ID LIPB_PARD8 Reviewed; 221 AA.
AC A6L9E1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 01-MAY-2013, entry version 44.
DE RecName: Full=Octanoyltransferase;
DE EC=2.3.1.181;
DE AltName: Full=Lipoate-protein ligase B;
DE AltName: Full=Lipoyl/octanoyl transferase;
DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase;
GN Name=lipB; OrderedLocusNames=BDI_0529;
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / NCTC
OS 11152).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC Porphyromonadaceae; Parabacteroides.
OX NCBI_TaxID=435591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / NCTC 11152;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M.,
RA Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P.,
RA Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A.,
RA Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
CC -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic
CC acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of
CC lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate
CC although octanoyl-ACP is likely to be the physiological substrate
CC (By similarity).
CC -!- CATALYTIC ACTIVITY: Octanoyl-[acyl-carrier-protein] + protein =
CC protein N(6)-(octanoyl)lysine + [acyl-carrier-protein].
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- MISCELLANEOUS: In the reaction, the free carboxyl group of
CC octanoic 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 LipB family.
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DR EMBL; CP000140; ABR42305.1; -; Genomic_DNA.
DR RefSeq; YP_001301927.1; NC_009615.1.
DR ProteinModelPortal; A6L9E1; -.
DR STRING; 435591.BDI_0529; -.
DR EnsemblBacteria; ABR42305; ABR42305; BDI_0529.
DR GeneID; 5305684; -.
DR KEGG; pdi:BDI_0529; -.
DR PATRIC; 22844206; VBIParDis29947_0515.
DR eggNOG; COG0321; -.
DR HOGENOM; HOG000194322; -.
DR KO; K03801; -.
DR OMA; NNIIPCG; -.
DR UniPathway; UPA00538; UER00592.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:EC.
DR GO; GO:0016415; F:octanoyltransferase activity; IEA:InterPro.
DR GO; GO:0006464; P:cellular protein modification process; IEA:InterPro.
DR GO; GO:0009107; P:lipoate biosynthetic process; IEA:InterPro.
DR HAMAP; MF_00013; LipB; 1; -.
DR InterPro; IPR004143; BPL_LipA_LipB.
DR InterPro; IPR000544; Octanoyltransferase.
DR InterPro; IPR020605; Octanoyltransferase_CS.
DR PANTHER; PTHR10993:SF0; PTHR10993:SF0; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR PIRSF; PIRSF016262; LPLase; 1.
DR TIGRFAMs; TIGR00214; lipB; 1.
DR PROSITE; PS01313; LIPB; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Complete proteome; Cytoplasm; Transferase.
FT CHAIN 1 221 Octanoyltransferase.
FT /FTId=PRO_0000321654.
FT REGION 81 88 Substrate binding (By similarity).
FT REGION 154 156 Substrate binding (By similarity).
FT REGION 167 169 Substrate binding (By similarity).
FT ACT_SITE 185 185 Acyl-thioester intermediate (By
FT similarity).
FT SITE 151 151 Lowers pKa of active site Cys (By
FT similarity).
SQ SEQUENCE 221 AA; 24945 MW; 5580792777599173 CRC64;
MESFRYHDLG RIAYADALEY QTAAFEVLLD AKATGKKEDN QLFFCEHLPV LTIGKSGKDS
NLLIPEETLR ERGVSFYHIN RGGDITYHGP GQITGYPVFD LEYWNLGLKQ YIHMLEETII
RFLSLYDLKG ERLEGATGVW LDPEVPGRAR KICAIGVKSS RFVTMHGFAL NINTDLSYFS
LINPCGFTDK GVTSLAMELG VPQDFELAKS QLRSIFMEIF A
//
