci. Rep. 6:27572-27572(2016).
CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate
CC (HTPA) to tetrahydrodipicolinate. {ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00102}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00102}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00102}.
CC -!- SIMILARITY: Belongs to the DapB family. {ECO:0000256|ARBA:ARBA00006642,
CC ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_00102}.
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DR EMBL; CP012098; AQP40347.1; -; Genomic_DNA.
DR EMBL; FP929061; CBL38008.1; -; Genomic_DNA.
DR EMBL; CYXY01000003; CUM79325.1; -; Genomic_DNA.
DR EMBL; CYXT01000004; CUM83368.1; -; Genomic_DNA.
DR EMBL; CZAU01000043; CUQ12578.1; -; Genomic_DNA.
DR RefSeq; WP_008392033.1; NZ_WQRB01000044.1.
DR AlphaFoldDB; D4MZG3; -.
DR STRING; 649756.ERS852387_02378; -.
DR GeneID; 15231099; -.
DR KEGG; bprl:CL2_10030; -.
DR PATRIC; fig|245018.3.peg.1244; -.
DR OrthoDB; 9790352at2; -.
DR UniPathway; UPA00034; UER00018.
DR Proteomes; UP000008960; Chromosome.
DR Proteomes; UP000095553; Unassembled WGS sequence.
DR Proteomes; UP000095564; Unassembled WGS sequence.
DR Proteomes; UP000095598; Unassembled WGS sequence.
DR Proteomes; UP000188159; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 NCBIfam; TIGR00036; dapB; 1.
DR PANTHER; PTHR20836:SF7; 4-HYDROXY-TETRAHYDRODIPICOLINATE REDUCTASE; 1.
DR PANTHER; PTHR20836; DIHYDRODIPICOLINATE REDUCTASE; 1.
DR Pfam; PF05173; DapB_C; 1.
DR Pfam; PF01113; DapB_N; 1.
DR PIRSF; PIRSF000161; DHPR; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01298; DAPB; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00102};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00102};
KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915,
KW ECO:0000256|HAMAP-Rule:MF_00102};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW Rule:MF_00102};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00102};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00102};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00102,
KW ECO:0000313|EMBL:CBL38008.1}.
FT DOMAIN 2..112
FT /note="Dihydrodipicolinate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01113"
FT DOMAIN 115..250
FT /note="Dihydrodipicolinate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05173"
FT ACT_SITE 143
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 8..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 85..87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 109..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 144
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
FT BINDING 153..154
FT /ligand="(S)-2,3,4,5-tetrahydrodipicolinate"
FT /ligand_id="ChEBI:CHEBI:16845"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00102"
SQ SEQUENCE 251 AA; 27228 MW; A0A3CD3796169F55 CRC64;
MVKIMMHGCN GVMGQVISKI VEETEGAVMA CGVDRVDDGH NDYPVFTDIN ACDVEVDAII
DFSAAPAVDG LLDFAVERQI PVVLCTTGLS DEQLERVHEA SKKTAVLRSA NMSLGVNTLF
KVLKSMTKLL ADAGFDIDIV EKHHRRKLDA PSGTAIALAE AVNEPLNNEY EFVYDRSQRR
EQRPKKEIGI SAVRGGTIVG EHEIIFAGQD EVIELKHTAY SRAIFGKGAV SAALYLAGKE
AGMYDMSDVI G
//
