ID A0A371J475_9FIRM Unreviewed; 244 AA.
AC A0A371J475;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=dapD {ECO:0000313|EMBL:RDY27467.1};
GN Synonyms=dapH {ECO:0000256|HAMAP-Rule:MF_01691};
GN ORFNames=CHL78_009650 {ECO:0000313|EMBL:RDY27467.1};
OS Romboutsia weinsteinii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Romboutsia.
OX NCBI_TaxID=2020949 {ECO:0000313|EMBL:RDY27467.1, ECO:0000313|Proteomes:UP000215694};
RN [1] {ECO:0000313|EMBL:RDY27467.1, ECO:0000313|Proteomes:UP000215694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-19649 {ECO:0000313|EMBL:RDY27467.1,
RC ECO:0000313|Proteomes:UP000215694};
RX PubMed=28982987;
RA Maheux A.F., Boudreau D.K., Berube E., Boissinot M., Cantin P., Raymond F.,
RA Corbeil J., Omar R.F., Bergeron M.G.;
RT "Draft Genome Sequence of Romboutsia weinsteinii sp. nov. Strain CCRI-
RT 19649(T) Isolated from Surface Water.";
RL Genome Announc. 5:e00901-17(2017).
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:RDY27467.1}.
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DR EMBL; NOJY02000013; RDY27467.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371J475; -.
DR OrthoDB; 9788080at2; -.
DR UniPathway; UPA00034; UER00022.
DR Proteomes; UP000215694; 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:UP000215694};
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 14..96
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT acetyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08503"
SQ SEQUENCE 244 AA; 26291 MW; 2BEAAA46458C70AA CRC64;
MNNNENKIQE ENLTDPYAIA RFIKNAKKST PVKVYIKGNL ENVDFAGLKE FGDNSFKIVF
AEYDEIQPIL ENNKDAIEYF EIENDRRNSA IPMLDMKNIK ARIEPGATIR DRVSIGENAV
IMMGAVINIG AEIGENTMID MNATVGARGT IGKNVHVGAG SVIAGVLEPP SKTPVIIEDD
VMIGANAVVL EGVRVGKGAV VAAGAVVTCD VEPNTVVAGA PARVIKAKDE KTSEKVQILE
DLRQ
//