ID S7PZF0_GLOTA Unreviewed; 3936 AA.
AC S7PZF0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPQ52677.1};
GN ORFNames=GLOTRDRAFT_112049 {ECO:0000313|EMBL:EPQ52677.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ52677.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ52677.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ52677.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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};
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DR EMBL; KB469307; EPQ52677.1; -; Genomic_DNA.
DR RefSeq; XP_007868953.1; XM_007870762.1.
DR STRING; 670483.S7PZF0; -.
DR GeneID; 19299491; -.
DR KEGG; gtr:GLOTRDRAFT_112049; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_2_0_1; -.
DR OMA; WQVTRKA; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000030669; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
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:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
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:0000287; F:magnesium ion binding; IEA:InterPro.
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; 1.20.1050.120; -; 1.
DR Gene3D; 1.20.930.70; -; 1.
DR Gene3D; 3.30.1120.100; -; 1.
DR Gene3D; 3.30.70.3330; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
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; 6.20.240.10; -; 1.
DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
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; IPR013785; Aldolase_TIM.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR041099; FAS1_N.
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; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR00556; pantethn_trn; 1.
DR PANTHER; PTHR10982:SF23; FATTY ACID SYNTHASE SUBUNIT ALPHA; 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; PF08354; Fas1-AflB-like_hel; 1.
DR Pfam; PF18325; Fas_alpha_ACP; 1.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF17828; FAS_N; 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 Pfam; PF16073; SAT; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 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:UP000030669};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2224..2299
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3175..3709
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 2186..2205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2658..2680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2186..2200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3936 AA; 432898 MW; 9DFA2C6882254058 CRC64;
MTAPNGHAVR HDDHEIHIRP VVIHSGPIRL TIPVSTETDQ WIAAEVLRDE FVHHQKTQDA
IDNTIELENE IEATVELFAR FLGFTAQKLN EECDSKKART SVLFHALKHF TASYLSDKDI
HTLTAKYDTD SRRTVIASYY QTIAALEAQS VSDIPRSSNS ALFSAAKEGR ASIYALFGGQ
GANEVYFDEL QALYDMYKPY VAPFLADVTS KVLLPLAAAS ESTAFYTHGL DVVSWLDGSA
TRPSTAYLAS IPLSLPLIGL TQLTQYFVVC RTSRLSPGEL RDALKGATGH SQGVVSAVAI
AASTTLESFY ENSRKALKWL FFCGLRGQEA FPVVALEPHI VQDSIEGGEG APSPMLAVTG
LSLKDLEVHI NKTNKHLADN SKLYVSLHNG PKAFVVTGPA KALYGLVTHL RKVRAPSGLD
QSKIPFSQRK PVFSVRFLVV NVPYHSPYLT GVTERMCSED LAGEELWKGE ELGIPVYHTE
DGSDLRQSES ITKSLCEQIF TQPIHWTVAT GFPNDATHAV DFGPGGLSGI GPLTARNLEG
RGVRVIVLGD KGQGVSELYE TKSIKYQDWW STKWAPSLVK TSDGQIHLDT PFSRLLGKPP
IMVAGMTPTT VKAGFVSAVL SAGYHIELAG GGHYNANALR AKVAEIQANI PAGVGITLNA
LYINPRQFNF QYPLWQDMRH EGLPIEGFCV AAGIPSTEKA AEIIDGLKAA GIKHVAFKPG
SVEGIRQVIS IAAANPDFPI IMQWTGGRAG GHHSCEDFHQ PVLATYGAIR RHENIILVGG
