DAPH_BACSU
ID DAPH_BACSU Reviewed; 236 AA.
AC O34981; Q796K1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 126.
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}; Synonyms=ykuQ;
GN OrderedLocusNames=BSU14180;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Scanlan E., Devine K.M.;
RT "Sequence of the Bacillus subtilis chromosome from ykuA to cse-15.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 190.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP CATALYTIC ACTIVITY.
RX PubMed=5411754; DOI=10.1128/jb.101.1.323-324.1970;
RA Weinberger S., Gilvarg C.;
RT "Bacterial distribution of the use of succinyl and acetyl blocking groups
RT in diaminopimelic acid biosynthesis.";
RL J. Bacteriol. 101:323-324(1970).
RN [5]
RP CATALYTIC ACTIVITY.
RX PubMed=11910040; DOI=10.1110/ps.4310102;
RA Beaman T.W., Vogel K.W., Drueckhammer D.G., Blanchard J.S., Roderick S.L.;
RT "Acyl group specificity at the active site of tetrahydrodipicolinate N-
RT succinyltransferase.";
RL Protein Sci. 11:974-979(2002).
CC -!- FUNCTION: Catalyzes the transfer of an acetyl group from acetyl-CoA to
CC tetrahydrodipicolinate.
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 ECO:0000269|PubMed:11910040, ECO:0000269|PubMed:5411754};
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; AJ222587; CAA10880.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13291.2; -; Genomic_DNA.
DR PIR; F69866; F69866.
DR RefSeq; NP_389301.2; NC_000964.3.
DR RefSeq; WP_003218680.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34981; -.
DR SMR; O34981; -.
DR IntAct; O34981; 1.
DR MINT; O34981; -.
DR STRING; 224308.BSU14180; -.
DR jPOST; O34981; -.
DR PaxDb; O34981; -.
DR PRIDE; O34981; -.
DR EnsemblBacteria; CAB13291; CAB13291; BSU_14180.
DR GeneID; 64303305; -.
DR GeneID; 939193; -.
DR KEGG; bsu:BSU14180; -.
DR PATRIC; fig|224308.179.peg.1547; -.
DR eggNOG; COG2171; Bacteria.
DR InParanoid; O34981; -.
DR OMA; HLEYDRR; -.
DR PhylomeDB; O34981; -.
DR BioCyc; BSUB:BSU14180-MON; -.
DR UniPathway; UPA00034; UER00022.
DR PRO; PR:O34981; -.
DR Proteomes; UP000001570; 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; 2.
DR Pfam; PF14602; Hexapep_2; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR03532; DapD_Ac; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Diaminopimelate biosynthesis;
KW Lysine biosynthesis; Reference proteome; Repeat; Transferase.
FT CHAIN 1..236
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT acetyltransferase"
FT /id="PRO_0000360657"
FT CONFLICT 190
FT /note="A -> P (in Ref. 1; CAA10880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 236 AA; 24961 MW; B70757BBB11B3A50 CRC64;
MKMMDANEII SFIQNSTKST PVKVYVKGEL EGINFGESAK AFINGNTGVV FGEWSEIQTA
IEENQSKIED YVVENDRRNS AIPMLDLKNI KARIEPGAII RDQVEIGDNA VIMMGASINI
GSVIGEGTMI DMNVVLGGRA TVGKNCHIGA GSVLAGVIEP PSAKPVVIED DVVIGANAVV
LEGVTVGKGA VVAAGAIVVN DVEPYTVVAG TPAKKIKDID EKTKGKTEIK QELRQL
