ID   PAPA5_MYCVP             Reviewed;         416 AA.
AC   A1T9S1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Phthiocerol/phthiodiolone dimycocerosyl transferase;
DE            EC=2.3.1.282 {ECO:0000250|UniProtKB:P9WIN5};
DE   AltName: Full=Acyltransferase PapA5;
DE   AltName: Full=Phthiocerol/phthiodiolone O-acyltransferase;
DE   AltName: Full=Polyketide synthase-associated protein A5;
GN   Name=papA5; OrderedLocusNames=Mvan_3119;
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes diesterification of phthiocerol, phthiodiolone, and
CC       phenolphthiocerol with mycocerosic acids, the final step in the
CC       phthiocerol, phthiodiolone and phenolphthiocerol dimycocerosate esters
CC       (PDIM) synthesis. Can directly transfer the mycocerosate bound to the
CC       mycocerosic acid synthase (mas) onto the substrate alcohols.
CC       {ECO:0000250|UniProtKB:P9WIN5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a mycocerosyl-[mycocerosic acid synthase] + a phthiocerol =
CC         a dimycocerosyl phthiocerol + 2 holo-[mycocerosic acid synthase].;
CC         EC=2.3.1.282; Evidence={ECO:0000250|UniProtKB:P9WIN5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a mycocerosyl-[mycocerosic acid synthase] + a phthiodiolone
CC         = a dimycocerosyl phthiodiolone + 2 holo-[mycocerosic acid
CC         synthase].; EC=2.3.1.282; Evidence={ECO:0000250|UniProtKB:P9WIN5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a mycocerosyl-[mycocerosic acid synthase] + a
CC         phenolphthiocerol = a dimycocerosyl phenolphthiocerol + 2 holo-
CC         [mycocerosic acid synthase].; EC=2.3.1.282;
CC         Evidence={ECO:0000250|UniProtKB:P9WIN5};
CC   -!- SUBUNIT: Monomer. Interacts directly with the acyl carrier protein
CC       (ACP) domain of the mycocerosic acid synthase (mas) protein.
CC       {ECO:0000250|UniProtKB:P9WIN5}.
CC   -!- DOMAIN: Consists of two structural domains that are related to each
CC       other. {ECO:0000250|UniProtKB:P9WIN5}.
CC   -!- SIMILARITY: Belongs to the acyltransferase PapA5 family. {ECO:0000305}.
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DR   EMBL; CP000511; ABM13921.1; -; Genomic_DNA.
DR   RefSeq; WP_011780326.1; NC_008726.1.
DR   AlphaFoldDB; A1T9S1; -.
DR   SMR; A1T9S1; -.
DR   STRING; 350058.Mvan_3119; -.
DR   EnsemblBacteria; ABM13921; ABM13921; Mvan_3119.
DR   KEGG; mva:Mvan_3119; -.
DR   eggNOG; COG1020; Bacteria.
DR   HOGENOM; CLU_050374_1_0_11; -.
DR   OMA; EMFAETH; -.
DR   OrthoDB; 1068442at2; -.
DR   Proteomes; UP000009159; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR031641; PapA_C.
DR   Pfam; PF16911; PapA_C; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Lipid biosynthesis; Lipid metabolism; Reference proteome;
KW   Transferase.
FT   CHAIN           1..416
FT                   /note="Phthiocerol/phthiodiolone dimycocerosyl transferase"
FT                   /id="PRO_0000332110"
FT   ACT_SITE        119
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   SITE            123
FT                   /note="Structural role in the organization of the active
FT                   site"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  45667 MW;  4EBB6293196C52F0 CRC64;
     MFPSSGIRKL ARSEEMFAET HNFIGLAAHV KGSMDADALS DAFDLLLQAH PVLGGHLEQL
     PDGKWEIVLD DLMHPGIEVV ELTGDEPAPP LIFDQTVSLV HLRLTIRDGQ AQPTLYIHHS
     LADGHHQFSL VEELFSTYTD LVTTGTTKPV EVHPAPEPLE VILANRGVEK RTRSGLERLL
     AAMFVYDLPP SRRAPSDVNP VLPQLVPMAY CTLSEQDTEK IIAFCRANKL GLNSLLSAAV
     LMAEWNVRRT PNIPVPYVYP VDLRYLLSPP VSATESTNPV GIATYLAEIE KGTDIAELAR
     DINDTYKKDI AEGVIQQSFL HFSPQYVGNP PGLPDVVMFT DNGIVPPLRT PPDMEVAASH
     GEFYFAVGAG IEIYTSKIFN GQLMIEYHSH GPDREKSVAA IEEQLRAVVA RQSGVG