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Database: UniProt
Entry: A0A1Z3HL67_9CYAN
LinkDB: A0A1Z3HL67_9CYAN
Original site: A0A1Z3HL67_9CYAN 
ID   A0A1Z3HL67_9CYAN        Unreviewed;      1837 AA.
AC   A0A1Z3HL67;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:ASC71043.1};
GN   ORFNames=XM38_019920 {ECO:0000313|EMBL:ASC71043.1};
OS   Halomicronema hongdechloris C2206.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nodosilineales; Nodosilineaceae;
OC   Halomicronema.
OX   NCBI_TaxID=1641165 {ECO:0000313|EMBL:ASC71043.1, ECO:0000313|Proteomes:UP000191901};
RN   [1] {ECO:0000313|EMBL:ASC71043.1, ECO:0000313|Proteomes:UP000191901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2206 {ECO:0000313|EMBL:ASC71043.1,
RC   ECO:0000313|Proteomes:UP000191901};
RX   PubMed=26514405; DOI=10.1016/j.bbabio.2015.10.009;
RA   Li Y., Lin Y., Garvey C.J., Birch D., Corkery R.W., Loughlin P.C.,
RA   Scheer H., Willows R.D., Chen M.;
RT   "Characterization of red-shifted phycobilisomes isolated from the
RT   chlorophyll f-containing cyanobacterium Halomicronema hongdechloris.";
RL   Biochim. Biophys. Acta 1857:107-114(2016).
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DR   EMBL; CP021983; ASC71043.1; -; Genomic_DNA.
DR   KEGG; hhg:XM38_019920; -.
DR   OrthoDB; 499075at2; -.
DR   Proteomes; UP000191901; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   CDD; cd08953; KR_2_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
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   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR006342; FkbM_mtfrase.
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; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR01444; fkbM_fam; 1.
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; PF05050; Methyltransf_21; 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   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; 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   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191901};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..435
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1471..1546
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1837 AA;  204042 MW;  2C6E658A4D00980D CRC64;
     MGNIETYESV EGIAVIGMAG RFPGAKSIEE FWQNLCDGVE SISFFTDEEL IASGIGASVL
     NDPHYVKAGA VLDDIEFFDA SFFDINPREA EVTDPQHRIF LECAWEALEN AGYDTTRCRN
     RIGVYAGTGI NNYLPFDISR DPMGSAQCYQ TLIGNDKDFL TTRISYKLNL KGPSVTVQTA
     CSTSLVSTTL ACQSLLNYQC DVALVGGISI RVPQKIGHLY QEEGVLSADG HCRAFDAKAQ
     GTVLGNGVGT VVLKRLEDAI ADGDCIHAVI KGSAINNDGS GKVGYTAPSV EGQTEVIAEA
     LALAEIESET VSYIETHGTG TSLGDPIEIA ALTKVFRGST DKKGFCAIGS VKTNVGHLDT
     AAGVTSLIKT VLALKHKQIP PSLNFKEPNP EIDFANSPFY VNTQLSEWKV NETPRRAGVS
     SFGIGGTNAH LILEEAPSVE TSSSFRPWQL LLLSAKTSSA LETATTNLGD HLQQHSELNL
     ADVAYTLQVG RRQFDHRRAV VCQDLQDAIA ALQNPKRVLT SSIQDTGTRS VAFMFTGLGP
     QYVNMGRELY QCQPTFREHV EHCCKILRPL LGLDLITVLY PDQDESSDDT GADLAQSGID
     LRQMLGRSEE PVNAASQQLN QTWLTQPALF VIEYALAQLW QAWGVRPRAM IGYSIGEYVA
     ACLAGVLSLE DALMLVARRA QLIQSLPSGA MLAIPLSEQE VQPLLGENLS LSAINGSSLC
     VVAGATDAID ELENQLTQQG LACRRLATSH AFHSHMMASM VDSFSRLVKT IRFKPPQIPY
     ISNVTGTWIT AAEATNPDYW TQHLCQPVRF ADGVSQLWQK YTPALLEVGP GQTLSSLALQ
     CLENQQVTDK VVLPSLRYTY DRQSDVAFLL NTLGQLWLAG ILIDWSGFYI NERRHRLPLP
     TYPFERQRYW IEPQKPGNPV NSGASNSQQK LDITEWFHIP SWKRAAPPVP FESGKWGNRK
     QPWLVLVDRC GVGSQLVKQL EKECQDIIIV GIGEEFRKLN QQEYTINPGK RDDYDTLLCE
     LHFSNKIPKS IVHLWTITAN EQAEPGLESW EQIQSLSFYS LLFLAQALGE QGIDDPLHID
     IISNNLQELT DTDDICPEKA TLLGPCRVIP QEYSNITCRS IDITLPQSGT RQWQQLIDQL
     FSELAAPTAD KVIAYRGNRR WVQCFEPLPV AGKTLRTAKL RQGGVYLITG GLGGLGLAIA
     QHLAKTVQAK LVIIERSGLP PKTEWEQWLS NHEEDNPVSI KIKKVQAMEE FGAEVLVIKA
     DVTHLEQMQG MVDRVRDRFG EIHGIIQTTP PIGASIIQLK TTESAASILN FKVKGAMVLD
     AVLKDTQLDF LVLFSSINAI TGGLGQVDYS AGNAFLDAFA HYNFYRRNIH TVSINWDPGP
     GHNLQAAVSP EIQAGLRQMR ERYGIEFKKG IAALWHILSS QQPQVVVSTR NLQTLFEENE
     VLAAASLLEN LEKRHPQSTQ LRPNLKTAYV APRNETECKI AELYQELLGV DRIGIHDNFF
     DVGGNSLIGI QLLSRLRQEF QVELSLRFIF EAPSVAELAL IIEEILIREI EELTENEAEE
     LVSVLPQSSE QTPRVVSQRR YKLPNHLEIA YQTKTEADYF YQDIFENKVY LKHGIALNEG
     DCIFDVGANI GLFTLFAYQH CKNPIIYAFE PAPPLFEILS FNTALHEVNV KLFNVGLSNE
     TKTATFTFYP QSSGMSSFYG DRGEEQEVLK AIMLNQLQTG MAGMEQVMQY SDELLEERFK
     SQSFTCQLKT LSDVISENNI ENIDLLKIDV QKSELDVLQG IKDKDWKKIK QIVLEIHDTE
     GRLVQITNLL KTQKYNVVAE QEDLYENSNI YNVYAAR
//
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