PAPA5_MYCLE
ID PAPA5_MYCLE Reviewed; 423 AA.
AC Q49939; Q9S381;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=ML2349; ORFNames=MLCB2407.01;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; U00023; AAA17363.1; -; Genomic_DNA.
DR EMBL; AL023596; CAA19141.1; -; Genomic_DNA.
DR EMBL; AL583925; CAC31865.1; -; Genomic_DNA.
DR PIR; S73020; S73020.
DR RefSeq; NP_302528.1; NC_002677.1.
DR RefSeq; WP_010908848.1; NC_002677.1.
DR AlphaFoldDB; Q49939; -.
DR SMR; Q49939; -.
DR STRING; 272631.ML2349; -.
DR EnsemblBacteria; CAC31865; CAC31865; CAC31865.
DR KEGG; mle:ML2349; -.
DR PATRIC; fig|272631.5.peg.4508; -.
DR Leproma; ML2349; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_050374_1_0_11; -.
DR OMA; EMFAETH; -.
DR Proteomes; UP000000806; 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..423
FT /note="Phthiocerol/phthiodiolone dimycocerosyl transferase"
FT /id="PRO_0000332104"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT SITE 129
FT /note="Structural role in the organization of the active
FT site"
FT /evidence="ECO:0000250"
FT SITE 313
FT /note="Important for mas ACP domain recognition"
FT /evidence="ECO:0000250"
SQ SEQUENCE 423 AA; 45595 MW; FED1483E87F4542E CRC64;
MFAGSVIRKL SHSEEVFARY EVFTSMTIQL RGVLDIDALS EAFDALVQAH PVLASHLETS
SDGGWNLVAD DLLHPGICVV DANNGAQSGC GGIQSETRLD QSVSLLNLRL TPREGGGELV
LYIHHSMADG HHGAVLVDEL FSRYTDVVTT GDPGPIIPQA TPLSMEAVLQ QRGVKKHALS
GAERFMSVMY AYDLPATGTP AVLAEPGLPQ AVPVTRLWLT KQETSDLAAF GREHRLSINA
VVAAAILMTE WRLRETPHVP IPYVYPVDLR YVLAPPVAPT ESTNLLGAAG YLAEIGQDTD
IVDLATDIVA TLRADLANGV VQQSGLHFGT AFEGTPPGLP PLVFCTDATA FPTMRTPPDL
AIEDIQGRFY CSISVPLDLY SCGVYEGQLI IEHHGHIEEP AKALEAIRSL LCTVPSEYGW
IME
