UniProt: K9XLC2

Database: UniProt
Entry: K9XLC2_9CHRO

LinkDB:  K9XLC2_9CHRO 
Original site:  K9XLC2_9CHRO

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Ontology (5)   
   GO (5)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (46)   
   InterPro (24)   
   Pfam (12)   
   PROSITE (3)   
   SMART (7)   
All databases (56)   

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ID   K9XLC2_9CHRO            Unreviewed;      2448 AA.
AC   K9XLC2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AFZ33410.1};
DE            EC=1.6.5.5 {ECO:0000313|EMBL:AFZ33410.1};
DE            EC=2.3.1.94 {ECO:0000313|EMBL:AFZ33410.1};
GN   ORFNames=Glo7428_5010 {ECO:0000313|EMBL:AFZ33410.1};
OS   Gloeocapsa sp. PCC 7428.
OG   Plasmid pGLO7428.01 {ECO:0000313|EMBL:AFZ33410.1,
OG   ECO:0000313|Proteomes:UP000010476}.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Gloeocapsa.
OX   NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ33410.1, ECO:0000313|Proteomes:UP000010476};
RN   [1] {ECO:0000313|EMBL:AFZ33410.1, ECO:0000313|Proteomes:UP000010476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ33410.1,
RC   ECO:0000313|Proteomes:UP000010476};
RC   PLASMID=Plasmid pGLO7428.01 {ECO:0000313|Proteomes:UP000010476};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished plasmid 1 of genome of Gloeocapsa sp. PCC 7428.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003647; AFZ33410.1; -; Genomic_DNA.
DR   RefSeq; WP_015191277.1; NC_019746.1.
DR   KEGG; glp:Glo7428_5010; -.
DR   PATRIC; fig|1173026.3.peg.5279; -.
DR   eggNOG; COG0500; Bacteria.
DR   eggNOG; COG0604; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000022_35_5_3; -.
DR   OrthoDB; 499075at2; -.
DR   Proteomes; UP000010476; Plasmid pGLO7428.01.
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:0003960; F:NADPH:quinone reductase 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; cd05195; enoyl_red; 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; 3.40.50.11460; -; 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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
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; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR020843; PKS_ER.
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; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 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; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 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; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
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:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:AFZ33410.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000313|EMBL:AFZ33410.1};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Plasmid {ECO:0000313|EMBL:AFZ33410.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010476};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFZ33410.1}.
FT   DOMAIN          36..458
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2326..2404
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   COILED          7..34
