ID   Q7NJ73_GLOVI            Unreviewed;      1296 AA.
AC   Q7NJ73;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   24-JAN-2024, entry version 121.
DE   SubName: Full=Gll1959 protein {ECO:0000313|EMBL:BAC89900.1};
GN   OrderedLocusNames=gll1959 {ECO:0000313|EMBL:BAC89900.1};
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC89900.1, ECO:0000313|Proteomes:UP000000557};
RN   [1] {ECO:0000313|EMBL:BAC89900.1, ECO:0000313|Proteomes:UP000000557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421 {ECO:0000313|Proteomes:UP000000557};
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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DR   EMBL; BA000045; BAC89900.1; -; Genomic_DNA.
DR   RefSeq; NP_924905.1; NC_005125.1.
DR   RefSeq; WP_011141957.1; NC_005125.1.
DR   STRING; 251221.gene:10759451; -.
DR   EnsemblBacteria; BAC89900; BAC89900; BAC89900.
DR   KEGG; gvi:gll1959; -.
DR   PATRIC; fig|251221.4.peg.1993; -.
DR   eggNOG; COG0236; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000022_30_4_3; -.
DR   InParanoid; Q7NJ73; -.
DR   OrthoDB; 499075at2; -.
DR   PhylomeDB; Q7NJ73; -.
DR   Proteomes; UP000000557; 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; 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   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; 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; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000557};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          18..474
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1198..1278
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          963..1008
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        968..985
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1296 AA;  139069 MW;  7B2619CF9DD6F525 CRC64;
     MAEEQRTESE QQRDALQRVP VAVIGMASIF PKAGNLQEYW ENILNKRDCI DEVPSTRWRV
     EDYYDPDPSA ADKTYCKRGG FIPDVPFDPL EFGLPPSILE VTDITQLLGL VVAKAALADA
     GYAGAAQAVR ERTGVILGVV GGTMQLLVPL TTRLQSPTWH RVLTSSGLSD EEACEIERKL
     KLAYVGWEEN AFPGWLGNVI AGRIANRLDL GGVNCVVDAA CASSLGAMKM AISELTEYRS
     DLMITGGLDL DNSIFMFMSF SKTPALSKTQ TIRPFGAGAD GTLLGEGLGM LVLKRLEDAE
     LDGDRIYSVI RGIGASSDGK HKSIYAPNWQ GQVQAMRNAY RAAGIAPAGV GLVEAHGTGT
     AAGDLSEFTA LRTVFGEGPA ARPRIALGSV KSQIGHTKGA AGAAGVIKAV LALHHKILPP
     TLHVERPNPE LNIEDSPFYL NTESRPWSRG QQPRRAGVSA FGFGGTNYHL VLEEYEAEHL
     RPYQLHRTGR VLLACAETPT HLLEQCRALL EELGGQSGER VFAQWIEATA ALVIPGDAAR
     LGFVAASREE TCALLAQAIE TLAGADPEDP WEHPAGIYYR RCGLAAGAKV VALFPGQGAQ
     YLNMGRSLAN NFPQVRQIFA DFDGLFSLEG ARTLSQTVYP EPGFGEEHSA LHSAALQATE
     YAQPAIGALS LSLFALLHEA GLRVDFAVGH SFGELSALWA AGVLNAPDYL ALVRARGRAM
     TPPIEPPHQA GAMLAVKHPA AVLQSWLPQL EGVSVANFNS PNQLVLAGGR AAILAAQQTL
     EARQIRTALL PVEAAFHTPA VDYALGPFAE AIGSVELKPP TVAVYANATA EPYPDDAEGI
     ASLLRQQIVN PVLFEPSIER IYAEGGACFV EFGPRGILTG LVKDILGQRP HVAVALNPST
     RGDSDRQLRT AAVQLRVVGL PLKDLSGYQR PYPAAGDGKR ALTIALNGRG YLSEKTRAAF
     EQALQSKPPT RAAPTNANRN GQRPVHSPNG APPAQVVQGP GRTNGHAALP PSDVVQFHPK
     VHSMSQHPTT TSVHARFFDS LDQTLSQLGK QQGETLRVHQ QYLNHQAEYT MVSLQLLQQQ
     HTLFGGRSGM GPMLEEVAGP LLKSLERSLL HLHQHEEGTL HLHEHYLKHQ VAYSQACVQL
     LKQQWALLAP PQSGEGVPAA AAFWAPPAVE PAVVPQPVLT PSAPPPEPPV QTSANGSSVR
     ATVQQVLLQV VSEKTGYPAE MLTMEMEMEA DLGIDSIKRI EILAAMQEAL SRLPEVEPED
     LAELRTLEQI GAHWVAVAEG AAKKKSPAVL PTRLVS
//