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Octanoyltransferase (EC 2.3.1.181) (Lipoate-protein ligase B) (Lipoyl/octanoyl transferase) (Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase)

 LIPB_ORITI              Reviewed;         208 AA.
B3CRE6;
24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 1.
25-OCT-2017, entry version 53.
RecName: Full=Octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_00013};
AltName: Full=Lipoate-protein ligase B {ECO:0000255|HAMAP-Rule:MF_00013};
AltName: Full=Lipoyl/octanoyl transferase {ECO:0000255|HAMAP-Rule:MF_00013};
AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
Name=lipB {ECO:0000255|HAMAP-Rule:MF_00013};
OrderedLocusNames=OTT_0672;
Orientia tsutsugamushi (strain Ikeda) (Rickettsia tsutsugamushi).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Rickettsiaceae; Rickettsieae; Orientia.
NCBI_TaxID=334380;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ikeda;
PubMed=18508905; DOI=10.1093/dnares/dsn011;
Nakayama K., Yamashita A., Kurokawa K., Morimoto T., Ogawa M.,
Fukuhara M., Urakami H., Ohnishi M., Uchiyama I., Ogura Y., Ooka T.,
Oshima K., Tamura A., Hattori M., Hayashi T.;
"The whole-genome sequencing of the obligate intracellular bacterium
Orientia tsutsugamushi revealed massive gene amplification during
reductive genome evolution.";
DNA Res. 15:185-199(2008).
-!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic
acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of
lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate
although octanoyl-ACP is likely to be the physiological substrate.
{ECO:0000255|HAMAP-Rule:MF_00013}.
-!- CATALYTIC ACTIVITY: Octanoyl-[acyl-carrier-protein] + protein =
protein N(6)-(octanoyl)lysine + [acyl-carrier-protein].
{ECO:0000255|HAMAP-Rule:MF_00013}.
-!- PATHWAY: Protein modification; protein lipoylation via endogenous
pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
protein]: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00013}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00013}.
-!- MISCELLANEOUS: In the reaction, the free carboxyl group of
octanoic acid is attached via an amide linkage to the epsilon-
amino group of a specific lysine residue of lipoyl domains of
lipoate-dependent enzymes. {ECO:0000255|HAMAP-Rule:MF_00013}.
-!- SIMILARITY: Belongs to the LipB family. {ECO:0000255|HAMAP-
Rule:MF_00013}.
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EMBL; AP008981; BAG40130.1; -; Genomic_DNA.
RefSeq; WP_012461303.1; NC_010793.1.
ProteinModelPortal; B3CRE6; -.
SMR; B3CRE6; -.
PRIDE; B3CRE6; -.
EnsemblBacteria; BAG40130; BAG40130; OTT_0672.
KEGG; ott:OTT_0672; -.
HOGENOM; HOG000194320; -.
KO; K03801; -.
OMA; MHGFAFN; -.
OrthoDB; POG091H0530; -.
UniPathway; UPA00538; UER00592.
Proteomes; UP000001033; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
GO; GO:0006464; P:cellular protein modification process; IEA:InterPro.
GO; GO:0009107; P:lipoate biosynthetic process; IEA:InterPro.
CDD; cd16444; LipB; 1.
HAMAP; MF_00013; LipB; 1.
InterPro; IPR004143; BPL_LPL_catalytic.
InterPro; IPR000544; Octanoyltransferase.
InterPro; IPR020605; Octanoyltransferase_CS.
Pfam; PF03099; BPL_LplA_LipB; 1.
PIRSF; PIRSF016262; LPLase; 1.
TIGRFAMs; TIGR00214; lipB; 1.
PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PROSITE; PS01313; LIPB; 1.
3: Inferred from homology;
Acyltransferase; Complete proteome; Cytoplasm; Transferase.
CHAIN 1 208 Octanoyltransferase.
/FTId=PRO_1000089468.
DOMAIN 30 208 BPL/LPL catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01067}.
REGION 69 76 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00013}.
REGION 142 144 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00013}.
REGION 155 157 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00013}.
ACT_SITE 173 173 Acyl-thioester intermediate.
{ECO:0000255|HAMAP-Rule:MF_00013}.
SITE 139 139 Lowers pKa of active site Cys.
{ECO:0000255|HAMAP-Rule:MF_00013}.
SEQUENCE 208 AA; 23648 MW; 9727DAF47D031716 CRC64;
MVEWIEIQYP IEYGEAYKMM KSRLTGILNG TASEAVFILE HQDVYTAGIS AKNDELLNCY
DIPVHHTDRG GKFTYHGPGQ IIIYPVINLA VNGRVKDIRN YVNNLASLVI NSLKFFNITG
ITVQDTIGVW IDSEFGRKKI ASIGVRIHKW ITYHGVAINV CPDLKKFKGI IPCGDRDTIV
TSISELLDQK IDLDYYKAIL KQEFYKIF


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