PAPA5_MYCBO
ID PAPA5_MYCBO Reviewed; 422 AA.
AC Q02279; A0A1R3Y4M0; Q7TXL2; X2BMV2;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 25-MAY-2022, entry version 104.
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=BQ2027_MB2964;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BCG;
RX PubMed=1527058; DOI=10.1016/s0021-9258(18)41788-7;
RA Mathur M., Kolattukudy P.E.;
RT "Molecular cloning and sequencing of the gene for mycocerosic acid
RT synthase, a novel fatty acid elongating multifunctional enzyme, from
RT Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin.";
RL J. Biol. Chem. 267:19388-19395(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA25370.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M95808; AAA25370.1; ALT_FRAME; Genomic_DNA.
DR EMBL; LT708304; SIU01585.1; -; Genomic_DNA.
DR RefSeq; NP_856609.1; NC_002945.3.
DR RefSeq; WP_003414853.1; NC_002945.4.
DR AlphaFoldDB; Q02279; -.
DR SMR; Q02279; -.
DR EnsemblBacteria; SIU01585; SIU01585; BQ2027_MB2964.
DR GeneID; 45426927; -.
DR PATRIC; fig|233413.5.peg.3253; -.
DR OMA; EMFAETH; -.
DR Proteomes; UP000001419; 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; Transferase.
FT CHAIN 1..422
FT /note="Phthiocerol/phthiodiolone dimycocerosyl transferase"
FT /id="PRO_0000058228"
FT ACT_SITE 124
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT SITE 128
FT /note="Structural role in the organization of the active
FT site"
FT /evidence="ECO:0000250"
FT SITE 312
FT /note="Important for mas ACP domain recognition"
FT /evidence="ECO:0000250"
FT CONFLICT 32
FT /note="G -> R (in Ref. 1; AAA25370)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="L -> H (in Ref. 1; AAA25370)"
FT /evidence="ECO:0000305"
FT CONFLICT 110..111
FT /note="IL -> MV (in Ref. 1; AAA25370)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="V -> G (in Ref. 1; AAA25370)"
FT /evidence="ECO:0000305"
FT CONFLICT 251..252
FT /note="QL -> HV (in Ref. 1; AAA25370)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 45429 MW; 19156C6B9FCC3AA7 CRC64;
MFPGSVIRKL SHSEEVFAQY EVFTSMTIQL RGVIDVDALS DAFDALLETH PVLASHLEQS
SDGGWNLVAD DLLHSGICVI DGTAATNGSP SGNAELRLDQ SVSLLHLQLI LREGGAELTL
YLHHCMADGH HGAVLVDELF SRYTDAVTTG DPGPITPQPT PLSMEAVLAQ RGIRKQGLSG
AERFMSVMYA YEIPATETPA VLAHPGLPQA VPVTRLWLSK QQTSDLMAFG REHRLSLNAV
VAAAILLTEW QLRNTPHVPI PYVYPVDLRF VLAPPVAPTE ATNLLGAASY LAEIGPNTDI
VDLASDIVAT LRADLANGVI QQSGLHFGTA FEGTPPGLPP LVFCTDATSF PTMRTPPGLE
IEDIKGQFYC SISVPLDLYS CAVYAGQLII EHHGHIAEPG KSLEAIRSLL CTVPSEYGWI
ME
