(data stored in ACNUC8465 zone)

SWISSPROT: B6HFE9_PENRW

ID   B6HFE9_PENRW            Unreviewed;       302 AA.
AC   B6HFE9;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 57.
DE   RecName: Full=Octanoyltransferase {ECO:0000256|PIRNR:PIRNR016262};
DE            EC=2.3.1.181 {ECO:0000256|PIRNR:PIRNR016262};
GN   ORFNames=Pc20g03070 {ECO:0000313|EMBL:CAP85636.1}, PCH_Pc20g03070
GN   {ECO:0000313|EMBL:CAP85636.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85636.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85636.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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|PIRNR:PIRNR016262}.
CC   -!- CATALYTIC ACTIVITY: Octanoyl-[acyl-carrier-protein] + protein =
CC       protein N(6)-(octanoyl)lysine + [acyl-carrier-protein].
CC       {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; AM920435; CAP85636.1; -; Genomic_DNA.
DR   RefSeq; XP_002562859.1; XM_002562813.1.
DR   ProteinModelPortal; B6HFE9; -.
DR   STRING; 500485.XP_002562859.1; -.
DR   EnsemblFungi; CAP85636; CAP85636; PCH_Pc20g03070.
DR   GeneID; 8317536; -.
DR   KEGG; pcs:Pc20g03070; -.
DR   eggNOG; KOG0325; Eukaryota.
DR   eggNOG; COG0321; LUCA.
DR   HOGENOM; HOG000194322; -.
DR   KO; K03801; -.
DR   OMA; VTEEPMW; -.
DR   OrthoDB; EOG092C4EGM; -.
DR   BioCyc; PCHR:PC20G03070-MONOMER; -.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-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   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; B6HFE9.
DR   SWISS-2DPAGE; B6HFE9.
KW   Acyltransferase {ECO:0000256|PIRNR:PIRNR016262};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transferase {ECO:0000256|PIRNR:PIRNR016262}.
FT   DOMAIN       58    276       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
FT   REGION      125    132       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR016262-2}.
FT   REGION      205    207       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR016262-2}.
FT   REGION      218    220       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR016262-2}.
FT   ACT_SITE    237    237       Acyl-thioester intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR016262-1}.
FT   SITE        202    202       Lowers pKa of active site Cys.
FT                                {ECO:0000256|PIRSR:PIRSR016262-3}.
SQ   SEQUENCE   302 AA;  32575 MW;  A347AB8948D72745 CRC64;
     MRLAHLHLPH TTPFSRVSHL QQTLTTRLLT HKKLASPGSI SSQEPSNPSA TLSKTPPSPP
     DPTIITFTPN PVYTTGRRDL PPSNTSPPST TNPILSLPPA LEPIRSLFTP DGTKPAKAEY
     HPTLRGGQTT YHGPGQMVAY TILDLKRLGL TPRCHIRVLE NSVIDLLKSY GVEGFTTEDP
     GVWVNPVSGS RSASGSALQP RKITAVGVHL RRNISSFGIG LNVTDEPMWF FKQIVACGLE
     GKEATSLQGV GVPGLEVGDV AAAFVEKFVS RVNADFACGE NSLGEKIDEV YQVREEDLLN
     SV
//

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