ID S0JI79_9ENTE Unreviewed; 233 AA.
AC S0JI79;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=OMQ_01749 {ECO:0000313|EMBL:EOT28235.1};
OS Enterococcus saccharolyticus subsp. saccharolyticus ATCC 43076.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1139996 {ECO:0000313|EMBL:EOT28235.1, ECO:0000313|Proteomes:UP000014136};
RN [1] {ECO:0000313|EMBL:EOT28235.1, ECO:0000313|Proteomes:UP000014136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43076 {ECO:0000313|EMBL:EOT28235.1,
RC ECO:0000313|Proteomes:UP000014136};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus saccharolyticus ATCC_43076 (Illumina
RT only assembly).";
RL Submitted (MAR-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOT28235.1}.
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DR EMBL; AHYT01000008; EOT28235.1; -; Genomic_DNA.
DR RefSeq; WP_016175536.1; NZ_KE136523.1.
DR AlphaFoldDB; S0JI79; -.
DR STRING; 41997.RV16_GL000670; -.
DR PATRIC; fig|1139996.3.peg.1736; -.
DR eggNOG; COG2171; Bacteria.
DR HOGENOM; CLU_103751_0_0_9; -.
DR OrthoDB; 9788080at2; -.
DR UniPathway; UPA00034; UER00022.
DR Proteomes; UP000014136; Unassembled WGS sequence.
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:UP000014136};
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 8..84
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT acetyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08503"
SQ SEQUENCE 233 AA; 24432 MW; 499D0376B64BCF81 CRC64;
MSELQFSDPY QLAKYIKDAT KQTPVKAYIN GDLTNVTSDR VKIFGNVAIG DAVDIDAFLE
ANKAVINDYY LENDRRNSAV PMLDVTKVDA RIEPGAFIRD QAIINKNAVV MMGAVINIGA
VVGEETMIDM GAILGARATV GKRAHIGAGA VLAGVLEPPS ASPVVVEDNV LIGANAVVLE
GVRIGEGAVV AAGAVVTQDV PANAVVAGSP AKIIKMKDDK TLSKTEFLDD LRG
//
