ID G7DY64_MIXOS Unreviewed; 2782 AA.
AC G7DY64;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAA95524.1};
GN Name=Mo02179 {ECO:0000313|EMBL:GAA95524.1};
GN ORFNames=E5Q_02179 {ECO:0000313|EMBL:GAA95524.1};
OS Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC Mixiales; Mixiaceae; Mixia.
OX NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA95524.1, ECO:0000313|Proteomes:UP000009131};
RN [1] {ECO:0000313|Proteomes:UP000009131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC {ECO:0000313|Proteomes:UP000009131};
RX PubMed=21478649; DOI=10.2323/jgam.57.63;
RA Nishida H., Nagatsuka Y., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL J. Gen. Appl. Microbiol. 57:63-67(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC Evidence={ECO:0000256|ARBA:ARBA00001572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+);
CC Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83139; EC=2.3.1.86;
CC Evidence={ECO:0000256|ARBA:ARBA00000343};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAA95524.1}.
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DR EMBL; BABT02000062; GAA95524.1; -; Genomic_DNA.
DR RefSeq; XP_014570033.1; XM_014714547.1.
DR STRING; 764103.G7DY64; -.
DR GeneID; 26264608; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_2_1_1; -.
DR InParanoid; G7DY64; -.
DR OMA; WQVTRKA; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000009131; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0004317; F:(3R)-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:InterPro.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00828; elong_cond_enzymes; 1.
DR CDD; cd03447; FAS_MaoC; 1.
DR CDD; cd08950; KR_fFAS_SDR_c_like; 1.
DR Gene3D; 3.30.70.2490; -; 1.
DR Gene3D; 3.30.70.3330; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.25.70; -; 1.
DR Gene3D; 6.10.140.1400; -; 1.
DR Gene3D; 6.10.140.1410; -; 1.
DR Gene3D; 6.10.250.1930; -; 1.
DR Gene3D; 6.10.60.10; -; 1.
DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR040899; Fas_alpha_ACP.
DR InterPro; IPR047224; FAS_alpha_su_C.
DR InterPro; IPR040883; FAS_meander.
DR InterPro; IPR041550; FASI_helical.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR039569; MaoC-like_dehydrat_N.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR00556; pantethn_trn; 1.
DR PANTHER; PTHR10982:SF21; FATTY ACID SYNTHASE SUBUNIT BETA; 1.
DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR Pfam; PF01648; ACPS; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18325; Fas_alpha_ACP; 1.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF13452; MaoC_dehydrat_N; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009131};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1083..1161
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2035..2572
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 38..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2265..2289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2782 AA; 304604 MW; D47000736B817D9E CRC64;
MESMTDFDKL PLAVELDFDE ATDLIDLTLY EHIRPPSLVH SSGSSSSDSG TSSTDILQSD
