(data stored in SCRATCH zone)

SWISSPROT: D1CDL3_THET1

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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