ID C3MFV8_SINFN Unreviewed; 2500 AA.
AC C3MFV8;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ACP24009.1};
GN OrderedLocusNames=NGR_c02090 {ECO:0000313|EMBL:ACP24009.1};
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24009.1, ECO:0000313|Proteomes:UP000001054};
RN [1] {ECO:0000313|EMBL:ACP24009.1, ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
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DR EMBL; CP001389; ACP24009.1; -; Genomic_DNA.
DR RefSeq; WP_012706794.1; NC_012587.1.
DR RefSeq; YP_002824762.1; NC_012587.1.
DR STRING; 394.NGR_c02090; -.
DR KEGG; rhi:NGR_c02090; -.
DR PATRIC; fig|394.7.peg.3007; -.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_31_5_5; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000001054; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05195; enoyl_red; 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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; 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; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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; 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; 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 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; 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.
DR PROSITE; PS50890; PUA; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
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:UP000001054};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..422
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2391..2465
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2500 AA; 266013 MW; 699911FC45A7BD82 CRC64;
MTVEIIGRAC LAPGAQSPQA LFKILRQGMC TVSSVPGDRW DLARFWHPVM GTQGKTYSFA
AGVLETIYDF DPAVFGMSQR EAMYMDPQQR VLLQLAWRAL EDANISVASL HGENVGVYIG
ASSLDHANLT VEDPAAAGPY FMTGNTLSIV SNRISHVFGL SGPSMTVDTA CSSSLVALDQ
AMRALNAGEI DTAIVGGVNI LAHPLPFVGF AQARMLSPEG LCRAYDNDGA GYVRAEGGVV
FVLRRSDRAR REKDRSYARI VASGVNSAGR TNGISLPSRE AQANLLKAIY EGNGIDANQV
AFVEGHGTGT KVGDPAEVWS IGTVIGAKRR APVPIGSIKS NIGHTEPASG LFGMMKAVLA
LEHNYLPASL HFDTPNEHID FEGLNVRVTA NPIELLKGKR ARLAGINSFG FGGANAHVVI
SDPDPVPQEK APATSAGHVF LASAHTQSSL ENLLKDYKAS FANASKEEAR AIIAASGANR
THMRHRFAAR SDHPEDIVRA IASHLDKPGS DIGEVGEAPV KNAQVAFVFS GNGSQWAGMG
VDAFRENLHF RQSFTSISAL FKFHSDIDLK DLLTDPELDK KLADTKIAQP LLFAIQAALS
DSLVAMGVKP AAVFGHSVGE IAAAYAAGAL TLVDAVSIVA KRSLHQDLLA GQGTMAAVML
GEEAAAAFAE ARGLDEVCVA AVNAHNSVTI SGPAHEVTAF RDAARKAKIP VQILDINYPF
HHPIIDQAKE AFLADIPDIA PRRTELTYLS TVTGDALDGT ELDPDYWWKN VREPVRFQAA
TDAALALGCR LFIEISPRPI LASYVKETIK QAAAPAMVVA TLLRDAAEKG QDPISASMAR
AVAHGAAVDR IRVYGKRDAL IELPSLPFEP VELRPQATTD ATDLFGRSSK PYRLTGWRGD
PNSGSWKNHV DAHLFPDLAE HVVDGKAILP GSGFIEVAVS AAQQYYGSDE VEITNLEIVR
PLELSDSRIM ELSTILSPET GDIEIRSRER LSEDDWTVHA VARSRKPIAR ANTRHASISS
LAKSGIVTPA KAYDTAKQFG LDYGPHFQLL ARAVAYGDRL IEVELKAPAG SGHPFVSYAL
HPISVDATFH GLVALFDRFT GDKGGAPYIP VRFGSVRVVN AGRPIARATI EIERVSANSI
KARFHFYDAA GEPIAHFDDC RFRRTYLRKH KALDGLSFHY ETVLSNVILP GTKVAGTVPA
KLSEPADAES GVDNATLLFN AAIYRACHEI ALKLARGRST IPGNGLPGDF AFQCFLTNCL
YALEDAGLCE HQDGNWKVAP EFTLPTVAEI LGELYGERPD RAVEAVLINN AHAEALGRLT
TLLAGTASGE AAAFNAGFIS EATLDHQAVH SVASRSRMDQ ILGMVERALA AQVEGARLRI
VELGSVSAGF TRRLADLAAR HGTTLSVVEP RDNAQRNLEI AFEEDAHVRI LKKSEFAAIG
PFDLAVSASD NLYQLIEEEA GIRTALRSAL RESGALVAAV SAPSIFSDFA LGLSEGWFER
SQTAEFPIGK RAAVSHWQKC LAELELADVS VSDCECPHGN AILIEARGTA VAAGPLASAA
GGIPYLLVET GVRGSSAAAG AIPVAVSGDM VADIDLLGTA LDGFGEKPVR AVFLSATTDH
VGDGDSALLQ TQVLALSAFA ETLKQRVANA ELVGEARPRL VLVAPGGAPV SESASSGVNS
GLWTFVRVLQ NEYEFLDVHS LDLADQTASR EEMLASALPL LTIEGSNREW LLDRATGLIS
EIRAVSGPAA KSEGKISAFS AATIRQRVSS QVSSITWEET DVPRAGPGEI VVSVAATGLN
FRDVMWAMGL LPEEALEDGF AGATIGMELS GHVVEVGEGV DDLAIGDAVM AIASAAFSTH
AVVSRAGVAK LPQTISPVAA ATLPVAFLTA YYAMVELGRI RSGETILIHG AAGGVGLAAL
QVAKLKGAKV IATAGTREKR RFLTMLGADH VFDSRSLGFV NDVRSVTGGE GVDLVLNSLF
AEAMEQSLAL VKPFGRFLEL GKRDYYADSK IGLRPFRRNV SYFGIDADQL LVNQPELTKQ
IFMEIGELFD QGRLTPLPYR AFDFDEIGNA FRLMQNAGHI GKIVVLPPVA GKHEIAAKPR
RGMKVDPDGM HLVVGGIGGF GLVAANWLVE KGARNIALCS RRGQPDTATS AMVERWKKAG
VAASLHACDV TDATAVEALL ATLRGQAPLR SIVHAAMVLD DALISNLTRE RNRPVIDVKA
KGAAILDRLT RQDTLDNFIL FSSATTLVGN PGQANYVAAN GYLEGLARTR RAAGLAGLAV
GFGAIADAGY LTQNADVNDL LAKRIGKTAL KAHMALDMVE SHIAADPGSI DAAVVMISEI
DWGAARNLPV TRNALFEVIL RSADQHASGT EGTKMDLVAM IEGKAPQEAE DILFDLVAGE
IAAILRVAKD TVTRGKILKE IGLDSLMAVE LGISFQQNTG FDMPLSGVAD NTTVGDVARK
LYEKVSKRDQ SDDGEAGDDK LVTELTQRHV GAAKEKALSQ
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