ID A0A1Y0RIH9_9CYAN Unreviewed; 1062 AA.
AC A0A1Y0RIH9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Type I polyketide synthase {ECO:0000313|EMBL:ARV59086.1};
GN ORFNames=BZZ01_10955 {ECO:0000313|EMBL:ARV59086.1};
OS Nostocales cyanobacterium HT-58-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales.
OX NCBI_TaxID=1940762 {ECO:0000313|EMBL:ARV59086.1, ECO:0000313|Proteomes:UP000196302};
RN [1] {ECO:0000313|EMBL:ARV59086.1, ECO:0000313|Proteomes:UP000196302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT-58-2 {ECO:0000313|EMBL:ARV59086.1,
RC ECO:0000313|Proteomes:UP000196302};
RA Hughes R.-A., Zhang Y., Zhang R., Williams P.G., Lindsey J.S., Miller E.S.;
RT "Genome sequences and microbial community composition of HT-58-2, a
RT tolyporphin-producing cyanobacterium-microbial holobiont.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP019636; ARV59086.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0RIH9; -.
DR KEGG; ncn:BZZ01_10955; -.
DR OrthoDB; 499075at2; -.
DR Proteomes; UP000196302; 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; 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 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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 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; 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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000196302};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..459
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 975..1053
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1062 AA; 117034 MW; CBBFEAC0382C567D CRC64;
MSDNNEQRYV QLMKVASQKI ASLQAEIEQL KQKEHEPIAI IGMGCRLGHA DNPEQYWDIL
SNGVDAIREA PEGHHSYLDP YYDPEPGLPG KVYIRRAAFL NQSPADFDAS FFGISPREAA
SLDPQHRLVM EVAWEALEGA GLVPENLAGS QTGVFIGICA NDYVWQLVKQ DPTETDVYIG
SGNAYSPVAG RLSYFFDFTG PCLAVDTGCA SSLAAIHLAV TNLRRGDCNL ALAGGVQRYV
SPEYWLNLCK SRMLSPDGRC KTFAAGADGY ARGEGCGIVV LKRLSDAQAD GDNILALIRG
SAHGQDGRTS GLTVPSGSSQ QGVIRRALAN AGIKPKEVNY IEAHGTGTSL GDPIEANALI
NVFRQREEPL ILGSAKTNIG HLEGAAGVAG LIKIVLSLQN ELIPPHLHFK EPSPYIAWDR
MPIKVPTEAI PWPATDKTRF AGVSSFGFTG INVHVVLSEA PAVTPKTEPE TWKRPLHLLT
LSAKTKPALE QMVHNYSQHL ATHPNLEWAD VCYTTNTRRT HFQERLAILA DSVSVAQEKL
LAYQAGAEDN HVFSGSKSES QPQIAFVFTG QGSQYLGMGR ELYATQPTFR QALDRCQEIL
HEIGNQEHSL LSVLYQNDDI SLLEQTAYTQ PTLFALEYAL AQMWKSWGIE PTAVMGHSVG
EYVAATVAGI FSLEDGLKLI AARGRLMQKL SGNGEMVSLL ASAAQVAEAI KDNDLVSIAA
INGPESTVIS GEREAVRTVV AELEQKGIKT KRLKVSHAFH SALMQPMVAE FRQVVKQVTF
HQPKLNFISN VTGAQERVLP TNPEYWVEHV LKPVRFASGM EALHRQGVEI FVEMGPAPIL
LGMGRQCLPS DYGTWLPTLH PEQSDWQGLL QALGQLYVRG VAVDWAAFHR DYAHRQVDVP
TYPWQRERYW IEVAQTQPLR ESETQAENRD FVATFEELQA KHASYKPLPQ QPEKKDKEKT
SLNLVEQLKA SEKEQRKELL ITHIQSLLSG VLGDKQERTF SLSQGFFDLG MDSMTSIELR
NRLQNSIGVS LSSTLFYKYP TVEALVGYLS QDVLATVVSF DD
//
