ID   DAPH_STAAS              Reviewed;         239 AA.
AC   Q6G9G4;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=SAS1338;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG43114.1; -; Genomic_DNA.
DR   RefSeq; WP_000249839.1; NC_002953.3.
DR   AlphaFoldDB; Q6G9G4; -.
DR   SMR; Q6G9G4; -.
DR   KEGG; sas:SAS1338; -.
DR   HOGENOM; CLU_103751_0_0_9; -.
DR   OMA; HLEYDRR; -.
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; 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; Repeat; Transferase.
FT   CHAIN           1..239
FT                   /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT                   acetyltransferase"
FT                   /id="PRO_0000376692"
SQ   SEQUENCE   239 AA;  25258 MW;  D7E6F32A2612525E CRC64;
     MVQHLTAEEI IQYISDAKKS TPIKVYLNGN FEGITYPESF KVFGSEQSKV IFCEADDWKP
     FYEAYGSQFE DIEIEMDRRN SAIPLKDLTN TNARIEPGAF IREQAIIEDG AVVMMGATIN
     IGAVVGEGTM IDMNATLGGR ATTGKNVHVG AGAVLAGVIE PPSASPVIIE DDVLIGANAV
     ILEGVRVGKG AIVAAGAIVT QDVPAGAVVA GTPAKVIKQA SEVQDTKKEI VAALRKLND