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ID D1CDL3_THET1 Unreviewed; 207 AA.
AC D1CDL3;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 08-MAY-2019, entry version 65.
DE RecName: Full=Octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262};
DE EC=2.3.1.181 {ECO:0000256|HAMAP-Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262};
DE AltName: Full=Lipoate-protein ligase B {ECO:0000256|HAMAP-Rule:MF_00013};
DE AltName: Full=Lipoyl/octanoyl transferase {ECO:0000256|HAMAP-Rule:MF_00013};
DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_00013};
GN Name=lipB {ECO:0000256|HAMAP-Rule:MF_00013};
GN OrderedLocusNames=Tter_0097 {ECO:0000313|EMBL:ACZ41019.1};
OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC Bacteria; Thermobaculum.
OX NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41019.1, ECO:0000313|Proteomes:UP000000323};
RN [1] {ECO:0000313|EMBL:ACZ41019.1, ECO:0000313|Proteomes:UP000000323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX PubMed=21304745;
RA Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT (YNP1).";
RL Stand. Genomic Sci. 3:153-162(2010).
RN [2] {ECO:0000313|Proteomes:UP000000323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX DOI=10.4056/sigs.1153107;
RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA Kyrpides N., Klenk H., Cheng J.;
RT "Complete genome sequence of Thermobaculum terrenum type strain
RT (YNP1T).";
RL Stand. Genomic Sci. 3:153-162(2010).
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 {ECO:0000256|HAMAP-Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] +
CC N(6)-octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665,
CC Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78463, ChEBI:CHEBI:78809;
CC EC=2.3.1.181; Evidence={ECO:0000256|HAMAP-Rule:MF_00013,
CC ECO:0000256|PIRNR:PIRNR016262, ECO:0000256|SAAS:SAAS01124903};
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00013,
CC ECO:0000256|PIRNR:PIRNR016262, ECO:0000256|SAAS:SAAS01056745}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00013}.
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. {ECO:0000256|HAMAP-Rule:MF_00013}.
CC -!- SIMILARITY: Belongs to the LipB family. {ECO:0000256|HAMAP-
CC Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262}.
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DR EMBL; CP001825; ACZ41019.1; -; Genomic_DNA.
DR STRING; 525904.Tter_0097; -.
DR EnsemblBacteria; ACZ41019; ACZ41019; Tter_0097.
DR KEGG; ttr:Tter_0097; -.
DR eggNOG; ENOG4108BDP; Bacteria.
DR eggNOG; COG0321; LUCA.
DR HOGENOM; HOG000194322; -.
DR KO; K03801; -.
DR OMA; GEVTYHC; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000000323; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102555; F:octanoyl transferase activity (acting on glycine-cleavage complex H protein); IEA:UniProtKB-EC.
DR GO; GO:0009249; P:protein lipoylation; IEA:InterPro.
DR CDD; cd16444; LipB; 1.
DR HAMAP; MF_00013; LipB; 1.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR000544; Octanoyltransferase.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR PIRSF; PIRSF016262; LPLase; 1.
DR TIGRFAMs; TIGR00214; lipB; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 3: Inferred from homology;
DR PRODOM; D1CDL3.
DR SWISS-2DPAGE; D1CDL3.
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00013,
KW ECO:0000256|PIRNR:PIRNR016262, ECO:0000256|SAAS:SAAS00853398};
KW Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00013};
KW Ligase {ECO:0000313|EMBL:ACZ41019.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00013,
KW ECO:0000256|PIRNR:PIRNR016262, ECO:0000256|SAAS:SAAS00853388}.
FT DOMAIN 23 205 BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT PS51733}.
FT REGION 68 75 Substrate binding. {ECO:0000256|HAMAP-
FT Rule:MF_00013, ECO:0000256|PIRSR:
FT PIRSR016262-2}.
FT REGION 135 137 Substrate binding. {ECO:0000256|HAMAP-
FT Rule:MF_00013, ECO:0000256|PIRSR:
FT PIRSR016262-2}.
FT REGION 148 150 Substrate binding. {ECO:0000256|HAMAP-
FT Rule:MF_00013, ECO:0000256|PIRSR:
FT PIRSR016262-2}.
FT ACT_SITE 166 166 Acyl-thioester intermediate.
FT {ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-1}.
FT SITE 132 132 Lowers pKa of active site Cys.
FT {ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-3}.
SQ SEQUENCE 207 AA; 23382 MW; B9385BD96F7AED87 CRC64;
MGIVPYMEAW ELQKSLVASI ASNEHPESLI LLQHPHTYTI GRKGGHDHLL ASIEQLRAMN
VEVIETDRGG DITYHGPEQI VGYPLINLRN IGSDVHKYLR MLEEVLIRTL NDYGFSAHRD
EQYTGVWIGK AKIAAIGVKI SRGITMHGFA ININTDLRYF DMIIPCGITG RSVTSLQVLL
GRTIPLEEVM DHIEHHFSEV FEVQITR
//
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