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DAPH_ENTFA
ID   DAPH_ENTFA              Reviewed;         233 AA.
AC   Q836H8;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
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}; OrderedLocusNames=EF_1133;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
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; AE016830; AAO80933.1; -; Genomic_DNA.
DR   RefSeq; NP_814863.1; NC_004668.1.
DR   RefSeq; WP_002386624.1; NZ_KE136528.1.
DR   PDB; 3CJ8; X-ray; 1.95 A; A/B/C=2-233.
DR   PDBsum; 3CJ8; -.
DR   AlphaFoldDB; Q836H8; -.
DR   SMR; Q836H8; -.
DR   STRING; 226185.EF_1133; -.
DR   EnsemblBacteria; AAO80933; AAO80933; EF_1133.
DR   KEGG; efa:EF1133; -.
DR   PATRIC; fig|226185.45.peg.2362; -.
DR   eggNOG; COG2171; Bacteria.
DR   HOGENOM; CLU_103751_0_0_9; -.
DR   OMA; HLEYDRR; -.
DR   UniPathway; UPA00034; UER00022.
DR   EvolutionaryTrace; Q836H8; -.
DR   Proteomes; UP000001415; 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; 1.
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..233
FT                   /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT                   acetyltransferase"
FT                   /id="PRO_0000376656"
FT   HELIX           2..12
FT                   /evidence="ECO:0007829|PDB:3CJ8"
FT   STRAND          18..25
FT                   /evidence="ECO:0007829|PDB:3CJ8"
FT   STRAND          36..40
FT                   /evidence="ECO:0007829|PDB:3CJ8"
FT   STRAND          42..50
FT                   /evidence="ECO:0007829|PDB:3CJ8"
FT   HELIX           51..60
FT                   /evidence="ECO:0007829|PDB:3CJ8"
FT   TURN            61..64
FT                   /evidence="ECO:0007829|PDB:3CJ8"
FT   STRAND          65..72
FT                   /evidence="ECO:0007829|PDB:3CJ8"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:3CJ8"
FT   STRAND          88..91
FT                   /evidence="ECO:0007829|PDB:3CJ8"
FT   STRAND          96..100
FT                   /evidence="ECO:0007829|PDB:3CJ8"
FT   STRAND          203..206
FT                   /evidence="ECO:0007829|PDB:3CJ8"
FT   TURN            207..210
FT                   /evidence="ECO:0007829|PDB:3CJ8"
FT   STRAND          211..215
FT                   /evidence="ECO:0007829|PDB:3CJ8"
SQ   SEQUENCE   233 AA;  24618 MW;  CE20F3EBA9B89DA2 CRC64;
     MDAYEIIQYI GDAKKQTLVK VTLKGQLKEV TFPETIKVFN NCKTGTLFGD WADVKPFLEA
     NKEKIEDYVV ENDARNSAIP FLDLKDINAR IEPGALIREK VEIGDQAVIM MGAILNIGAV
     VGAGTMIDMG AVLGGRATVG KHCHIGAGTV LAGVIEPPSA APVVIENEVV IGANAVVLEG
     VRVGEGAVVA AGAVVVEDVP AHTVVAGVPA KVIKQIDDKT KSKTEILEEL RKL
 
 
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