ID A0A1Z4V7G4_9CYAN Unreviewed; 1760 AA.
AC A0A1Z4V7G4;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Polyketide-type polyunsaturated fatty acid synthase PfaA {ECO:0000313|EMBL:BAZ87472.1};
GN ORFNames=NIES806_36950 {ECO:0000313|EMBL:BAZ87472.1};
OS Dolichospermum compactum NIES-806.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Dolichospermum; Dolichospermum compactum.
OX NCBI_TaxID=1973481 {ECO:0000313|EMBL:BAZ87472.1, ECO:0000313|Proteomes:UP000218702};
RN [1] {ECO:0000313|EMBL:BAZ87472.1, ECO:0000313|Proteomes:UP000218702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-806 {ECO:0000313|EMBL:BAZ87472.1,
RC ECO:0000313|Proteomes:UP000218702};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AP018316; BAZ87472.1; -; Genomic_DNA.
DR OrthoDB; 499075at2; -.
DR Proteomes; UP000218702; Chromosome.
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 CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 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; 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; IPR004432; Omega_3_polyunsat_FA_synth.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR02813; omega_3_PfaA; 1.
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; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 61..519
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1290..1374
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1400..1480
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1072..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 8..35
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1760 AA; 193122 MW; B143ADCF0D26E0A8 CRC64;
MSCPPQKIDT IKSSLTELEA QINSFEQAVL KFIEEGKMNS GNLENSINSM STKEINRKLH
TTPIAIIGMA SLMPQSRTLR DYWQNIVNKI DCITDVPSSH WSVEDYYDPN PRTAEDKTYC
KRGGFIPEVD FNPMEFGIPP SILEVTDVSQ LLSLVVAKET MEDAGYGDSR EFSRENIGVI
LGVAMGKQLG MPLAARLEYP IWEKVLKSTG LSDEDTKKIV DKIKSAYVKW DENAFPGMLA
NVVAGRIANR LDFGGTNCVV DAACASSFGA LKMAISELVE HRSNMMLTGG VDTDNTIMAY
ISFSKTPAVT PSDNVKPFDA KSDGMMLGEG IGMILLKRLE DAQKDGDKIY AVIKGIGTSS
DGRYKSIYAP RKEGQVKALE RAYDDAGFSP ATVGLMEAHG TGTMAGDPIE FSSLQDFFGK
YDTQKQHIAL GSVKSQIGHT KAAAGTASLI KTALALHHKV LPATINITEP NPKLDIENSS
FYLNTQTRPW IKVEGETPRR AGVSAFGFGG TNYHVVLEEY EPEQQSSYRL HGAAGEVLLF
GATHAELISK LEATLNNLQA DDGERFYSQL VLDCQSLTIP KTAVRIGFVS ENLQEACKLL
EVGIGLLKSK PDAIYWEHPQ GIYYRSAGMD LGGKVVALFS GQGSQYLEMG REAVMNFPSL
RQLYGKMDHL FKQGNLQPVS EVVFPRSSFD EVEKKAQVAT LQRTEYAQPA IGVFSAGLYG
ILQQAGFKAD FTAGHSFGEL TALWAAGVLS EADYLFLVKA RGQAMAAPKD PDHDAGSMLA
VKEDISKIEP LLKQFPKVSI ANFNSPTQIV LAGPKLEIEK IQAACQKLGY SAVLLPVSAA
FHTPLIAFAQ KSFAIATKSV TFKNPQIPVF SNVTGKQYPQ NAAAIQKNLE SHLASSVLFK
QEIENIYAAG GYCFVEFGPK RVLSNLVKDI LGDRPHLTIS LNPSASKNSD RSLREAAVQL
RVIGMNIANL DPYKRLAVLP PISTKKTLSV KLTGINYISD KTKNAFTEAL QDGHKISGVQ
EFKSLEVQEF KNLEIETPVI AKISPTNGHN GNGNGNGHKK QPLIETQLQP QMTTTATIQK
QSSPELFAPQ SSEKMQTPDK LINCQQILTS LEQLLSQFQH NQSENLEVHS TYLNHQIEYA
KTFFQLMQQQ NTLFANAKSS AEAAQIKQVI MESLERSMIQ FHSQQGETLR IHEQYLREQI
EYTKHFFQLI QEEYSQLISD TQEIAPVNVS VTPEEAPVPP TATIIPPQPL PVIEPKVQIA
EPVIAAPVIE PEPIIIPQSP VAFIPEPTPV TSNLNLDDLA NNLLSITSEK TGYPIEMLEL
DMDMEADLGI DSIKRVEILG GLQELYPNLP KPNLEELAEK RTIGQVVEYL QGQGTGDRLQ
VTSDSVEVIG NRLQVTGDSN EYADLGQTLL NITSEKTGYP VEMLELDMDM EADLGIDSIK
RVEILGAMQE AYPDLPKPNI EELGDLRTIG QIVNYLQSLV GGEKKKPHID VNLVTTTSVG
AQVLRPLLDS LTPLPIVDPN LPRRPAQLKT LPRPDFLEAQ LPEGHIGLIT DDGSLTTSKV
VHALIEQGWK VVVLSFPQSL VASQLPLPAG VTRVTLANMS EQHLQLLLQS VTTKHGAIGA
FIHLHPQFTP EKPGHISYPE AEKAILKQVF LMAKHLKATL NNAASLPGRT SFCTVAHLDG
EFALGHQTNF SAIAAGLFGL TKSLRWEWPQ VFFRAIDLNP SLDPYESAQY IVAELHDSNR
YIGEVGYGNQ GRVTLVAKAE
//
