ID A0A1H5KP32_9ACTN Unreviewed; 2284 AA.
AC A0A1H5KP32;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Polyketide-type polyunsaturated fatty acid synthase PfaA {ECO:0000313|EMBL:SEE66639.1};
GN ORFNames=SAMN05216489_07689 {ECO:0000313|EMBL:SEE66639.1};
OS Streptomyces sp. 3213.3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855348 {ECO:0000313|EMBL:SEE66639.1, ECO:0000313|Proteomes:UP000198754};
RN [1] {ECO:0000313|EMBL:SEE66639.1, ECO:0000313|Proteomes:UP000198754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3213 {ECO:0000313|EMBL:SEE66639.1,
RC ECO:0000313|Proteomes:UP000198754};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNTK01000001; SEE66639.1; -; Genomic_DNA.
DR STRING; 1855348.SAMN05216489_07689; -.
DR Proteomes; UP000198754; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 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; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
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; IPR004136; NMO.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43074; OMEGA-3 POLYUNSATURATED FATTY ACID SYNTHASE PFAB-RELATED; 1.
DR PANTHER; PTHR43074:SF1; PKS_AT DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF03060; NMO; 2.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 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; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 2.
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; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Reference proteome {ECO:0000313|Proteomes:UP000198754};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 672..1113
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1692..1771
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2284 AA; 237932 MW; 5DEAB577D91D2C60 CRC64;
MTSVARAAEM IIGITPFHEP DARLAAAVSR AGGLGVLDLG IGDRRSREAL ARIRRWAPGP
FGVRVGAHCR IDPAELATTA DGGPHTVVLT VDTAWRVEEV ADAYRVLVEV TDPDQALTAV
RSGAHGLIAR GAESGGRIGE LSTFVLLQRL LAEPGVTVPV WACGGIGPRT AAAAVAGGAA
GVVLDSQLAL LAESALPETA AAALRSMDGS ETTVIAGHRV LLRRGPDAPQ VPAERVSELL
GARDPRTQLL PVGQDGFLAA RFAERWGDVG RTVRELTAAV RESIRDEGPA GALRAGSPMS
RRIGTQLPLA QGPMTRVSDQ AEFAAAVAGG GALPFVALAL ASGEQSRTVL AETRAALGDR
PWGVGVLGFA PEEMRNAQLE AVRELRPTHA IVAGGRPSQA EALERSGIAT FLHVPSPGLL
RQFLDAGVRR FVFEGSECGG HVGPRGSFPL WEAQLAVLDD FLETAAAGTA EHVEVFFAGG
VHDERSAAMV AALAAPLTAR GAAVGVLMGT AYLFTEEAVT RGAVQPLFQE QVVRATRTAL
LETAPGHATR CVPSPFSDNY LLFEAELREQ GVPDRQIWEK LERLNVGRLR IASKGVERDA
AGALTSVDEE RQLAEGMFMA GEVAVLRSAT TTIDALHRSV TEGAADFLAD SARTARVLLG
VEEQAEPEPP APLDIAVIGM ACMFPEAPDL PTFWANILGG RDAVTEVPAD RWDPAVHYAD
DKSGATPSKW GGFLPRIPFD PLRYGIPPTS LGSIEPVQLL ALEAARRSLE DAGYGDRGRH
FDRARTSVVF GAEAGSDLSN ATTLRAVLPS YYGRIPQGIE EQLPTLTEDS FPGMLSNVIS
GRIANRLDLG GANFTVDAAC ASSLAAVDVA CKELVGGTSD IVLCGGADLH NGINDYVLFS
SVHALSPTGR SRAFDNSADG IALGEGVACV VLKRLADAER DGDRIYGVIK GVGSSSDGRS
LGLTAPRPEG QRAALERAYR NAGVSPASVG LVEAHGTGTV VGDRTELSIL SEVFTESGAE
TGSCALGSVK SQIGHTKCAA GLAGLIKTVL SLYTGVKPPT LHMKQPNSAW KEDDSPFVFH
ARPRPWAAPA EERVAGLSAF GFGGTNFHTV IQAYGDAVPP AHGLDAWPAE LFIFRGADRA
AARRGIEETL KLAESGSWRL RDLALGASRR SDARHEPVQV AVVATGVEEL AGQLRRALAG
EHDPGAGIHA ADLQEDAGKV AFLFPGQGSQ RPGMLADVFI AFPELQHYLH LGRDHADTLY
PPTAFDDTAR DRQQAGLTDT RVAQPTLGIA GLAAHALLTE AGVRPDMAAG HSYGELVALC
AAGAIAPEAL LELSAERAAA ILEATGADDP GTMAAVAAGA EDVEQALKTA GAPDSVVLAN
HNSPRQTVIS GPTAAVAEAV RLLREAGLGA KRIPVACAFH SPLVAGAGER FARALAQQAV
LTPEFPVWSN RTAAPYGEGA DAVRAELAAQ IGAPVGFVAQ IEAMYEAGAR VFVEAGPGSV
LTRLVAQILG ERPHRTVACE PRPDSGLRGW LDALAQLAVA GLPVRTGWLF NGRDAVDAAR
TPVPKRPGWT VDGQLVRTAA GELLPGALAP ARRVVETTVT TNPQGGAPVE ANRDALISEF
LRTSREMVAA QRDVLLTYFG ATQATVPQGT WVPAPAPAAV EALPQLPALP AAAEAPVAQQ
STAQPESVPE AVTEDDVLRV VLEIISERTG YPVDMIEPDL DLEADLSIDS IKRAEIAGEL
AQRLGIGGGA DIASLDDAEL EDLAKARTAA SVTGWLSARL TEPAAPAADT SPQDEVTGSA
PKRLQLRPVL LPHQDSDNPA DPASVLSGRR FVLYGAGDVP EAVAARLSSY GADTVIVAPE
HQLTDADGQV DGVLYLAPLT ASAPVLPDAF PVFQAVLRRA PRQLIAVQGA ESGSAGLHGL
FRTVAREYPD TVARIVEVAD PASAAIADAV LAELLAPGDE PVVLRTAVGR HGLELTETPL
GALATNGAGP AGDGVAEAAA IGLDRDAVVL LVGGARGITA KFAVALAAAS RCRIELLGRT
TAPAGPEDPA TAGARTPAEL RAALAGQGGR TPAEINRTAE LLLAQREITA TLDELAALGS
EARYHSVDFR EPDAALQAVK EIHAEHGRLD GVVYAAGVIE DRLIAEKTTE SFQRVYGTKT
HGAETLLSAL EELPNGPAFA VLFGSISAVL GNRGQVDYAA ANDALESLGT AWSARTGHRA
LTVHWGPWAP TGGHHGMVTP ELGREYARRG ISLIDPEEGT AALLRELAFG DESAGAVVYT
ASGW
//