ID E5R2A6_ARTGP Unreviewed; 2503 AA.
AC E5R2A6;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Fatty acid synthase S-acetyltransferase {ECO:0000313|EMBL:EFQ96996.1};
GN ORFNames=MGYG_00039 {ECO:0000313|EMBL:EFQ96996.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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DR EMBL; DS989822; EFQ96996.1; -; Genomic_DNA.
DR RefSeq; XP_003175948.1; XM_003175900.1.
DR STRING; 535722.E5R2A6; -.
DR GeneID; 10031243; -.
DR VEuPathDB; FungiDB:MGYG_00039; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_1_1; -.
DR InParanoid; E5R2A6; -.
DR OMA; EDVGWIS; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR011032; GroES-like_sf.
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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF28; SYNTHASE, PUTATIVE-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; PF13489; Methyltransf_23; 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; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFQ96996.1}.
FT DOMAIN 58..478
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2416..2493
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2503 AA; 273753 MW; 2737A0E5E84022D0 CRC64;
MTINDNSNID GQNVTMGLKL NGASTNGHST NGMHAEGIST DTNGLNGISA DAVHYNGQIP
IAICGMACRL PGGLTTPEEL WDFLLAKKDG RCRVPESRYN INSYYSDAKQ PGTVSTECGY
FLDESVDVGA LDMSFFTMTR TEVERADPQQ RLMLEVAREA FEDAGVTNWR GKTIGTYIGN
FGEDWLEMLG KETQPWGIHR ISGSGDFVVA NRLSYEFDLQ GPSMTIRTAC SSALVALNEA
CAAISRGDCE SALVGGVNLI LAPGMSMAMQ EQGVLSKDGS CKTFSANANG YARGEAVTAV
FVKPLAHALR DGNPIRAIVR ATSHNADGKT PTLSQPSTDA QEALIRRAYE LGGINNYAET
AMVECHGTGT PTGDPIEAGA VARVFGEKGV YIGSVKPNLG HTEAASGLVS LLKMVKALEH
RVIPPNIKFT SPNPNIPFVD CKLTVPTEPT PWPEDRLERV SVNSFGIGGA NAHVILESAA
TYHIPTPVYE TPETPQLLLF TANSLKSITR LVDNYKAWIE ENPDKVSDLA YTLARRREHL
PHRVFAIVSN GGVESVSQPT KSKSAKPPGV VMVFTGQGAQ WPQMGRELLR SNEVFKSSIR
SLDEYLQTID GEKPQYTIEE ELKRPGKKSK LSLAEISQPL CTAIQIALVD TLKSAGVVPD
AVVGHSSGEI AAAYASGALT AREAITAAHH RGAVTNRQKR AGTMAAIGMS WEETEKYLAP
NVTIACDNSP KSVTISGDVD AVKSVIATIK EEQPQILARL LQVDKAYHSY HMKEIGEDYQ
LLIGEEVVGR APSVLFFSSV TGNLLSTEQK IDSKYWQDNL ESPVRFKEAV TAILKHEVGK
NSVFLEVGPH GALAGPLRQI FTQASSSAPY ISTMARNQDC TASFLAAIGA LHSLSVSIDL
ESLFPTGSCL PDLPRYPWNH EGSYWYETRL SKEWRNRKYP YHDLLGARVA ESSDSEPVWR
NLFHVTNTPW IRDHKVGENI VFPFCGYIAL AGEAARQLTN IEEGFSVRNI IVSTALVLSE
GKPTEILASF RPHRLTNSLN SAWWEFTVTA YNGRNWTKHC TGEVSAFSST LGQAQNPNPL
PRKLNVRKWY EKMSKGGLDL GGSFQTLDTI TTSTSDQQAV GNIVNGRQGD EANYHIHPTA
LDGTLQILGA AAVNGYARKT KTWLPTSIDK VSVRRCASDL VTSVSARLSS NFSVVGEGRC
TSGGMTVVEA SGIRMSLADG AGASDVPDTH AASRCEWRPD IDFLDVNELI HAPHGRTNHL
RLLEELGDIC LLLSQRSFSE SPRQPILPHL SKYVAWVQSQ STSIVTRLPW TWTGLDNEAI
SARVEGIISR LSGTPAAPVA SMIHQVCTNM DSFLSGENFG NDFPGGKLIP IYDFIGQVDR
KEFIRHLSHS KPNLRILEIG TGKGVSLHRH ILDELTRPDG EILCSKYTLT NPGYVVETTQ
EKLFPNMEFA SLDINKDPFD QGFEEVGYDL IIAVNALHET ENIIASLANI KKLLRPDGRL
FLQELCPSSN WVNYVLGLLP TWWSNAADKP AEALILGKEG WQSKLKAAEF GNIEAVTLDA
EEPHQVTVTM VVRQPCAMPT KKITALVEGE GPAVIRILDQ LNNQGYQVTR CKLNDIPPAG
QDVISLLDAE TPFFHGIDEA HFLSFKAFLL CLQDRDAGML WVTHLIDIGC NDPRYAQILG
LSRTIRTEQL ADLAICQVDS FESNTSINQL LQVLAKFQAR KGDEELNPDF EWAIFNERVQ
VARFHPFVLA DELLVAEGAN EKATLNVRTP GRVNSLHYER HARKELESDE VEVQVYTAGL
NFRDILVALG IVELPIRLFG IEAAGIVTRV GVDVSPNDLQ IGDRVVCFCR KDAFSTYTTT
LAAVCVRIPD SLSFNQAGTM LIPYFTAIHS IVNVGRVSKG QSVLIHSACG GVGLAAIQVA
QMLEAEVYAT VGSETKVKYL MENYHIPRNR IFNSRDKTFV DGVMRETEGR GMDFILNSLS
GDLLHATWSC VAEFGTLLEI GKRDLIGDGR LDMKPFLANR SYCCVDIDGL WKKIHVARAL
IFSILEFYNK GHISPLPTTI FPASQTQDAF RFMEKGQHIG RVGVSIKQTE EAVLGFETTK
RSLTIAFNEA SSYLMVGGLG GIGRAVSTWM VDHGVRELIY LSRSAGRTAK DDVFVHELRT
MGCAVKLVSG DTTKLEDVQR AIAAATYPMK GIVQMSMVVA NENFTKMSFG EWMASTAPKV
QGTWNLHNAS LAAGIDLDFF LMFSSVSGIV GQAGQANYAS GNSFLDAFAQ YRNGLGLAAS
VVDMGAVEDV GWISEHQGMM GKMSRSGFKP VLEQEVIDAM AICMLVHSKP GQAAERALAV
ASKNDSCFVH KNTFLVGLAL LIPLHDPSNY VIWKRDRRMA SYHNNSTISA AAASTDTLKS
YLNSAQADPS ILKSSEAARL FAVEIGKKLF DLLLKPQDEL NTSWPLLDLG LDSLVALELR
AWIKQVFSFD LPMLEMMSIG SLDILGQYAA NEVYRIVTDN NES
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