(data stored in ACNUC7421 zone)

SWISSPROT: Q750P9_ASHGO

ID   Q750P9_ASHGO            Unreviewed;       342 AA.
AC   Q750P9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 105.
DE   RecName: Full=Octanoyltransferase {ECO:0000256|PIRNR:PIRNR016262};
DE            EC=2.3.1.181 {ECO:0000256|PIRNR:PIRNR016262};
GN   ORFNames=AGOS_AGL107W {ECO:0000313|EMBL:AAS54384.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54384.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54384.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid
CC       from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-
CC       dependent enzymes. Lipoyl-ACP can also act as a substrate although
CC       octanoyl-ACP is likely to be the physiological substrate.
CC       {ECO:0000256|PIRNR:PIRNR016262}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-
CC         octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-
CC         COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181;
CC         Evidence={ECO:0000256|PIRNR:PIRNR016262};
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|PIRNR:PIRNR016262}.
CC   -!- SIMILARITY: Belongs to the LipB family.
CC       {ECO:0000256|PIRNR:PIRNR016262}.
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DR   EMBL; AE016820; AAS54384.1; -; Genomic_DNA.
DR   RefSeq; NP_986560.1; NM_211622.1.
DR   STRING; 33169.AAS54384; -.
DR   EnsemblFungi; AAS54384; AAS54384; AGOS_AGL107W.
DR   GeneID; 4622859; -.
DR   KEGG; ago:AGOS_AGL107W; -.
DR   HOGENOM; HOG000248573; -.
DR   InParanoid; Q750P9; -.
DR   KO; K23735; -.
DR   OMA; YLNTFEM; -.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0016874; F:ligase activity; IEA:EnsemblFungi.
DR   GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR000544; Octanoyltransferase.
DR   InterPro; IPR020605; Octanoyltransferase_CS.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   PIRSF; PIRSF016262; LPLase; 1.
DR   TIGRFAMs; TIGR00214; lipB; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR   PROSITE; PS01313; LIPB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750P9.
DR   SWISS-2DPAGE; Q750P9.
KW   Acyltransferase {ECO:0000256|PIRNR:PIRNR016262};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|PIRNR:PIRNR016262}.
FT   DOMAIN          126..336
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
FT   ACT_SITE        296
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016262-1"
FT   SITE            262
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016262-3"
SQ   SEQUENCE   342 AA;  38445 MW;  C0D76A4A55B61A28 CRC64;
     MLRYAMTPRR SIWTPLQVNQ GVMVRMVMHR PILGHLSRMR YSSTSPKDAQ AITYPVTEKA
     RVLEHIHFKK RCTFKEGLQI QELYVMHALE AKRMQSKIAQ RLRQRAETAT NTDLLLDWPA
     PAKCISTPRP TVLTFEFEPT YTGGKRIKKT ITKDEVQALE SFTPPGSEGY PSPKFVQVER
     GGQVTFHGPG QMVAYIVLDL KAFHGFTVRC LVSAIERATI NTLQCAPKHE ASRNATRRRN
     DKLGIKAIQT SENGVWIDEK RKIASLGVNV RRSITSHGVC INVNPTLQYL NHFTMCGLPE
     SSATSIHELV PSATCGVGDI AATFVNQFRM LLGIEEIVRS DI
//

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