ID A0A0G3UDM1_9ACTN Unreviewed; 846 AA.
AC A0A0G3UDM1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phthiocerol/phthiodiolone dimycocerosyl transferase {ECO:0000256|ARBA:ARBA00013449};
DE EC=2.3.1.282 {ECO:0000256|ARBA:ARBA00012866};
DE AltName: Full=Acyltransferase PapA5 {ECO:0000256|ARBA:ARBA00033407};
DE AltName: Full=Phthiocerol/phthiodiolone O-acyltransferase {ECO:0000256|ARBA:ARBA00030465};
DE AltName: Full=Polyketide synthase-associated protein A5 {ECO:0000256|ARBA:ARBA00032317};
GN ORFNames=M444_02655 {ECO:0000313|EMBL:AKL64497.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL64497.1, ECO:0000313|Proteomes:UP000035653};
RN [1] {ECO:0000313|EMBL:AKL64497.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL64497.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
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:0000256|ARBA:ARBA00000625};
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:0000256|ARBA:ARBA00000026};
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:0000256|ARBA:ARBA00001907};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyltransferase PapA5 family.
CC {ECO:0000256|ARBA:ARBA00006558}.
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DR EMBL; CP011664; AKL64497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3UDM1; -.
DR KEGG; strm:M444_02655; -.
DR PATRIC; fig|465541.12.peg.665; -.
DR Proteomes; UP000035653; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR031641; PapA_C.
DR PANTHER; PTHR46496; -; 1.
DR PANTHER; PTHR46496:SF1; ZEAXANTHIN EPOXIDASE, CHLOROPLASTIC; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF16911; PapA_C; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000313|EMBL:AKL64497.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000035653}.
FT DOMAIN 7..344
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 624..726
FT /note="Phthiocerol/phthiodiolone dimycocerosyl transferase
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16911"
SQ SEQUENCE 846 AA; 92735 MW; 958B2C9CFEB7B6A0 CRC64;
MSSGRRMKAL VIGAGIGGLT CAVALRRVGI DVEVYERATE LRDVGSGLSV MSNAVTALAG
FGIDLGLDKR GQAVESFRIM DRRGRRIRDL PFQDTRGQVG SPSYCLSRAD LQEALLAEIG
DCPVHLGSTA IGFETAGAGV TARFEDGRSA SGDILIGADG FNSSVRRHLV GPEQAKDSGY
LFRLGIVPFR HRHLTTGAVR HYWGSGQRFG LIDIGKGRCY WWAAMSTPED APAPSRVKEL
LRRAYGDWAD EVRAVIDATP QADILTVPSR DRAFLERWGD GPVTLLGDAA HPMLTTLAQG
AGMAMEDAVV LARTLAEPMT GDDPARALRA YEERRLDRTR AMVAGSRRMS ELTQGATPRS
RLVRNAYFRF VPRRVLVRQT AQALTYPDDS ATGSGSVQRE LSPLERLYWI ADRTSPLNVI
ARARVHGHLP PSLHRRALDL LQLRHPLLRV AITDDGTGAH PAFVPLDARQ IPLRHVHVPP
DDPTADTRWE REVNDRELVK SVDWRAGPLL RAVVISSEGT DGENAGDFHD LLLTASHIIA
DGKTCLSLVR EWINLTAQLD RGTQPRVTPL RALPATDDLL PRRHRGAAGV AGFKALMRRE
EQAARRHPAQ RVLPSHQVPF EQRRTRMVHR SLPAEQLDLL VTAAKRHGTT VHGLLAAAMV
TAVARDAGTS TTAHFSIGSP VDFRDDLEPA VSPDEAGTYV ATVPSRVRYE PGRPLWLMAR
AISQDLVRRR GRQEHLATIS LPRWAGPKSL ADSESFMRFM DEEGPINLCL SNVGRYEFPD
QAGPWRVGEA QFLTGVSVMG SIVATATTSH AQLAWNFSYV EGLVPAPRAR RIADDSVRTV
LSVLTE
//
