ID Q8YWG4_NOSS1 Unreviewed; 1570 AA.
AC Q8YWG4;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=All1649 protein {ECO:0000313|EMBL:BAB78015.1};
GN OrderedLocusNames=all1649 {ECO:0000313|EMBL:BAB78015.1};
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690 {ECO:0000313|EMBL:BAB78015.1, ECO:0000313|Proteomes:UP000002483};
RN [1] {ECO:0000313|EMBL:BAB78015.1, ECO:0000313|Proteomes:UP000002483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576
RC {ECO:0000313|Proteomes:UP000002483};
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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DR EMBL; BA000019; BAB78015.1; -; Genomic_DNA.
DR PIR; AC2012; AC2012.
DR RefSeq; WP_010995818.1; NZ_RSCN01000013.1.
DR IntAct; Q8YWG4; 1.
DR STRING; 103690.gene:10493666; -.
DR KEGG; ana:all1649; -.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR OrthoDB; 499075at2; -.
DR Proteomes; UP000002483; 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; 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 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; 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; 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; 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; 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 SMART; SM01294; PKS_PP_betabranch; 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; 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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002483};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..425
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1443..1518
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1570 AA; 170792 MW; AB778DE7B95F6A52 CRC64;
MEPIAIIGIG CRFPGADSPQ AFWQLLSNGV DAITEIPAER WNIDEFYDRN PETPGKMNAR
YGGFLSQVDR FDPHFFGISP REALLMDPQQ RLLLEVAWEA LEDAGIVREQ LTGSKTGVFV
GISTNDYSRI HPEFDSNPQG YDLTGNCINI AAGRLSYLFN LRGPSLAVDT ACSSSLVAVH
LACQSIWNQE SSMAIASGVN LVLSPIGNIA LSKLKALSPD GRCKTFDESA NGYVRSEGAG
CIILKPIAQA LADHDPIYAV IRGSAINHDG RSKGLTVPYG PAQESLIRQA LQQAQVQPKE
ISYVELHGTG TPLGDPIEAM AIGAVLGEGR DAAHPCLVGA VKSNIGHLEA AAGIASIIKM
ALALKYQQIP PSLHFHQPNP YIPFDQLPLR VQTSLIPWPK SKYGAKAGVS SFGFSGTNAH
VILEGVSSFN SPEQQTCKFP HLLPLSAHTP AAVQTLALGY QDLINAQKLT PEFVQNLCYS
ASVRRTHQSY RSAVVVNSPE DLPSCLQALA TADITTQTKQ SKRKPKVAFV FSGQGPQWWA
MGRELLAQEP VFRAVIEECD ALIQKYAQWS LLTEFAVPES QSRFQETEIA QPALFALQVG
LAHLWRSWGI EPKAVVGHSL GEVAAAHIAG VLSLEDAVHL ICHRGRLMQQ ATGNGKMLAV
ELPATEVEPL LTAWAGQLEI AAINSPTATV ISGQSQALQI FVTQLQQQHP DIFYKELPVN
YAFHSQQMAP FAEALVEKLS HIQPQAGSLA VFSTVTGDKQ AGEKFNADYW GQNLRHTVCF
APALTALIQS GYTQFVEISP HPVLSGYINA CLRKQEVDGV ILPSLKRGFG ERATLLKSLG
TLYTLGHSIN WQSLYPDGCQ MVDLPLYPWQ RESYWVSESQ PQFQKALPAS SLLNLLVAGK
TEQLTQELSN HHQLSPEAKQ FIPQLLQLLA TGKSTAKITQ DLSNARYRIE WQLSPLTVDN
KTSEAERWLI FSDNQGLGQE LAAVVNDSCI LVSSGESYEK LSSSHYQINP HQAADFQQLL
ADISEPITKV VYLWSLDSSI NLENSQPQCY SHLLYLVQAL AKISSKIAPQ LWIGTQQAQA
VTPSCHQINV AQTPLWGMGQ VIALEYPQLW GGLIDFGNQD VAATAIIAEM TAKTGEDRVA
FRDGKRYVAR LMPISAPLPA PQPLISDGSY LITGGLGALG LTLAEWLVQQ GARHLVLTSR
QGLLNQSEEK QQKIRALENQ GATVKVVAAD VSDYQQMSQL FAQIQLNSPK LRGIIHAAGV
LNDCSIAQMD SETFTKVFQP KVTGAWNLHQ LTQDLSLDFF VCFSSMSALL GSRGQLHYAA
ANSFLDGLVY HRQSLGLPGL SINWGPWAEG GMATQGYEVG LKRMGIEPLE PTAALQVLGG
LLGSASMQTM VAAINWSAFG KIVAAKGRVA FLEALLTQES KDGSNGENFR QKLSAAPLHR
RPALLTTQVQ QEVAQVLGHS GSYVPEVEQG FFDMGMDSLM SVQFRHSLEA LLAVSLPSTL
VFECPSIGDV VSYLMREVFA WQLDADDSSA MESQASVVIE NTIAQLEGLS TAETEALMEQ
EIAELQALLS
//