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   2448 AA;  268951 MW;  01C7E377E88201BB CRC64;
     MNQRSPQHDY RTLMQNALRE LQQMRAKLAT LEQNKTEPIA IIGIGCRFPG GADTPAAFWQ
     LLQNGVDAIA EVPPNRWHLD SYFDPNPEAP GKIYTRYGGF IDNLETFDTE FFGIAPREAL
     SLDPQQRLLL EVSWEALENA GIVPKNLSGS KTGVFVGISS NDYSHHLLTR EPDEIDAYLA
     TGNSHSTAAG RLSYTYGFVG PSFAVDTACS SSLVAVHLAC QSLRNQECDL AVVGGVNRLF
     APEFTINFAK ARMLAADGRC KTFDAAADGF VRAEGCGVVI LKRLADAIAD RDKILALIPA
     SAVNQDGRSS GLTVPNGPAQ QSVIVEALRN GNIDPVQISY IEAHGTGTAL GDPIEVNALG
     AIFGKSHTFD QPLRIGSVKT NIGHLEAAAG VAGLIKVILA LQNRQIPPHL HYKQPNPHIP
     WQQLPIQVTT ALTPWTGSIA GVSSFGFSGT NAHVIVAEAT NSAVEASSHV DTPQILTLSA
     KTLPALSELT KRYEAYLAAN PNVSIADVCF NAQTRRSHFQ HRLAIVAQSS REAQEKLKLF
     NTHQQESTTK HRPKIAFLLT GQGSQYANMG KHLYQTQPIF TQHIDRCCEL LQPYLSIDLR
     EVLYPKAECQ LNLNDTIFAQ PAIFIVEYAL YQLWTSWGVY PDVVIGHSIG EYVAATIAEV
     FSLEDALKLV VTRAQLMQAL PPNGKMVAVA ANETTVAAII EDYQQVSIAA INAPENTVIS
     GNINAVDAIV TTLEAQHIAA KTLAVSHAFH SPLMQPMVQK FAQIAREVEY NAPKLNLISN
     LTGKLAGDEI ATPEYWCEHI LQPVRFAAGM KVLAELDCNI CVEVGAKPTL LGLGRAILAN
     SNILWLPSLK PSDQINPILS SVAQLYVAGV KIDWRSFGCD RPLLALPNYP FQRQRFWVDV
     AKKSPRIIDN GLHPLLGQRF ELARPKTVYF ENYLGLNRLS YLQDHQVFDK IIFPGAGYLE
     MAIAAGNLVL NTNVILENVE ISQALVLTET KLQLVLQHNK FEILSLSAAT DEWIVHATGK
     IQSLNEPQNP TFIDIATVQR QCQEINPLLY YQTLRSHGIN YGATFQAIAQ LWQGENQALA
     QIQLPPELTD TNYRLHPVLL DAAFQAIGAA VNEELSIYLP VGLEKLVVYK NAPRSLWSYV
     QVYTTNAPGS LKADVQLIAA SGELVATISG LHLRQAQQAL DVYRDWYQVE WQSEGRVRWI
     PSLASVCDRL SPTVQNLVAQ PEIQQYQKLL PQLEKLSISY VIDAFTSLGW QFVPNQYFST
     SQLVEKLAIA PQYQQLCDRL LEMLAEEHFL RRHDDLWQVV ALPQSTAPQL TESVELTLLD
     RCGKELANLL QGKTEPLQLL FPQGDLTNAT QLYQDSPAAK LMNTLVQQVV LALEKPHYRR
     VRILEIGAGT GGTTAYLLPH LDPAVTEYTF SDVSPRFVHN AQQRFQEYAF VQYRVLDIET
     PPQAQGFAVD RYDIVIAANV LHATCSLAQS LAHVQQLLVD DGVLILLEST QKLRSLDLIF
     GLTDGWWRFG DRDLRAKHPL LSVAQWQQLL ANCGFVDVAA IAPEPQSILL ARKQVFCQWV
     ILCDRLGLGE ELARLLAQRG DDCVLVFAEE VDWRRVFEDA ERGVRVVYLW GLDGETNHRD
     AESAEGRSKG GLVGECRCVL ELVRGLGDKS AGLWLVTQGA VMDVDRRGIW QSPLWGLGRV
     IALEHPELGG FCVDLDPAVG VVEQASELCA VLVDSLPQVA LRNQQCYVPR LVRYCSSLLE
     VSEPFRLGMS TKGTLDLQFQ PMMRNAPQAG EVEIRVRATG LNFIDVLDAL GLLPFERDWF
     GVECSGEVVA VGDGVEHLQV GDAVIALAPA SFAQFVTTNA KWVVLKPHNL SFATAATIPA
     NFLTADYALN HVAKIIRGKR ILIHAAAGGT GMAALQLALQ AGAEVFATAS PSKWQQLQAM
     GVKHVFNSRN IDFAAEIMVL TDGEGVDVVF NSLSGDFIAK SLSVLKPDGH FLEIGKRDIW
     SQTQVQQVNP GATYTLIDLM SVAQQQPDRM QSMLRHLVSL FATSQLQVSP QTVFPIEKVV
     DAFRYMQQAK HIGKIIITHY PLPLTSFPGT YIITGGLGGL GLLIANWLVE QGARHLVLVS
     RREADAEIIQ RIEMLKSAGA EILVISADVT DESQVSGVLS TIKSSLPPLR GVIHAAGVLD
     DGVMQQMTWE RFAKVLYPKM LGAWHLHTLT QDQPLDFFVL FSSAASLLGS PGQANHVAAN
     TFLDALAHYR QAQGLPGLSI NWGAWSVVGA AAKRGVAQQM RSRGIHEISP QQGLQSFAAL
     LRQTAAQVGV VPIDWSTFLQ HTNSDFFADF QTATQPKSPP QSVKVERPQQ LKAYLQTEVA
     QVLGLPISQL PALKQGFFEL GMDSLMTVEL KNRLETNLGV SIPASAIFEY PTIEDLAGYL
     AEKLANNSDT NLQPKTEDND DPNLTNADII SELAELETLL QGQTDESN
//

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