(data stored in ACNUC7421 zone)

HOGENOM: BACAN0_1_PE1013

ID   BACAN0_1_PE1013                      STANDARD;      PRT;   329 AA.
AC   BACAN0_1_PE1013; Q81U05; E9QU81; E9QU82; Q6I290; Q6KW25;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=Lipoate-protein ligase A, putative;SubName: Full=Putative
DE   lipoate-protein ligase A; (BACAN0_1.PE1013).
GN   OrderedLocusNames=BAS1017, BA_1089, GBAA_1089;
OS   BACILLUS ANTHRACIS STR. AMES.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus
OC   group.
OX   NCBI_TaxID=198094;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACAN0_1.PE1013.
CC       Bacillus anthracis str. Ames, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:Q81U05_BACAN
CC   -!- CATALYTIC ACTIVITY: ATP + lipoate = diphosphate + lipoyl-AMP.
CC   -!- CATALYTIC ACTIVITY: Lipoyl-AMP + protein = protein N(6)-
CC       (lipoyl)lysine + AMP.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC   -!- GENE_FAMILY: HOG000260593 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q81U05; E9QU81; E9QU82; Q6I290; Q6KW25; -.
DR   EMBL; AE016879; AAP25068.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT30187.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT53341.1; -; Genomic_DNA.
DR   RefSeq; NP_843582.1; NC_003997.3.
DR   RefSeq; YP_017712.1; NC_007530.2.
DR   RefSeq; YP_027290.1; NC_005945.1.
DR   ProteinModelPortal; Q81U05; -.
DR   IntAct; Q81U05; 2.
DR   EnsemblBacteria; EBBACT00000010232; EBBACP00000009988; EBBACG00000010224.
DR   EnsemblBacteria; EBBACT00000017075; EBBACP00000016696; EBBACG00000017066.
DR   EnsemblBacteria; EBBACT00000019679; EBBACP00000019164; EBBACG00000019670.
DR   GeneID; 1089024; -.
DR   GeneID; 2814491; -.
DR   GeneID; 2848279; -.
DR   GenomeReviews; AE016879_GR; BA_1089.
DR   GenomeReviews; AE017225_GR; BAS1017.
DR   GenomeReviews; AE017334_GR; GBAA_1089.
DR   KEGG; ban:BA_1089; -.
DR   KEGG; bar:GBAA_1089; -.
DR   KEGG; bat:BAS1017; -.
DR   TIGR; BA_1089; -.
DR   TIGR; GBAA1089; -.
DR   GeneTree; EBGT00050000002150; -.
DR   OMA; SEERYQN; -.
DR   ProtClustDB; CLSK2391388; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009249; P:protein lipoylation; IEA:InterPro.
DR   InterPro; IPR004143; BPL_LipA_LipB.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR019491; Lipoate_protein_ligase_C.
DR   InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR   Gene3D; G3DSA:3.30.390.50; CO_DH_flav_C; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF10437; Lip_prot_lig_C; 1.
DR   TIGRFAMs; TIGR00545; Lipoyltrans; 1.
DR   HOGENOMDNA; BACAN0_1.PE1013; -.
KW   lipoate-protein ligase A, putative;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Reference proteome; Transferase.
SQ   SEQUENCE   329 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLFIDNKGIT DPRINLAIEE YCVKNLDINE TYLLFYINEP SIIIGKNQNT VEEINADYVK
     EKGIHVVRRL SGGGAVYHDL GNLNFSFITK DDGDSFSNFK KFTEPVTKAL GKLGVNAELS
     GRNDILAEGR KISGNAQFST KGRMFSHGTL LFDSEIDHVV SALKVKMDKI QSKGIKSIRS
     RVANITEFLN EEMTTEEFRQ LLLETIFEGE TEIPTYELTE EDWKEIHKLS EERYRNWDWN
     YGKSPKFNLQ HSHRFPVGQV DVRLEVKKGT VTECKIYGDF FGSLDVHDIE ERLTGVQFDK
     DAFTTALEGV DIARYFGNIT TEDFLHLFF
//

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