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DAPH_STAHJ
ID   DAPH_STAHJ              Reviewed;         239 AA.
AC   Q4L6A2;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 120.
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=SH1514;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04823.1; -; Genomic_DNA.
DR   RefSeq; WP_011275806.1; NC_007168.1.
DR   AlphaFoldDB; Q4L6A2; -.
DR   SMR; Q4L6A2; -.
DR   STRING; 279808.SH1514; -.
DR   EnsemblBacteria; BAE04823; BAE04823; SH1514.
DR   GeneID; 58062287; -.
DR   KEGG; sha:SH1514; -.
DR   eggNOG; COG2171; Bacteria.
DR   HOGENOM; CLU_103751_0_0_9; -.
DR   OMA; HLEYDRR; -.
DR   OrthoDB; 752123at2; -.
DR   UniPathway; UPA00034; UER00022.
DR   Proteomes; UP000000543; 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; Repeat; Transferase.
FT   CHAIN           1..239
FT                   /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT                   acetyltransferase"
FT                   /id="PRO_0000376704"
SQ   SEQUENCE   239 AA;  25121 MW;  DD64ABDE911EE5AB CRC64;
     MVQHLSAEEI IQYISDAKKS TPLKVYVNGN FDGVTFPDSF KVFGSDNSKV IFCEADDWKP
     FYESNQSTIT ELEIEMDRRN SAIPLKDLTN TNARIEPGAF IREQAIIEDG AVVMMGATIN
     IGAVVGEGTM IDMNATLGGR ATTGKNVHVG AGAVLAGVIE PPSASPVVID DNVLIGANAV
     ILEGVHVGEG AIVAAGAIVT QDVPAGAVVA GTPAKVIKQT SEVEDSKREI VSALRKLND
 
 
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