(data stored in ACNUC7421 zone)

HOGENOM: PROMH_1_PE1014

ID   PROMH_1_PE1014                       STANDARD;      PRT;   339 AA.
AC   PROMH_1_PE1014; B4ETM3;
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   RecName: Full=Lipoate-protein ligase A; EC=2.7.7 63;AltName:
DE   Full=Lipoate--protein ligase; (PROMH_1.PE1014).
GN   Name=lplA; OrderedLocusNames=PMI1051;
OS   PROTEUS MIRABILIS HI4320.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PROMH_1.PE1014.
CC       Proteus mirabilis HI4320 chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:B4ETM3_PROMH
CC   -!- FUNCTION: Catalyzes both the ATP-dependent activation of
CC       exogenously supplied lipoate to lipoyl-AMP and the transfer of the
CC       activated lipoyl onto the lipoyl domains of lipoate-dependent
CC       enzymes (By similarity).
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   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group
CC       of lipoic acid is attached via an amide linkage to the epsilon-
CC       amino group of a specific lysine residue of lipoyl domains of
CC       lipoate-dependent enzymes (By similarity).
CC   -!- SIMILARITY: Belongs to the lplA family.
CC   -!- GENE_FAMILY: HOG000260594 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B4ETM3; -.
DR   EMBL; AM942759; CAR42278.1; -; Genomic_DNA.
DR   RefSeq; YP_002150801.1; NC_010554.1.
DR   ProteinModelPortal; B4ETM3; -.
DR   STRING; B4ETM3; -.
DR   GeneID; 6802674; -.
DR   GenomeReviews; AM942759_GR; PMI1051.
DR   OMA; YDRMENL; -.
DR   ProtClustDB; PRK03822; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016979; F:lipoate-protein ligase activity; IEA:HAMAP.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0018055; P:peptidyl-lysine lipoylation; IEA:HAMAP.
DR   HAMAP; MF_01602; LplA; 1; -.
DR   InterPro; IPR004143; BPL_LipA_LipB.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR023741; Lipoate_ligase_A.
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; PROMH_1.PE1014; -.
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Transferase.
SQ   SEQUENCE   339 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSGKLRLLLS ESYDPWFNLA VEECIFKQMP ADQRVLFLWR NDNTVVIGRA QNPWKECNTR
     KMEEDGVKLA RRSSGGGAVF HDLGNTCFTF MAGKPEYNKT ISTQIILDGL SKAGIQATAS
     GRNDLVVPLA DGERKISGSA YKETKDRGFH HGTLLINADL SRLANYLNPD PKKLQAKGIT
     SVRSRVTNLV ELKPDITHEK LCHAITDSFF DYYGERVEAE IISPQKLPDL PGFAETFAKQ
     SSWEWNFGQA PAFSHLLDNR FKWGGVELHF DIERGTIIRS QIYTDSLDPA PLEKLSQMLV
     GQRYASGSMK RLLAQLIEQY PNNQSELEEL QQWLVHALS
//

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