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
//