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Database: UniProt
Entry: I0JLW8_HALH3
LinkDB: I0JLW8_HALH3
Original site: I0JLW8_HALH3 
ID   I0JLW8_HALH3            Unreviewed;       239 AA.
AC   I0JLW8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01691};
DE            EC=2.3.1.89 {ECO:0000256|HAMAP-Rule:MF_01691};
DE   AltName: Full=Tetrahydrodipicolinate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01691};
DE            Short=THP acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01691};
DE            Short=Tetrahydropicolinate acetylase {ECO:0000256|HAMAP-Rule:MF_01691};
GN   Name=dapH {ECO:0000256|HAMAP-Rule:MF_01691};
GN   OrderedLocusNames=HBHAL_2790 {ECO:0000313|EMBL:CCG45138.1};
OS   Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS   3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG45138.1, ECO:0000313|Proteomes:UP000007397};
RN   [1] {ECO:0000313|EMBL:CCG45138.1, ECO:0000313|Proteomes:UP000007397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC   NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX   PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA   Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA   Oesterhelt D.;
RT   "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT   salinities by the moderately halophilic, chloride-dependent bacterium
RT   Halobacillus halophilus.";
RL   Environ. Microbiol. 15:1619-1633(2013).
CC   -!- FUNCTION: Catalyzes the transfer of an acetyl group from acetyl-CoA to
CC       tetrahydrodipicolinate. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01691}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. DapH
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01691}.
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DR   EMBL; HE717023; CCG45138.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0JLW8; -.
DR   STRING; 866895.HBHAL_2790; -.
DR   KEGG; hhd:HBHAL_2790; -.
DR   PATRIC; fig|866895.3.peg.1808; -.
DR   eggNOG; COG2171; Bacteria.
DR   HOGENOM; CLU_103751_0_0_9; -.
DR   UniPathway; UPA00034; UER00022.
DR   Proteomes; UP000007397; 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 {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_01691};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01691};
KW   Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915,
KW   ECO:0000256|HAMAP-Rule:MF_01691};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW   Rule:MF_01691}; Reference proteome {ECO:0000313|Proteomes:UP000007397};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01691}.
FT   DOMAIN          4..88
FT                   /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT                   acetyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08503"
FT   REGION          220..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   239 AA;  25253 MW;  322E1A03000C5833 CRC64;
     MNQMDANEII SFISNSEKST PVKVYLKGDQ LESLDFGEQV QDFVSGQSGV IFGEWKVIQP
     LLEKYSSQIN DYVIENDRRN SAIPLLDLKK VNARIEPGAI IRDQVEIGDG AVIMLGAMIN
     IGSVVGEGTM IDMNVVLGGR ATVGKNCHIG AGAVLAGVIE PPSASPVVIE DGVVIGANAV
     ILEGVTVGEG AVVAAGSIVT ADVEPNTLVA GTPAKKIKDI DDQTKSKTEI KQELRKLDQ
//
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