FSO1_OMPOL
ID FSO1_OMPOL Reviewed; 4547 AA.
AC Q52US9;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 23-FEB-2022, entry version 72.
DE RecName: Full=Nonribosomal peptide synthase fso1 {ECO:0000303|PubMed:16019163};
DE EC=6.3.2.- {ECO:0000305|PubMed:16019163};
DE AltName: Full=Ferrichrome A biosynthesis cluster protein fso1 {ECO:0000303|PubMed:16019163};
DE AltName: Full=Ferrichrome A synthetase {ECO:0000303|PubMed:16019163};
GN Name=fso1 {ECO:0000303|PubMed:16019163};
OS Omphalotus olearius (Jack o'lantern).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Omphalotaceae; Omphalotus.
OX NCBI_TaxID=72120;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DOMAIN.
RC STRAIN=TA90170;
RX PubMed=16019163; DOI=10.1016/j.femsle.2005.06.013;
RA Welzel K., Eisfeld K., Antelo L., Anke T., Anke H.;
RT "Characterization of the ferrichrome A biosynthetic gene cluster in the
RT homobasidiomycete Omphalotus olearius.";
RL FEMS Microbiol. Lett. 249:157-163(2005).
RN [2]
RP DOMAIN.
RX PubMed=16502473; DOI=10.1002/cbic.200500301;
RA Schwecke T., Goettling K., Durek P., Duenas I., Kaeufer N.F.,
RA Zock-Emmenthal S., Staub E., Neuhof T., Dieckmann R., von Doehren H.;
RT "Nonribosomal peptide synthesis in Schizosaccharomyces pombe and the
RT architectures of ferrichrome-type siderophore synthetases in fungi.";
RL ChemBioChem 7:612-622(2006).
CC -!- FUNCTION: Nonribosomal peptide synthase; part of the siderophore
CC biosynthetic pathway (PubMed:16019163). Omphalotus olearius produces
CC ferrichrome A, but no other siderophore has been detected
CC (PubMed:16019163). Ferrichrome A consists of a hexapeptide ring made up
CC of one glycine, two serine, and three N(5)-hydroxyornithine amino acid
CC residues, the latter acylated by trans-(alpha-methyl)-glutaconic acid
CC residues (PubMed:16019163). The biosynthesis of ferrichrome A depends
CC on the hydroxylation of ornithine to N(5)-hydroxyornithine, catalyzed
CC by the monooxygenase omo1 (PubMed:16019163). The second step, the
CC acylation of N(5)-hydroxy-L-ornithine is probably catalyzed by the N-
CC acyltransferase ato1 (PubMed:16019163). Finally, assembly of
CC ferrichrome A is catalyzed by the nonribosomal peptide synthase (NRPS)
CC fso1 (PubMed:16019163). {ECO:0000269|PubMed:16019163}.
CC -!- PATHWAY: Siderophore biosynthesis; ferrichrome biosynthesis.
CC {ECO:0000305|PubMed:16019163}.
CC -!- INDUCTION: Expression is iduced under iron-depleted conditions
CC (PubMed:16019163). {ECO:0000269|PubMed:16019163}.
CC -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC (C) domains) which when grouped together are referred to as a single
CC module (By similarity). Each module is responsible for the recognition
CC (via the A domain) and incorporation of a single amino acid into the
CC growing peptide product (By similarity). Thus, an NRP synthetase is
CC generally composed of one or more modules and can terminate in a
CC thioesterase domain (TE) that releases the newly synthesized peptide
CC from the enzyme (By similarity). Occasionally, methyltransferase
CC domains (responsible for amino acid methylation) are present within the
CC NRP synthetase (By similarity). Fso1 has the following architecture: A-
CC T-C-A-T-C-A-T-C-T-C-T-C (PubMed:16019163, PubMed:16502473).
CC {ECO:0000250|UniProtKB:A0A144KPJ6, ECO:0000305|PubMed:16019163,
CC ECO:0000305|PubMed:16502473}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; AY929618; AAX49356.1; -; Genomic_DNA.
DR SMR; Q52US9; -.
DR UniPathway; UPA00783; -.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0031169; P:ferrichrome biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1200.10; -; 5.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.559.10; -; 5.
DR Gene3D; 3.40.50.12780; -; 3.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR Pfam; PF00501; AMP-binding; 3.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 5.
