ID   DAPH_PSELT              Reviewed;         238 AA.
AC   A8F8L8;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   25-MAY-2022, entry version 76.
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=Tlet_1948;
OS   Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS   TMO) (Thermotoga lettingae).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Pseudothermotoga.
OX   NCBI_TaxID=416591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga lettingae TMO.";
RL   Submitted (AUG-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABV34502.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000812; ABV34502.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_028843625.1; NC_009828.1.
DR   AlphaFoldDB; A8F8L8; -.
DR   SMR; A8F8L8; -.
DR   STRING; 416591.Tlet_1948; -.
DR   EnsemblBacteria; ABV34502; ABV34502; Tlet_1948.
DR   KEGG; tle:Tlet_1948; -.
DR   eggNOG; COG2171; Bacteria.
DR   HOGENOM; CLU_103751_0_0_0; -.
DR   UniPathway; UPA00034; UER00022.
DR   Proteomes; UP000002016; 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; 1.
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; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..238
FT                   /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT                   acetyltransferase"
FT                   /id="PRO_0000376728"
SQ   SEQUENCE   238 AA;  25244 MW;  75F52C0F90418334 CRC64;
     MNNDLTADSI IEMISSSKKK TPVIAYVKGH LSDIDMSGVQ FFGTDNFGII FADYEDLRQF
     LEKNGNKIHD VHIEAKARNS ALPMADITKF NARVEPGAVI RDLVKIGDGA VIMMGAIINV
     GAVIGEKTMI DMNAVIGGRA IIGRNCHIGA GAVIAGVIEP PSATPVVIED NVMVGANAVV
     LEGVKVGKGS VVAAGAVVVS DVDPYTVVAG IPAKFIKKVD EKTIEKTKII EILRQRDH