DAPH_CLOBA
ID DAPH_CLOBA Reviewed; 236 AA.
AC B2V5B7;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01691};
DE EC=2.3.1.89 {ECO:0000255|HAMAP-Rule:MF_01691};
DE AltName: Full=Tetrahydrodipicolinate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01691};
DE Short=THP acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01691};
DE Short=Tetrahydropicolinate acetylase {ECO:0000255|HAMAP-Rule:MF_01691};
GN Name=dapH {ECO:0000255|HAMAP-Rule:MF_01691}; OrderedLocusNames=CLH_2265;
OS Clostridium botulinum (strain Alaska E43 / Type E3).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=508767;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alaska E43 / Type E3;
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of an acetyl group from acetyl-CoA to
CC tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_01691}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + acetyl-CoA + H2O = CoA +
CC L-2-acetamido-6-oxoheptanedioate; Xref=Rhea:RHEA:13085,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:58117; EC=2.3.1.89;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01691};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC (acetylase route): step 1/3. {ECO:0000255|HAMAP-Rule:MF_01691}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. DapH
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01691}.
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; CP001078; ACD53028.1; -; Genomic_DNA.
DR RefSeq; WP_003373203.1; NC_010723.1.
DR AlphaFoldDB; B2V5B7; -.
DR SMR; B2V5B7; -.
DR KEGG; cbt:CLH_2265; -.
DR HOGENOM; CLU_103751_0_0_9; -.
DR OMA; HLEYDRR; -.
DR OrthoDB; 752123at2; -.
DR UniPathway; UPA00034; UER00022.
DR GO; GO:0047200; F:tetrahydrodipicolinate N-acetyltransferase activity; IEA:UniProtKB-EC.
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_01691; DapH; 1.
DR InterPro; IPR019873; DapH.
DR InterPro; IPR013710; DapH_N.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF08503; DapH_N; 1.
DR Pfam; PF00132; Hexapep; 3.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR03532; DapD_Ac; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Diaminopimelate biosynthesis;
KW Lysine biosynthesis; Repeat; Transferase.
FT CHAIN 1..236
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT acetyltransferase"
FT /id="PRO_0000376644"
SQ SEQUENCE 236 AA; 25002 MW; 8EA0AB0A6126708F CRC64;
MSYNLTDPYE IARFIKESKK STPVKVYVNG DLSEALMDDI EWYGANGFYI LIGESDLVAK
IILDNKHLIK HFRLENDRRN SAIPMLDLLE VEARIEPGAI IRDKVTIGKN AVVMMGAVIN
IGAEIGDGTM VDMNAVIGAR GKLGKNVHLG AGAVVAGVLE PPSKEPCTVG DNVLIGANSV
ILEGVKIGAG SVVAAGSVVA EDVPEGVVVA GSPAKIIKSV DDKTKGKTQL LDDLRK