ID B2J540_NOSP7 Unreviewed; 2016 AA.
AC B2J540;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ACC80700.1};
DE EC=2.3.1.94 {ECO:0000313|EMBL:ACC80700.1};
GN OrderedLocusNames=Npun_R2081 {ECO:0000313|EMBL:ACC80700.1};
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737 {ECO:0000313|EMBL:ACC80700.1, ECO:0000313|Proteomes:UP000001191};
RN [1] {ECO:0000313|Proteomes:UP000001191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACC80700.1, ECO:0000313|Proteomes:UP000001191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191};
RX PubMed=23463784; DOI=10.1104/pp.112.213116;
RA Ekman M., Picossi S., Campbell E.L., Meeks J.C., Flores E.;
RT "A Nostoc punctiforme Sugar Transporter Necessary to Establish a
RT Cyanobacterium-Plant Symbiosis.";
RL Plant Physiol. 161:1984-1992(2013).
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DR EMBL; CP001037; ACC80700.1; -; Genomic_DNA.
DR RefSeq; WP_012408705.1; NC_010628.1.
DR STRING; 63737.Npun_R2081; -.
DR EnsemblBacteria; ACC80700; ACC80700; Npun_R2081.
DR KEGG; npu:Npun_R2081; -.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG2226; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_0_3; -.
DR OrthoDB; 499075at2; -.
DR PhylomeDB; B2J540; -.
DR Proteomes; UP000001191; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR013217; Methyltransf_12.
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; IPR029063; SAM-dependent_MTases_sf.
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; PF18558; HTH_51; 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; PF08242; Methyltransf_12; 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; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:ACC80700.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACC80700.1}.
FT DOMAIN 32..459
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1888..1963
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2016 AA; 220650 MW; B354DEC351D3CF64 CRC64;
MNSFSKRISE MSPVKLAFAA QQLESKLELL KAEPIAIVGL GCRFPGGVDS PEAYWELLRN
GVDAITEVPK ERWDVDAYYD PDPSKPGKIN TRNGGFLAEV DGFDPHFFNI SPREAISLDP
QQRLLLEVTW EAMENANQTP QNLFNSPTGV FIGISADDYS QRLLDAEGRE GIDAYFGTGK
AFSAAAGRLS YFLGLTGPSF AVETACSSSL VSVHLACQSL RQRECNLALA GGVNLILSPE
ASLTFSKARM LADDGHCKTF DAAANGYARG EGCGIIVLKR LSDAITDQDR ILAVIRGSAV
NQDGPSGGLT VPNGPSQEAV IQRALATAGV EPAQVSYVEA HGTGTFLGDP IEVGALGAVF
GKNHSPSNPL NIGSVKTNFG HLEAAAGIAG LIKVVLQLQH QEIAPHLHFQ QPNPHINWEA
LPITVPTQST PWIVPGDRRI AGVSAFSFSG TNAHVVLEES PTSGTSSVTN PEQPFNLLTL
SAKTPEVMQK LASRYHLYFK AHPELSLADV CFSANTGRSH FPYRFSLVAN SSSQLCDQLA
ALAAGETNVT GIWQGQQPAT KSKIAFLFAG QGSQQAGMGQ ELYATQPTFK AALDECAEIL
RPYLDVPLLE LLWGNSSHLL DQTAYTQPAL FAVEYALYQL WQSWGIQPDA VLGHSVGEYI
AACVAGVFSL ADGLKLIASR AKLMQALPSG GAMAAVLVDK SKLVQALAPY AKQVAIAAHN
GPRSFTISGA VEPLEAVCKA LSANGGKIKR LSVSHAFHST LMEPMLAEFE AVARQVKYQQ
PRIPVIANLT GQVAGGQIAT PQYWVRHVRE AVQFEMSIQT LHQDGYELFV ELSAKPTLLS
MARQCLPEST GVWLPSLRPG QSDWQSLLSS LGQLYVSGAT VEWSSNRPSH KVALPTYPWE
RQRYWIETPQ KQAQLARSQS TASTSIVRLI DQGNTQELLQ QLATTSNYSP EQQELLLEML
TQLVKQHHQQ VTAESIQDWL YELNWRSQAR FGKELYPNYL PTPEQISSDL NPQIAELLPE
LNSYRQEVLS PLEAISIDYV VKAFQDLGWN FQIGSRFSTE SLAQQLGVIS QHRRLWQRLV
EMLAEVGIVQ RLGTQWEVTQ VPQKGDPQAQ IEHLHHQYPA AQAELTLLGN CGPNLAEILQ
GKCDPLQLIF PDGDATIATQ FYQESPGARV MNILVRQAVS SALQQLPVGR GLRVLEIGAG
TGGTTAHLLP LLSQEQTEYV FTDVSPVFLG QAQQKFPDYP CLRYQTLDIE KDPISQGFPA
EQYDIIVASN VLHATKDLRV TMQHARQLLA PGGILVLMEV TARQRWLDLI FGLLDGWWRF
EDVDLRPDYA LLTTVQWQKL LKEVGFSTTT ALPSITQNSG VLPEQAVMVA QVAKIPAYSS
QNWLILADQQ GIGQQLANQL RSQGQECVLV FQGEKYRDLG EQSFVVAPDR LEDFSRLLTS
QSAINKVVHL WGLDAPNADV LTVEGIKTAT HNGCGSILHL IQAILQAEAS QLPRLWLVTE
GTQAIANQVL PLPGIAQSPL WGMGKVISLE HPEAWGGMID LEPGLASEKA ASILQAEILE
SDGEDHIVFR QQQRYVARLV RSQHPENLQN LKFQADGSYL ITGGLGFLGL KLAQWMVEQG
AKEIILAGRR GLPPRQQWAS LSENTEEGRK VKAIQALEAK GAKVTILVVD VCDLVQMSLA
LKQVHTIHSP LRGIIHAAGV TPGYQALQNL DSKTLEAVLY PKTVGTWVLH CLTQEIKLDF
FVCFSSAGSV WGAKGQGDYD AANHFLDTFA HYRRSIGLPA LSVNWALIGS GGMVNAEYDR
WLSRIGIEEF PAEAGFNALG FLLAANVTQT VVAKVDWGKF KAVYEANKQR RLLLDIEVAS
ENEPEEATVK QPEILEKLKT AQECDRHDLL VAYLQSEVAQ VLGLGSAHLP DPQQGFFNMG
MDSLITLELR NRLAASLNCT LPSTLAFEFP TINDLVAYLS TEVLGWESSV TETLELPITH
EQVNTLFEIE QLGEDEIEAS ISQRLARLES FLQDAN
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