ATR1_STEAL
ID ATR1_STEAL Reviewed; 2500 AA.
AC A0A8F4SKJ7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2022, sequence version 1.
DT 03-AUG-2022, entry version 3.
DE RecName: Full=Non-reducing polyketide synthase atr1 {ECO:0000303|PubMed:34154413};
DE EC=2.3.1.- {ECO:0000269|PubMed:34154413};
DE AltName: Full=Atranorin biosynthesis cluster protein 1 {ECO:0000303|PubMed:34154413};
GN Name=atr1 {ECO:0000303|PubMed:34154413};
OS Stereocaulon alpinum (Alpine snow lichen) (Stereocaulon paschale var.
OS alpinum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae;
OC Stereocaulaceae; Stereocaulon.
OX NCBI_TaxID=350623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=34154413; DOI=10.1128/mbio.01111-21;
RA Kim W., Liu R., Woo S., Kang K.B., Park H., Yu Y.H., Ha H.H., Oh S.Y.,
RA Yang J.H., Kim H., Yun S.H., Hur J.S.;
RT "Linking a gene cluster to atranorin, a major cortical substance of
RT lichens, through genetic dereplication and heterologous expression.";
RL MBio 12:e0111121-e0111121(2021).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of atranorin, a depside of polyketide
CC origin that accumulates in the cortical or medullary layers of lichen
CC thalli (PubMed:34154413). The first step in the pathway is performed by
CC the non-reducing polyketide synthase atr1 that produces 4-O-
CC demethylbarbatic acid composed of two 3-methylorsellinic acid (3MOA)
CC moieties from S-adenosyl-L-methionine (SAM), acetyl-CoA and malonyl-CoA
CC units (PubMed:34154413). The pathway continues with the actions of the
CC cytochrome P450 monooygenase atr2 that catalizes the oxidation of c-9
CC and the O-methyltransferase atr3 that performs the methylation of the
CC carboxyl group to yield atranorin, via the proatranorin II and III
CC intermediates if atr2 acts first, or the proatranorin I intermediate if
CC atr3 acts first (PubMed:34154413). {ECO:0000269|PubMed:34154413}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:34154413}.
CC -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide
CC backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; and an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm. {ECO:0000250|UniProtKB:Q5ATJ7}.
CC -!- DOMAIN: The release of the polyketide chain from the non-reducing
CC polyketide synthase is mediated by the thioesterase (TE) domain
CC localized at the C-ter of the protein. {ECO:0000250|UniProtKB:Q5ATJ7}.
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DR EMBL; MZ277879; QXF68953.1; -; Genomic_DNA.
DR UniPathway; UPA00213; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR041068; HTH_51.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 2.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Transferase.
FT CHAIN 1..2500
FT /note="Non-reducing polyketide synthase atr1"
FT /id="PRO_0000455741"
FT DOMAIN 1649..1725
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 13..260
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000250|UniProtKB:Q5ATJ7, ECO:0000255"
FT REGION 388..811
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000250|UniProtKB:Q5ATJ7, ECO:0000255"
FT REGION 908..1199
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000250|UniProtKB:Q5ATJ7, ECO:0000255"
FT REGION 1287..1583
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000250|UniProtKB:Q5ATJ7, ECO:0000255"
