ID DAPH_KOSOT Reviewed; 232 AA.
AC C5CHX7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=Kole_0104;
OS Kosmotoga olearia (strain ATCC BAA-1733 / DSM 21960 / TBF 19.5.1).
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae;
OC Kosmotoga.
OX NCBI_TaxID=521045;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1733 / DSM 21960 / TBF 19.5.1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Noll K.;
RT "Complete sequence of Thermotogales bacterium TBF 19.5.1.";
RL Submitted (JUN-2009) 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; CP001634; ACR78832.1; -; Genomic_DNA.
DR RefSeq; WP_012744620.1; NC_012785.1.
DR AlphaFoldDB; C5CHX7; -.
DR SMR; C5CHX7; -.
DR STRING; 521045.Kole_0104; -.
DR KEGG; kol:Kole_0104; -.
DR eggNOG; COG2171; Bacteria.
DR HOGENOM; CLU_103751_0_0_0; -.
DR OrthoDB; 9788080at2; -.
DR UniPathway; UPA00034; UER00022.
DR Proteomes; UP000002382; 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 CDD; cd03350; LbH_THP_succinylT; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
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 NCBIfam; TIGR03532; DapD_Ac; 1.
DR PANTHER; PTHR43300:SF10; 2,3,4,5-TETRAHYDROPYRIDINE-2,6-DICARBOXYLATE N-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43300; ACETYLTRANSFERASE; 1.
DR Pfam; PF08503; DapH_N; 1.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF14602; Hexapep_2; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Diaminopimelate biosynthesis;
KW Lysine biosynthesis; Reference proteome; Repeat; Transferase.
FT CHAIN 1..232
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT acetyltransferase"
FT /id="PRO_1000215930"
SQ SEQUENCE 232 AA; 24081 MW; 86403D69C45858E6 CRC64;
MNAETIIKMI KDSKKKTPAV CYVSGNLEGL ETGTLNFVGG KDFGVIIGDF KEIQDLIARE
RERITGYHID IQARNSALPL ADLTKYEARI EPGAIIRDLV EIGKGAVIMM GAVINIGAVI
GKGTMIDMNA VIGGRAIIGD NCHIGAGAVV AGVIEPPSAT PVIIEDNVLV GANAVILEGV
RVGANSVVAA GAVVTKDVPS GTVVAGIPAK VIKAFDATTA DKTKIVQDLR EL
//
