DAPH_CLOB8
ID DAPH_CLOB8 Reviewed; 236 AA.
AC A6LUD2;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Cbei_1791;
OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS acetobutylicum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=290402;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA Blaschek H., Richardson P.;
RT "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL Submitted (JUN-2007) 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}.
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DR EMBL; CP000721; ABR33962.1; -; Genomic_DNA.
DR RefSeq; WP_011969114.1; NC_009617.1.
DR AlphaFoldDB; A6LUD2; -.
DR SMR; A6LUD2; -.
DR STRING; 290402.Cbei_1791; -.
DR EnsemblBacteria; ABR33962; ABR33962; Cbei_1791.
DR GeneID; 66344685; -.
DR KEGG; cbe:Cbei_1791; -.
DR eggNOG; COG2171; Bacteria.
DR HOGENOM; CLU_103751_0_0_9; -.
DR OMA; HLEYDRR; -.
DR OrthoDB; 752123at2; -.
DR UniPathway; UPA00034; UER00022.
DR Proteomes; UP000000565; Chromosome.
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; 2.
DR Pfam; PF14602; Hexapep_2; 1.
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_0000376643"
SQ SEQUENCE 236 AA; 25143 MW; 7CBA8671245523D7 CRC64;
MSYNLTDPYE IARFIKESKK STPVKVYVNG DLSNAEMNDV EWYGSNGFYI LMGESDSITK
IVLDNKHLIK HFRIENDRRN SAIPMLDLLE VDARIEPGAI IRDKVTIGKN AVIMMGAVIN
IGAEIGDGTM VDMNAVVGAR GQLGKNVHLG AGAVVAGVLE PPSKEPCMIG DNALIGANSV
ILEGVKIGAG SVVAAGSVVT EDVPDNVVVA GSPAKIIKAV DDKTKDKTQI LDDLRK