DR Pfam; PF00550; PP-binding; 5.
DR SMART; SM00823; PKS_PP; 4.
DR SUPFAM; SSF47336; SSF47336; 5.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 5.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE 2: Evidence at transcript level;
KW Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Repeat.
FT CHAIN 1..4547
FT /note="Nonribosomal peptide synthase fso1"
FT /id="PRO_0000444315"
FT DOMAIN 737..812
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:16019163, ECO:0000305|PubMed:16502473"
FT DOMAIN 1823..1899
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:16019163, ECO:0000305|PubMed:16502473"
FT DOMAIN 2910..2986
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:16019163, ECO:0000305|PubMed:16502473"
FT DOMAIN 3440..3516
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:16019163, ECO:0000305|PubMed:16502473"
FT DOMAIN 3998..4074
FT /note="Carrier 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:16019163, ECO:0000305|PubMed:16502473"
FT REGION 200..612
FT /note="Adenylation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16019163,
FT ECO:0000305|PubMed:16502473"
FT REGION 851..1259
FT /note="Condensation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16019163,
FT ECO:0000305|PubMed:16502473"
FT REGION 1295..1693
FT /note="Adenylation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16019163,
FT ECO:0000305|PubMed:16502473"
FT REGION 1930..2365
FT /note="Condensation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16019163,
FT ECO:0000305|PubMed:16502473"
FT REGION 2390..2769
FT /note="Adenylation 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16019163,
FT ECO:0000305|PubMed:16502473"
FT REGION 3015..3429
FT /note="Condensation 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16019163,
FT ECO:0000305|PubMed:16502473"
FT REGION 3557..3967
FT /note="Condensation 4"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16019163,
FT ECO:0000305|PubMed:16502473"
FT REGION 4136..4461
FT /note="Condensation 5"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16019163,
FT ECO:0000305|PubMed:16502473"
FT MOD_RES 772
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1860
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2947
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3477
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4035
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 4547 AA; 499822 MW; 769EFB27CC5A85AF CRC64;
MSSLEGRFTL PATCIPCVFP RVISSTLNAR LDVITINSPE SKLDLVAFAT VLRALLATSG