DEILGPDNVV PLKLQYAYKP QYGFAPLHEV TEGRNERIKQ HYWRLWGLDT PSTAAQTGAT
DQDGGMRQGF SSLSVDAEFI GDDVYIDHQD VQRFCRVVGN AQQAYRADAS ASLDAKGKSR
EIGLPVPMDF AMKLGWKSLM TAIFPQAIDG DLLRLVHLSN AFSYLSDTIV LRTGDTVNSS
SRISKVVNSD SGKVVTVTGT IFLKSSPSGT LDDHTGSVPV VEVESSFLYR GNFDDFAGTF
ESRKETNYAL TFKSAQDVAV LKSKEWFEWL DDSVLLTIND TLTFEVESDI RFKTKASFAS
LDVTGFATAL KQVSDGRSET VKVAEINYVS AGTTKGNPVL EYLKRHGQAL HQPVPLVAPY
ALAGPTSEEK GVDNVFKTPA SNQAYSDVSG DVNPIHVNPY FSDLAQLPAP ITHGMATSAM
TRRFVETIAA ENQSERVRSF QASFTGMVLP SSKLRVDLKH VAQQNGNKII SVATVDTETE
QPVLVGQASV AQARTCYVFT GQGSQEQNMG MDLYASSPVA RAVWDAADTH LGDVYGFSII
DIVKNNPKEL TVHFGGLKGH QIRQRYMEMT YHSTDKSGQV QVLPLFADID LRTSRYVFSS
PTGLLSATQF TQVALVVTEK AYFEDLRAKG LVQPDCPFAG HSLGEYSALA SIANALPIHA
LVDVVFYRGI TMQRAVERDH LNRSQYGMMA VNPSRVGPTF TDPALREVVT SVAEKTGRLV
EIVNLNVEGQ QSVVAGELVA LHTLTNVLNL LKMQKIDIWK LMEQMSLEDV REKLGEIVQE
CWTVSLEKQE KEGYIHLQRG FATIPLPGID VPFHSRYLWA GVMPFRTYLS KKLKIEDLKL
DLLVGRYIPN LVATPFEVTK EYAERIHTQT ASPPLEKILK NWEKESWGSD EKKPMLGYTI
LVELLAYQFA SPVRWIETQD LLFQKFKFER LVEIGPGPTL TGMASRTLKL KYEAQDAANG
LKRHILSIAK NQKEIYYSFE DEPEVAEAAP TPTSAPVVAV PAAAAPVAAA PAASTAAAAE
IPDQPLKAVE TLRAIIAQKL KKPIGEVPLS KAIKDLVGGK STLQNEILGD LQGEFSSAPE
KGEELPLEEL GAALGVGYGG SLGKHTSGLV SRMVSSKLPG GFGISNTRGH LAKQWGLGPG
RTDGALLVGI TMEPAKRLGS EAEAKAWLDS VAQAYAQQAG ISLSAPGASA GGGGGSGGAV
VDSEALKQLQ ASQDEFVSRQ VEVLLRYLKR DSRDGHRLND ISTREALALQ SQLDAISREH
GDFYISGIQP TFNPLKARHF NSAFNWVRQD ALSMFFDVIY GRLTTVDRDV TRRCLIIMNR
ADRPLIEYFK YHLDRVDVTK GETYQMVKEF GTLLLQNCEE VIGTPPVYKD VTFPTAPRTT
IDERGNIVYE EVPRPRVSRL EKYVAEMAAG TSAQPQVDLE KVHETLSSLY RLVKSNTSVS
KAHLSAVKQL YGEVVKTLGE SKKAVTRPTG SARARRNSNS FLRPEKVNEP VKISSSAKPL
LFLNRKVGNT WQYSERLTSL YLDILKEIAT AGTTFEHKTA LLTGVGRDSI GVEVVKGLLS
GGARVIVTTS SYRRETVEYY QSIYQEVGSR GSSLTVVPFN GGSKQDVEAL VEYIYTDMAI
DLDYVLPFAA LSENGREIDG IDDRSELAHR LMMTNLVRLL GAIKAKKASR RFITRPTEVV
LPLSPNHGLF GGDGLYSESK IALETLFNRW SSESWGTYLC IAGAVIGWTR GTGLMAPTNM
ISEEIEKHGC RTFSAKEMAF NILGLMHPLV MDITQVEPIW ADFGGGMSAL NDLHILTTRI
RNSIKSEADT RRAVSIDNSF DFKIINGVEA ESMHKRVNIQ PRAHFQLPFP ELKPTFDGNS
LSELRGVIDL DKVIVCTGFG EVGPFGGSRT RWESEVNRFF SIEGLLELAF VMGLITHFDG
KLKSGQSYVG WVDTKTQEPI DDKDVRAAYE KHIIEHTGIR MIEPELFKGY DPKRKGFTQE
IELNHDLEPI ETSPEDAEKF VLEHGAQFVD SWTEGDRCFV KFKKGAKLFV PKALRFDRLV
AGQIPTGWDA TVFGIPADII SQVDRTALWA LVSVAEALLS SGITDPYELY KYVHPSEVGS
SLGSGMGGMQ SLSSMFRERR EERDVQKDIL QETFINTVAG WVNLLLLSSS GPIKIPVGAC
ATALQSVEIA CDTILSGKAK VMIAGGYDDF SEEGSYEFAN MQATSNTETE LASGREPNEM
SRPMTSTRSG FMESQGCGVQ ILMSASTAIK MGATIYGVVA YTATATDKAG RSIPAPGRGV
LSTAREASSS SPSMLLDLKY RKRQLAFRRG QISQWLDNEL NCLEMEKQGR SGANAALSTD
DLSHRMTEIE REASRQEAEA VATYGMLEGA DPSIAPLRRA LAVWNMTIDD VGVASLHGTS
TKANDKNESE VYNSQFQHLG RTVGNACPVI SQKWLTGHPK GGAAAWMLNG LAQSINSGII
PGNRNADNIA PEMQAFEFLV YHSKSIQTTG IKSGLLTSFG FGQVGGQCLV LHPDYLLATL
DQSRYDVYKT ANATRKQQSY KKFNDMFTER NLVVLKEAPP YTPDLEKEVL LNPLARVEPT
KLGSYAFTAK SVRATLASQV EGVDAVGTDV EVIADFAVDN DTFIERNFTS DEIAYCHAAP
DSKASFTGRW AAKEAVFKAM GVKGKGAGSA LKDIEIIASE TGPQVKLTGD AALAASERGF
KTFSVSISHT DGVAVSVAMG QR
//
