ID A0A2K8SKI1_9NOSO Unreviewed; 1590 AA.
AC A0A2K8SKI1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Non-ribosomal peptide synthetase component F {ECO:0000313|EMBL:AUB35345.1};
GN ORFNames=COO91_01223 {ECO:0000313|EMBL:AUB35345.1};
OS Nostoc flagelliforme CCNUN1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=2038116 {ECO:0000313|EMBL:AUB35345.1, ECO:0000313|Proteomes:UP000232003};
RN [1] {ECO:0000313|EMBL:AUB35345.1, ECO:0000313|Proteomes:UP000232003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCNUN1 {ECO:0000313|EMBL:AUB35345.1,
RC ECO:0000313|Proteomes:UP000232003};
RA Shang J.;
RT "Complete genome of a free-living desiccation-tolerant cyanobacterium and
RT its photosynthetic adaptation to extreme terrestrial habitat.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP024785; AUB35345.1; -; Genomic_DNA.
DR KEGG; nfl:COO91_01223; -.
DR OrthoDB; 499075at2; -.
DR Proteomes; UP000232003; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd08955; KR_2_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; 3.40.50.720; 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; IPR049490; C883_1060-like_KR_N.
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; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
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; PF21394; Beta-ketacyl_N; 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; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 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; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000232003};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..424
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1457..1534
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1590 AA; 173695 MW; EA863947625B9014 CRC64;
MEAIAIVGIG CRFPKAKNPE SFWHLLRDGV DAIAQVPPER WDINAFYESK PATPGKMNSR
SGGFLDQVDL FDPNFFGISA REAEHLDPQQ RLVLEVAWEA LENTGLVPKT LADSQTGVFI
GVTNADYHKL IYKDSSQIGA YSATGTTPCI AANRLSYLLN LRGPSIAIDT ACSSSLVAIH
LACQSLRNGE SNLCLAGGVN LMLAPEPAIS CSQAQMMAPD GRCKTFDASA DGYSRGEGCG
VVVLKRLEDA LRDGDNILAL IRGSAVNQDG TSNGLTAPNG PSQQAVIRQA LEQAGVAPAQ
ISYVEAHGTG TSLGDPIEVK SLKAVLMEGR SPEQPCWIGS VKTNIGHLEG AAGMAGLIKV
VLQMQQREIA PHLHLKQLNP YISLEGTPFA IPVELQPWSS PGSRLAGVSA FSFGGTNCHI
ILEEAPLPTP VASEVERPQH ILTLSAKTAP ALAELAQEYQ DFFASHPEVS LADVCFSGNT
GRSHFEHRLA VVGESAVQMC QQLSAFGAGE DTAGLKSEQL KKKKLPKLAF LFTGQGSQYV
GMGRQLYNTQ PIFREAIDKC AQILHPYLKQ PLFEILYPEA GKSSPLDETA YTQPALFALE
YALFQLWESW GIKPDAVMGH SVGEYAAACI AGIFSLEDGL KLIAERARLM QALPQDGEMV
AVIASEALVT SIIEPYVQVA IAAINGPKNI VISGDRHVIE TVTNILRTQG ITTKKLQVSH
AFHSPLMEPM LGEFEQVAKN ITYSSPKISL ISNLTGQPIT DEMATPEYWC NHVRQPVRFA
DSMESLYQRG YKIFVEIGPK PILMGMGRYC LPEGEGTWLP SLRTGRDDWK QILDSLAALY
ISGAIVDWNG FDRDYARRQV VLPNYPFQRQ RYWFEQAKNG NSKTESLSQD RIQTQIFNLL
HQGETQELAK YLQTATQFSQ EEIKVLPKLL DILAKQHQQQ LTAASYKDWL YEVSWQPKPR
QLTQISAQEP GSWLILADKR GVGQALAHLL QEQGESCFLV YPGEGYEVKQ PGTWSVNPSN
PADFERLFQE VVGTNKLPLK GVVHLWSLEA GLTSELTVPL IEKIQVLGCA STLHLVQALA
SRLASPRLWL VTRGAVPAVS SLQAPAQASL WGLGKVIALE HPKLWGGLLD LAADAPTDEA
VNLLAEIWDS QGENQIAFRE GRRYVARLIR SEVPEARSIS LQSDSTYLVT GGLGALGLKV
AQWMVEQGAR HLMLTGRKQA SAEVLQAIAQ MENLGAKVAI AQADVAHWSD MVRVFEEIKT
SMPPLGGIIH AAGMLHDGIL RQQEWKSFEQ VMAAKVKGTW ILHTLSQQLQ LDFFVTFSSA
AALLGSPGQG NYAAANAFMD ALTDYRRASG LPGLSINWGL WKDAGMATSL GNRDQARLAA
QGMESIPLEQ GLQILGNLLG QDRSQVGVLP VNWSKFCEQF PEGVVSPFLE SFIARDKKPS
LQRTQLLQQL EASPVNERQT LLIAHIQTEL VKLLGIDASE LEPQQGFLDL GMDSLMAVEL
KNRLESTLSC SLPSTLVFDY PTIEALVDYL LKDAIPSVSF ANASLISDES AVESQETNHE
EQVVTDSYLD DLSDSEAEEL LLGKLNSMRY
//