EFSFGLGKNQ FVVVESVDET EKEVEEKLSV HDASQVTGSE NVQARIDSDA LEIDGSVPSI
VSSSQELVLF HLNAQPSSVS LVYSTDYIPD SLAKSLLELY FIKCAAKFDI GAISGALSIV
NHPVQSVLSN RKPLLHAAFV ERADETPDAL AIDYLSAIDE YPLRKTLSYG DLDKYSLAVA
RILRGIVPST EKAIVPLALP PSPELYIGYL ATLRAGYAFC PLPGCDAAPV ERIRELITDV
SASVVLGLGS RPPWLADLGH IRWVDISLEA DNFALKSASL VDGQDWVEPE ADDLAYVLFT
SGSTGKPKGV QITHLAAASS IAGHLAVRPL PPYTRWFQFA ASTFDPSLME TFMNLSSGTT
ICAANRQRLL TDPESVLCEL ECTHMMATPS FAAMLRPERL GNTASKSFLE HGVKFELWTM
GERLLEKVIA AFSRPDEGYV LCNAYGPTEA AINTTLRVHP RHETGARLGQ PIPSATMVIL
HPTEPWLVPQ GFPGELGLAG PQLARGYLNM PDQTARAFVL VDGIGRVYRT GDKARLVPDS
NNEWTCVEYL GRMGLGQVKL SGRRVELGEI DVVMASVPGV QSAHAIVHQQ SGNGAVQLVA
FLTPDDEKLV EKVKAVVDAR LPQHMRPSRY FLGESVPRST SGKADRRAIG AVIASRIAQS
DADNRTTDTE GEIVADREML ERIIKIVAET VDVLDNSAVT PISNLFDLGI DSLRGVRLLS
LAREAGIQGL TIKDLLQNAT PIALVNALCS RQNDADSSQY LDTLLRFTAE AAPAVRRELS
LSDNDPLPPI LPATPMQAGV LALYLRGGPA SKGYINHSVY KLASGIDLDR FKDSWVHIVQ
RNDILHSRFV LVDNSATSPF AMVTLNDASV SWVERTGDDV EALVETYLKD IPSDFSLTSL
KAFALLKNAD GSDVRFVLSL HHSISDGASL ALMLEELSLN YRGNDVSLRR EGFEHSVKDA
LTADTDANTS YWKEQLEDFT PDAFPDLTGL RPSAKYTGHH VTTVISSMSF SNLLKTSRAL
KSTPLAVLQA AWASILLAYS ESESPDIVFG SIVGGRSSEA LEYTVGPVFT AVPVRVRNVS
GVTTGDLLST FVSNNVQGLV HRYPPVSVLS GSSGIIYDTT IALQHFGQEQ SQTALWTAAD
YPAMETEFAV VLEVWPEEDD SIRLRATCSN HVLIPSASEA MLHQFDDILK FILENPAEAQ
FANVTDGVRQ RLQSSINSHP QPFPVAPNTL IHHEFEQNAR LHPDALAIWF KEDIEHPEND
IRWTYRELNE KANRLAHLLA STYGNLCDRA IPLCMEKCPE LYVAILGVLK AGAAWCPVDF
AAPEMRKQNL FARAGGPVVL ISSNTEFSHI KAALPGGLDI FSLDDPRLND QPDSAPVIET
TPSHLAYLIW TSGTTGLPKG VPIEHKAAVQ SLKVLQREIP HNTAVRCLNF SAYTFDVSVL
DVFYALGSAC GTLCSSRKEI LVGKFAEAVN AFEATQAFLT PAFMTQSSLD ECRTLESLIS
IGEKLPDTVA DKWCRPGTAS LNTYGPAEST IIATYRRFTP NDSTKAHNVG LPIQTVSCFA
MKEGRIVPRG AVGELALGGY QNARGYHRQP DMTAKKFIEH PTAGSIYLTG DIVRFLHDGT
CEFVGRNDDL VKLGGIRVEL SEISAALESC HPAVHEAVTI QLSRPDRPQK IVCTFVAAPG
ISGDKNICIG TDAVEIACAA KERAELSLPV FMHPNVVIIV KRLPHTASNK IDRKALGEYY
CDLDIMAWEN SLADHMGTGD IEATWSETEL KIRDTVSELT GSPKEWISKT THLPALGVDS
IRALQLASRL RAIDVNISVQ DILQHSTIRQ LARQSETASS NLHNVISPWL EGFSSRWSPV
VQRDFVEKVE RVLPCAPLQE GMLGESVKNP EAYWSHRLFP LNKNIDLGRL SNAWNTATEH
YEILRVVFMP AAAYASSNVM ETDPNSVFLQ VLLSRYEVPS TRQQIGRSEV YSMAREYARN
IAISRSRSLQ PRWSLIVLES TDGHSWMMFS MHHALYDAHA VTYLLADIQR RYHGISPSPQ
LQLTSALSRT FFANGPQESL DVWRDILTPF ADRNALEWPT LTDGRSREDA RFFSSAFERD
YFSLTELATK AGGTAGHVLQ AAWSIVSAAY LETDRVVFGE TLSLRLEDHE LQHAIAPLIT
TKPVAAHLKG TTTPRVLIRE LADLTKLASL HRSIGFQHIR KILQRPINQP LFPSIFVIYF
