ID A0A143H935_9BACL Unreviewed; 237 AA.
AC A0A143H935;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 ORFNames=ATY39_01810 {ECO:0000313|EMBL:AMW98263.1};
OS Rummeliibacillus stabekisii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Rummeliibacillus.
OX NCBI_TaxID=241244 {ECO:0000313|EMBL:AMW98263.1, ECO:0000313|Proteomes:UP000076021};
RN [1] {ECO:0000313|EMBL:AMW98263.1, ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|EMBL:AMW98263.1,
RC ECO:0000313|Proteomes:UP000076021};
RX PubMed=27231360;
RA da Mota F.F., Vollu R.E., Jurelevicius D., Seldin L.;
RT "Whole-Genome Sequence of Rummeliibacillus stabekisii Strain PP9 Isolated
RT from Antarctic Soil.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|Proteomes:UP000076021};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; CP014806; AMW98263.1; -; Genomic_DNA.
DR RefSeq; WP_066784973.1; NZ_JAMAVX010000001.1.
DR AlphaFoldDB; A0A143H935; -.
DR STRING; 241244.ATY39_01810; -.
DR KEGG; rst:ATY39_01810; -.
DR OrthoDB; 9788080at2; -.
DR UniPathway; UPA00034; UER00022.
DR Proteomes; UP000076021; 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|HAMAP-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:UP000076021};
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..87
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT acetyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08503"
SQ SEQUENCE 237 AA; 25293 MW; 06F4C7D9CF9B87EA CRC64;
MEKLNAEQII SYLANAKKAT PVKVYVKGKD ISSIPFGENS KVFGEKDAAV VFGEWQDIKK
ALEENKETIE DYVVEHDRRN SAVPTLELLD IHARIEPGAI IRDQVTIGQN VVIMMGSVIN
IGAEIGDRTM IDMNAVLGGR ATVGKDCHIG AGAVLAGVIE PPSADPVVVE DNVLIGANAV
VLEGCRIGEG AVVAAGAIVT KDVPPYTVVV GAPARVIKEI DEKTKSKSEI MQDLRQI
//
