DAPH_BACAN
ID DAPH_BACAN Reviewed; 240 AA.
AC Q81MQ2; Q6HU47; Q6KND1;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 136.
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};
GN OrderedLocusNames=BA_4194, GBAA_4194, BAS3891;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
CC -!- FUNCTION: Catalyzes the transfer of an acetyl group from acetyl-CoA to
CC tetrahydrodipicolinate. {ECO:0000255|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:0000255|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: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; AE016879; AAP27916.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33313.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT56192.1; -; Genomic_DNA.
DR RefSeq; NP_846430.1; NC_003997.3.
DR RefSeq; WP_000783248.1; NZ_WXXJ01000027.1.
DR RefSeq; YP_030141.1; NC_005945.1.
DR PDB; 3R8Y; X-ray; 1.70 A; A/B/C/D/E/F=1-240.
DR PDBsum; 3R8Y; -.
DR AlphaFoldDB; Q81MQ2; -.
DR SMR; Q81MQ2; -.
DR STRING; 260799.BAS3891; -.
DR DNASU; 1088777; -.
DR EnsemblBacteria; AAP27916; AAP27916; BA_4194.
DR EnsemblBacteria; AAT33313; AAT33313; GBAA_4194.
DR GeneID; 59155456; -.
DR GeneID; 64199323; -.
DR KEGG; ban:BA_4194; -.
DR KEGG; bar:GBAA_4194; -.
DR KEGG; bat:BAS3891; -.
DR PATRIC; fig|198094.11.peg.4163; -.
DR eggNOG; COG2171; Bacteria.
DR HOGENOM; CLU_103751_0_0_9; -.
DR OMA; HLEYDRR; -.
DR UniPathway; UPA00034; UER00022.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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 3D-structure; Acyltransferase; Amino-acid biosynthesis;
KW Diaminopimelate biosynthesis; Lysine biosynthesis; Reference proteome;
KW Repeat; Transferase.
FT CHAIN 1..240
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT acetyltransferase"
FT /id="PRO_0000376625"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:3R8Y"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:3R8Y"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:3R8Y"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:3R8Y"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:3R8Y"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:3R8Y"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:3R8Y"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:3R8Y"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3R8Y"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:3R8Y"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:3R8Y"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:3R8Y"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:3R8Y"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:3R8Y"
SQ SEQUENCE 240 AA; 25704 MW; 8C78BA2E7F97A6E0 CRC64;
MKMMDANEII SFIQKSEKKT PVKVYIKGDL KEVTFPETVQ AFVNKKSGVL FGEWSEIKTI
LDENSKYIVD YVVENDRRNS AIPMLDLKGI KARIEPGAII RDHVEIGDNA VIMMNATINI
GAVIGEGSMI DMNAVLGGRA TVGKNCHVGA GAVLAGVIEP PSAKPVIVED DVVIGANVVV
LEGVTVGKGA VVAAGAVVTE DVPPYTVVAG TPARVIKEID EKTKAKTEIK QELRQLNPEK