EEDSSVPSDI AENLWSSPHD VSSLGVEHPI AINVNVSGEK VVVNVLGNGA IMSESQVELL
SQQFNAVLTR MLNEPDVPIM SLVSALDEMH LSIVKGASPM SQTHPLHWLE KFALTRPDAV
AVSSYRSLSN EVPNEIWTYR ALEEASNRVA HWIRRRYHSG IVAFCMPRSH TSIVYQLGIF
KSGNIYLPIG EEIPAFRKRL IFRTSQTSLV FTTKALLHEF KSLDKNAIIC VDDVQHLLEV
SDSAITKPPL SIPETSCILV DDGHLCTSRA SLVSSQNLIS MVEGFVHEVY SSVLSLDENI
FLSWMPSSAD IHLIELFAPL RMGMKSASIP HQFLHQDASA VFHRTGASHS FLTTLGLNRR
FETVDLPSVK CAIFTGIPSR AALLKEWRNG QGLMVLRAFG FPGLFTLGQY EYDLPMNIGK
PVNSCTTLVL RQDSSAITLR GEAGELCIAE DILSPQYSKA HVFTDTVGYG RVHRTRHVGR
VRADDTIDYN GPINIYRNNA GQVIDLTELS ELLRSTSHLS IDVATFVFDH PEGIRNYIVS
FVSRSSSADP LNGALPVVVV TDFAFTSNLL GHYKRHVSAH LVPDFIIPLD YLPLSSLATG
RKHEARLKRV FHNFSLSALN QGSEKKRSAR SLTAVEEEIR AILSKTTGIP VQTIDADSTT
IELGIDSLSA ISLSYQLKSA GYFVPPHVIL SGPSVAKLGK SSKAIVESNT KVLSSWEVED
SIKKFVCEQL KVEVQSVLPC LPLQEGLIAH TLNSAKPIYV NHFVLRLDEA DPMLLRAAFE
ETVKANDILR TCFVAANQNI VQAVLSETPE IWRSVSVESQ EDLLSKLRHD MAGVEHDVVQ
NLGQKPPIRL GLYLSDSSPT YFCLTMHHAV YDGQSLSMLL SEVRDRYTGC FQIQRGSTSN
FLNYLARQSQ DASRAFYSDY LHNIPRPPVS PFVDDTLSSH HQSLKLDVSL SHLERISRSV
NASLHSLALA AFGVATAEYR KRNDLVIGVV LSGRSVLVDG IETMLAPCIT TVPVRVRTGK
SEVFSDIAQR IHTEMSSLLA YQHTPLRLIQ RWLGSSEPLF DTLFSFNRMT TGSSSSTLWS
SVESKAALDY PFALAIDADS TSDSLVIRAG HIPSFGSKAT VKTIMLRVAE LLANLDTRID
LLVSHKLLET QEDSPMYDSS AWSQEEILIR NNVAEVCNVD RNLVTKDISF LHLGIDSITS
IRLAQQLRNA GLAIPTFAIM RHPCVGALAE YLKDNPMVST SAIALRELNE IQEVLRKEYG
DSIPRLAAED EILSLFPATP LQTGMLSQTI YSGGRLYMVH HSLQLDINTV SLERLRNAWE
VVVASTDILR CSFHVCPSGD YPWLAAIHSK TPLRWKEYDV PSTSVLRLIA FQIENTELIK
DESGFATPPL SLHLINSPDM CVLIISMHHC LYDGLSLAYI LEDVTAAYFG HEAVRRPQFT
DAVPFVLYSS KDRAHFWQKR LSGFSASPIP KRQPEGHSPN LASQFVDLPD GSLDAIKEMG
VLVQATALLA WGKTLAALTG SLDVVFGQVV AGRAIELDNA LLVNGPLFNT VPFRFTISDP
SWSNAEGVQA QHAFNIAAEP HSHVPLRTIQ AEWRSQNMSR DTLFDTLFVF QQGKGPSMSS
LWTRFNVSDD ASASQYPLSL EIIHTNNKIE LRAGCQAGIM SQTELQDLLR LLHDTLLDIV
VHPTANILDQ SPSLKDLHTV PQHRAPSAQE GHSKSPGRAL TVNEETLRDV FSSVTKIPKD
QIGLETPLYA LGLDSVGAIQ VAAKCRIDGL NITVVDIFAG ETIAGICKAY ETRDIPETGT
LLEPSELVSS NIRDKALALL NLEQESVQEV LPVLAGQSYH LGAWLACGGI SYEPVFAYRA
AVPLDPERLR KAWNALRSQH GILRTSFAAT SPDEVVQVVL KQLPDSDPSW SFVEVEGDFD
QRVREQARIE YSRPSTLFRP PARARLVRVG NQDALLLVFH HATYDAWSIP LLVRDLCALY
DGLHCKSTSN FTGLVQYLHT TSDKGSQATF WRDSLDADSG VRPTILPTTS PSSGLKQVFV
RVPGVVSSVD QLSNRCQTAG VGLQALVLAV WGRVCQNLIR STSAPILGVY HTGRAASFDG
LGELAGPTVN VLPMRVPVAS PGKIWDVAKQ IQRDLGRRTA FEHSSLREIM SHVGHKNGPL
FNVFVNLLWH GDKIRTIRQD SLLSSLSIGP PTDYAPDKPF ALKSSVNALD HSHLPKFGLY
IDVVLDSKDQ SLAVAARCHE ALLNKEQLRS VVDSFGDGVV DAIGELE
