ID M2RA57_CERS8 Unreviewed; 2574 AA.
AC M2RA57;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
GN ORFNames=CERSUDRAFT_96782 {ECO:0000313|EMBL:EMD35671.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD35671.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD35671.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD35671.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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DR EMBL; KB445800; EMD35671.1; -; Genomic_DNA.
DR STRING; 914234.M2RA57; -.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase 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 CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 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; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
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; IPR013120; Far_NAD-bd.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..421
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 2574 AA; 282414 MW; 1EA37C53ADD9BD7C CRC64;
MASGVAIVGI SVELPSGNYS EENLDHNSFF EFLLNYGESY ERLPRDRFNV EAWRGNGIGQ
IHVDGGTFLK EIDSFDNIEF GVSSRDARAM APVTKKLLEN CFLALLDSGI DYRARNVGCY
TAGNSFELSN ITEPDEYEPQ GSFAGYAAMV ANRVSNHLDL LGPSLPTDTA CSSTLVALHL
AVQAVLNGDC EAAVVGGCQL NHRLMDWITY SQGSLLAKDG KCKPFDASAD GFARAEGCVA
VVLKTLEDAL RDNDYIYATI LGTAINNGGA GAPPGAPVAD AQRDAMLQAF RRAGRCPKDV
DYIELHATGT AKGDPTEANW VGKEFQREDE VLIGSVKGNI GHTEITAFLA SLSKVLSILQ
RGTIPPNVNL TDPNPEIKWA EYRLKVPTSP MLLPRHSPNT HLVSMAGSGI GGSNGHVVLE
GPPLRAPVGA QQHLKARRPV LLLAGGLTPR SAAAVAESII ACIEGGEVDV SAMSTILGRR
ARQMTWRSYV VSGGDTSNSI SFGEPQHCPR NANPLVFVFS GQGPQHINMG RELFKTFPVF
RNSVLNMDNT YKTATGKSII DDWGLFGGNC STALPDVWPI SLTLPAIAIF QIALFDLLVH
LGINPDIVIG HSAGETAVLY ASGAAPKAMT VELAVLRGVI FTQLEHQGGT MAALSCTAHE
AMQILDQACA QEPGCAVEIA CYNAPAAVAI AGHMRAVDRV VELAQARGIY IRKLPTRVPI
HSSLMDACRE EYCGGLYELF ARYPGAHVPK ILTYSTLTGG PFGGPFDADY FWQNTRGEVR
FTETVEAIAS YGSHTFVEIS PRPALASYVR SMAQEPNIVL TTVRRQRSGQ DPSEYRDVLE
LCGQLTITGH NCVDFTVLNG RACYEVQVPL PSYPFSKKRF PLYPDTAGYR KQLEPRRGPL
NHRHLRVNKE SHPSLGEHVI RGEPIMPAAG FIEMALEFGA RTLINVNLQS ILSLSAERPV
SLQVRLQGSF WTVSSTVPTS KISSNIDSDH IERLHADGFL SFEAVPTYPD LDVSGLRKHL
QNNVGSDFYP SLSYYSSYGP RMRRVTNVYF GRNEALASIC GMDDILSEDA AYFLHPAILD
ACIQVSAYKP FHGNFDPNVY YLPAHVDAVF VHEPLKTSYF PAHLYAHVEL RAWHPDHMRY
DVSLVNDFGK RLCTVKGLRM TKHHINPLAS VSGPLELVLQ PISILSLPTT SGRISTAHQN
TQLFEISDEI ELHHQYRTNG VHDCSDVQYW CHSRDIQALN LESQSGLSSH EDTTGSVIEG
VLHTILSHIS DQSHIRVIRV LISRLHPIML ESFAQVLKGF PAVFFEIYIS SDDTSATLLV
EDFSGIVRTA ATDIQRSFFE MIFTSPNDFP EAVIQSFGSM LVPGGVIVFA EGLPKPLGHR
YLSLDTVRHV SSTPTLPLET LEKLGFSVVQ PHGPDCAIAQ NCTADALQAT EPLYDPLEAF
VFQYELRNEV ELQWEFSGLN IRQELDVWIL ASEGKDGGSA VGMVRALRRE YSSWTIRLVV
FPLSYPEEMR LQCLRRLPTY MKEELDILVS RTGDFTVFRL APVGRPPHDH NPARWNDTTS
DIPHGHVLVH VLYSSSHYDI SALVASVDNA NNTGIREGSI LLAMITGTPG TSLVLDVTIT
CSVPPSLLEQ VSMVVQMMAP LVTAVLAPGL AAFRSPARLR TLRILLTHAD IPFGRIIKSI
YAEKATLTEV VENITLFDLA SLESQPFDLI ISGYDDHAHS QVLRSILRPG RGRLFLWGNR
QGLRELIDRE LYTVVDAMNC VLQSLDEQPR IICENTSITP SLAPSDVIVT QVSPQAISTG
VTFSADKTYL LVGGIGSIGA RLALYLYERG ARHIVVSSRT GARGLRTSNN LMVYRIFEYL
KGISDLDIRL VAVDASSRHE MKTLRDNINP KIAGCIILTA VLSDRVFQYL EEEQFTAVFA
AKIGVLDALI DTIDVSSLEF LVAFSSVSGL FGVGGQSNYG AANSTLEETM SVISNGFCFV
CPGILDSSLM LANGMDTEKH RLAHFIEWSI TTDEMVLWFD DAMTRYQGGQ KFSRYIPNLN
WEVMDRTHGM NKLGAHLVPT RTAKAPTTED DTGRVAEIVR STLNISSDDF SAEVPFTAYG
LDSLSASRLS FMLRPMMSVT QIQLLADMTL RDLQTRLSAE PVSEDFRALE PTTGKNEIQA
MRDMLSKYTQ DLREQRATTD IRATRNDVVL LTGSTGALGA NILAQLLDNS DVTKVFALNR
KGTDRHCLIE RQVAALVTQG LPPTLAESQK LVLIEGDLLL DGLGIPLEVF SEMLSSVTHV
IHNAWTIDFL SSLEAMEDLV RGTRRLLDIA ALSTRATPPS FSFISSIGIY QHYSGSAPAP
EEPVLDAKMA VQTGYMESKW VAERIVQIAG ARLGLKAHVI RVGLLTGGVN GSWDPTHWLP
ALVQSATYVG CLPESDSLVS WIPVDVAAAA VVDLRHASDD TLHVIHPRPM LWSDIMVPIA
SLLDVPLVPY IEWFCRLENM ANAISHAPSQ RDSRRLRHAL RLIDFYRLGM RGSKGVSGST
ESMGLLPQVK CQKAMRSSAT LQNPELCQLG ISDIERWVSY WRQAGHLPNN DSPN
//