FT REGION 2164..2496
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000250|UniProtKB:Q5ATJ7, ECO:0000255"
FT ACT_SITE 557
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 995
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 2285
FT /note="For thioesterase activity"
FT /evidence="ECO:0000250|UniProtKB:Q5ATJ7"
FT ACT_SITE 2434
FT /note="For thioesterase activity"
FT /evidence="ECO:0000250|UniProtKB:Q5ATJ7"
FT MOD_RES 1683
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2500 AA; 273246 MW; 9A3969772327D0DF CRC64;
MASNHEELPS MVVFSPQSKA PKEGYLDELR SYLCGKAELR PLLDGIENLP NTWSIFAQRN
SDIAALTQGI RYTQALSDWA KHGTSSGISN VMSGILSLPL LTIIQVVQYF QFLEVKKLRH
SDFMERLRCR GGVQGYCGGL MPAIAIACSA TEAEVVTNAV KAMGIALGVG AYGELGDDEN
VLGPTTIVVR LKQEGQGGDI IKDFPDAHIS AITDPKTVSI VGSAPSLAEI QARVKSNGMQ
TQAMHLRGKV HNPENANLAL ELCMLCDEHE ELSLPNASHL TAPLRSNKTG KKLLDVSLTH
EAIETILASC CQWYDLLKGV CKDLEKTGTQ SHLFASFGIG DCIPLTPFHQ AGLQITKLDV
LSFVKALMPP VLPMSGHNHQ YAYPTDAVAV VGMACRLPGA NSVEELWDLI SSGGSTVTPV
PEDRMDIAGS FRAMQDPKWA AKQQWWGNFI SDIAGFDHSF FRMSPREAAS MDPQQRILLE
TAYQAMESSG YLGSHRRESG DPVGVFLGAS FVEYLDNTSS NPPTAYTSTG TIRAFLSGKI
SYYFGWTGPS EILDTACSSS LVAINRACKA IQNDECPMAL AGGVNLITGI HNYLDLAKAG
FLSPSGQCKP FDGAADGYCR SEGAGLVVLK RLSQALTDGN QILGVITGAS TNQGGLSPSL
TVPHSAAQVK LYQNILHQAG MRPEQVSYCE THGTGTQAGD PLEIESVREV FGGPKRQDSM
HIGSIKGNIG HCETAAGVAG LLKALVMVNK AAIPPLASHK SLNPKIAALE PDKLAISSCL
EDWRVSPRAA LVNSYGAAGS NSAVLLCQAP DIDNAPLHRV ATTEHTYPII LSAASKPSLL
SNAENIASYL RKATSKCTIA DVAFTLVKQR KRHPLQWITM ESSIDGLVKS LGSLQDPSNA
PQPKKVVMTF SGQSRQSIGL NKEWYDSFPL FRRHVNECDD LLQQSGFPSC KSAMFDKEPA
RDVVPLQCAM FAVQYASALS WIDCGLQVEA VIGHSFGELT ALAVSGTLSL KDALNLVATR
ATLMQSKWGP HKGTMLLISA ATEMVRKIIA GNRDVEIACH NAPTSQIVVG TQAAISEVEK
VLENNTEYRG IQSQRLNVTH GFHSQFTEPL LENLSESARS LVFHEPKILL ECCTLEELNH
VGPDHLARHT REPVYFYHAV RRLEQRLGTC LWLEAGFDSP IIPMTKRAVE FPERHTFLDM
KTPSGTNPTK MLTTATINLW QNGATSSFWG FHPIETTNIK QVWLPPYQFD RTSHWMPYTD
HALEMSKIQA VISNSEPLVE LSTKPPRLVE PRTKPSEKGE FSMNTQARRY TEIVSGHAVL
SRPLCPAAMY MECAIMAAQL SIGNIVGQAP WFENLTFEAP LGMDPDNDTT VVLKDDGSKS
RWSFVARSTS RSNPKRKPVL HAKGDFGFTT QTQVHRYERL VTDRMRHLQH SKSETLKSKR
AYGLFSRIVR YAELLKGISS ITLGDSEASA IIDVPLGAST EDSSATGLCD CVALDAFIQV
VGLLINSGDD CAEDEVFVAT GVENFSMSLA CDFDRCRTWL VFAMFTPSGN GKAMGDVFIL
TRDNVLVMTI MGVQFTKLPI TRLEKLLDSA NPKAHNTPIL KSSQQDSIVS ASSSSSTEHS
DDDSEDDGSR SPSHSDTSVD SESEAPADNG AAKKLKSLIA SYVGIAEDAI SDDANIADLG
VDSLAATELA DEISNDFAKE IDGGELPMMT FGELCRIVAP EMAAKPAKAK KKIPYKGKDE
ATVVESHPGK SQSEIKDLKA VVEPLPRSTP MLSDTTVVRS DPTQVLRQID TMFQSSADTF
GFTDYWTAVA PKQNKLVLAY IGEEFRKLGL DLWAVQPGAT LPHIEYLPKH EKVVQRLWDI
LADHGIVYNY DAAKVRSSKP LPDAPSTALL NELNALFPNF ANENRLMSVT APHFADGLRG
KTDHISLLFG SQRGQECLND FYNNSPQLAV MTDHLLTFFK QLLKEAPLEG SLRILEVGGG
FGGTTKRLAE MLEALGQPVE YTFTDVSSML VKEARKKFSK HSWMDFQSLN LEKDPPASLQ
RTYDIVIGTN VVHATSNIVN STTRMRSLLR KGGFIVLSEV TRIVDWYDLV YGLLDGWWAF
KDSRTYPLQP ADDWVRDLMK AGFETASYSR GDSEESNTQQ LIIGSTRPSK VASTSGLSEA
RLSKSYRIET MPYKIIDDTE ILADVFFPEH EVASEAMPIA LMIHGGGFMT LSKTAIRPYQ
TQFLVENGYL PISIDYRLCP EIDLIAGPMT DVRDALTWVR KQLPAIARTR GINVDPTKVV
VIGWSTGGHL ALTTAWTCED IGEEPPVAVL SFYGPTNFES EDIDRRRAEQ YPERTMSFDR
IRKSLSTKPI TSYDCPTGTD STGLGWVRPG DPRSELVLSL FKESHGLQVM LNGLSAADLA
KPPPLAKIQA ISPMAQLKAG RYNVPTFVIH SDCDEIAPFR DSEAFVEELA RRGVKTGLGR
VRGKKHIHDL ALKPEKDGWV DGAGVGYEFI FDVVGRGVRG