SGFGGADDIW PYLTGDWSVA YGVQPMPFDG FLFASRVMVA KEAHTSSSVK DLIVAASGVD
DAQWEGTYSK ETGGILTVRS ELGEPIHKIA TRGVKLWKEF DDTVFALPKE KRITWLKERR
AEVIAKLNKD FQKPWFGWKK DGSVAEDLGD MTYEEVALRM VRLMYVAHES RWVDPSLRNL
TGDWLRRVEE RFAGVNGGLK PSILQSYSSL NEPAPFLEQF FNTYPLAKEQ LLASEDSAYF
LAISQRPGQK PVPFIPVLDA SFEVWFKKDS LWQAEDIEAV FDQDPQRVCI LQGPVAVKHS
TKKDEPIKEM LDNITASLVS KLLERRYDGD VNKVPTVDYL APPTRGQDIA GLECEEDGNK
LTFRFGSSLP DKAAWLEFLA GPRLTWLRAL LTSPLVVQGP SYADNPMKRL FTPRVGQTVT
LTLGDDHVPV SLTAHGAARS HGKHKELFKA VEVRYNASDK AIEVVIYEDR RDTAVPLQLQ
FNYVPSMGYA PIHEVMSDRN HRIKSFYWKL WFGDDSEMPA LDVRERFTSP EVTISSSDVE
RFCAVVGNQT ESFKPARTEN VMAPMDFAIV TGWQAIMKAI FPAAIDGDLL KLVHMSNGFK
MVAGAEPLRA GDVCTAEAGI TSIRNTNAGK VVKVSGYVLR GGQRVVEVIS SFLYRGRFLD
FQNTFEIVEE PDYVVDLPTE ADVAVLLSKE WFEWGDDSKP LKAGTALVFR VKSEVTFKNE
TSCSSVSVSG DVFVRDQIKR LVKVASVEFE QEDCPGNPVV AYLQRSGTPQ GLMTPLPNEG
YTMASGPIPA TFIAPSSNEP YSSVSGDFNP IHINPYFSDY AALPGTITHG MWSSAATRRF
VENVAAQGRP ERVISYDVAF VGMVLPGDVL QVKLRHIGMR AGNLVIKVET INEQGEKVLE
GTAEVAQPTT IYVFTGQGSQ EPGMGMDLYN NSPAARAVWD AADAHLLDVY GFSIVEIVKN
NPKEKTIHFG GIRGQAIRQR YMEMSYDTMD KDGNIKTLPL FADINVRTQR YTFSHPSGLL
FATQFAQIAL VVTEKAAFED MRAKGFVQKD CAFAGHSLGE YSALASIADV LPISSLVDVV
FYRGITMQRA VERDAENRSN YAMCAVNPSR ISKTFTDAAL REVVETISQR TGCLLEIVNY
NVEGQQYVCA GELVALQTVT NVLNYLKVQK IDISKLTETF TIEQVKEMLG EIVDNCYAKA
LELQKAQGYL QLERGFATIP LPGIDVPFHS RYLWAGVMPF RAYLSKKIDA THLNPDMLVG
KYVPNLVAKP FEVSRDYAQL IYDQTSSPRL DKVLRKWDEE HWDSPEQRQK LAYIILVELL
AYQFASPVRW IETQDIFFAK YKFERLIEIG PSPTLTGMAT RTLKAKYEAE DDSVGRSRSI
LCHAKHAKEI YYQYEDEPEA VSVEESNADF TATEPAPSAS TPALVSAPAA APPSVAASIE
DVPLKASEIL ITVIAQKLKK KIDEVPLSKS IKDLVGGKST LQNEILGDLQ LEFSSAPEKG
EELSLEELSS ALAVGHSGAL GKYTSGLVSR LVGGKMPGGF NISAIKSYLA KSWGLGPARA
DGVLLLGTTM EPPKRLGSEA EAKTWLDSVV SVYAQRSGIS LSAASAGGGG GGGGGGAVIN
SEEFLKFRSE QDQFVSQQIE VFMRYLKRDP RAGEIAYDKE KANSAVLQGR LDNIVREHGD
VYLDGVQPVF DPLKARHFDS SWNWVRQDAL LMFYDIIFGR LTAIDREITA RCIAIMNRAD
PELINYMQYY IDRCDPTRGE TYALAKQFGQ QLIDNCLEVV GQPPRYKDVT FPTAPHTEVT
DKGDIVYKEV VRENVRKLEA YVEEMASGDT IAGSLNIQKV QDDVLRLWNV VKSQPEITEE
QKNRIKALYE GVVRSLRKGS DARPRTTGAP RKRRSSSQFL RPSVSSIASV SSDKVPLLHL
KRKVGTTWEY SSNLTGVYLD VLHEIATSGT TFKDKNALLT GVGKGSIGVE IVKGLLSGGA
HVVITTSRYN RSTVEYYQGI FQRFGSRGSA LTVVPFNQGS KQDVHALVDY VYETLGLDLD
YILPFAAIPE NGREIDSLDD KSELAHRIML VNLLRLLGAV KVKKASRHIV TRPTQVILPL
SPNHGLFGND GLYSESKISL ETLFNRWNSE SWGEYLGLSG AVIGWTRGTG LMEATSMVAQ
EVERHGVRTF SAKEMAFNIL GLMHPLLFSI TQVEPIWADL SGGMDRLPDL AELTTRIRLD
INKKSQLRRA IARDNAADFK VTHGLEAERV LQTVNVTPRA NFRYEFPTLE DADSLEDVAK
LRGLIDLDKV IVVTGFGEVG PWGSSRTRWE MEARGELTLE GCIEMAWMMG YIKHFDGRLP
DGSLHVGWVD AKSGEPVDDK DVKAKYEKDI ITHAGVRLIE PELFRGYDPK KKVFHQEIEL
LHDLEPFEVS AAEAEKFKFE HGDKCDVWAG EGDQWLVKLK KGTRVLVPKA FKFSRSVAGQ
LPTGWHAGRY GIPEDIIAQV DRCTLWTLVA AAEALNMSGI TDPYELYQYV HPSEVGSSIG
SGMGGVESLQ KMFKDRREEK EVQNDILQET FINTTAGWIN LLLLSSSGPI KIPVGACATA
LQSLEIACDT LLSGKAKVML AGGFDDMSEE GSYEFANMKA TSNAETEFAM GREPTEMSRP
ATTTRAGFME AQGSGVQVVM SARTALELGA PIRAVVAFTS TSTDKAGRSV PAPGRGALTV
AREVPSKHPL PMLDVTYRSR QLAFRRKQIS QWLSNEHELL RAEVEFRKEH GEDVNEEYLA
SRVADIEQEA ARQEKDALAT YGMLQGADPR VAPMRRALAV WGLTADDIGV LSIHGTSTGA
NEANETHIWN DVLTKIGRTP GNAVPIMAQK SLVGHAKGGS AAWQVIGLVQ SVASGIVPGN
RNNDNVDSAF QEYSLLLFPS KSIHTDGIRA GVMSSFGFGQ VGGTALIVHP RYLFGALEPS
TYESYKARNR LRSLQCYKAM SDMMIRNSLV KIKDGPPYSK DLEAPVLMNP MARTTFDSKS
SSYSFSAKLD TKPPMDVSNV KTVSELLNST GSVAGVGVDQ ELISSVPSWN PTFVERNFTP
SEVEYCRSQP SPPASFAARW VGKEAIFKAL GVASKGAAAA MKDIEILPDP ETGAPQVQLH
GDAKQAAEAK KIEKVLVSLS HSETVAIAFA QASTSA
//
