ID G4RJD0_CHOCO Unreviewed; 2963 AA.
AC G4RJD0;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AIR74926.1, ECO:0000313|EMBL:CBD77746.1};
GN Name=croI {ECO:0000313|EMBL:CBD77746.1};
GN ORFNames=CMC5_030080 {ECO:0000313|EMBL:AKT38862.1};
OS Chondromyces crocatus.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC Chondromyces.
OX NCBI_TaxID=52 {ECO:0000313|EMBL:CBD77746.1};
RN [1] {ECO:0000313|EMBL:CBD77746.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Cmc5 {ECO:0000313|EMBL:CBD77746.1};
RA Rachid S.;
RT "Isolation and Characterization of the Crocacin Biosynthetic Gene Cluster
RT from Chondromyces crocatus Cmc5.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AIR74926.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Cm c5 {ECO:0000313|EMBL:AIR74926.1};
RX PubMed=24981773; DOI=10.1016/j.chembiol.2014.05.012;
RA Muller S., Rachid S., Hoffmann T., Surup F., Volz C., Zaburannyi N.,
RA Muller R.;
RT "Biosynthesis of crocacin involves an unusual hydrolytic release domain
RT showing similarity to condensation domains.";
RL Chem. Biol. 21:855-865(2014).
RN [3] {ECO:0000313|EMBL:AKT38862.1, ECO:0000313|Proteomes:UP000067626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm c5 {ECO:0000313|EMBL:AKT38862.1,
RC ECO:0000313|Proteomes:UP000067626};
RA Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT high potential for natural compound synthesis and the genetic basis for the
RT loss of fruiting body formation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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DR EMBL; KJ868728; AIR74926.1; -; Genomic_DNA.
DR EMBL; CP012159; AKT38862.1; -; Genomic_DNA.
DR EMBL; FN547928; CBD77746.1; -; Genomic_DNA.
DR RefSeq; WP_050431043.1; NZ_CP012159.1.
DR STRING; 52.CMC5_030080; -.
DR KEGG; ccro:CMC5_030080; -.
DR PATRIC; fig|52.7.peg.3308; -.
DR OrthoDB; 9757540at2; -.
DR Proteomes; UP000067626; 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 GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd12116; A_NRPS_Ta1_like; 1.
DR CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.10.129.120; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 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; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
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; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 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; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
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; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000067626};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 999..1074
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1107..1532
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2842..2917
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2963 AA; 319855 MW; B207B7220269E8E9 CRC64;
MSEELRGAGD TAPSLVSNTA RPAGATSHPL SYGQRALWFL HQLSPQSHAY NTLFAVRIRS
TLDLAKLAEA FRLMVQRHPT LRSTYCLEDG VPRQIIHPSL ELPLVEEDAA SLDEKQLAPR
LLERAHRPFD LVRGPVARAH VFTRGPEHHV LLVAAHHITC DFFSGASLLE ELFAAYSALR
CGELPTLPTP ALQYTDFVAR QEELLASDGE ELFAYWQTQL ATAPVSLDLP LDRPRPPIPT
GRGASVSFHI GSELTRRIST LTRSQGATLN MALVAMFQVL LHRYTRESDI VVGSPMAGWS
RSEFKGVVGD FINMVVLRSD LSADPSTKEL LLQVSERVMG ALMHQDYPFP LLVERLSPTR
DPARTPFSSA AFLFHDLDRF GPLGRLFSPA QGKSLEVGEL KLEGLYLPQQ EGQFDVTLEV
LYAAEELHGN LKYNADLFLP ETVERMAHHY AELLAAMVEA PERPVGQLRL LGKEEREAVL
RAGQGPSSSL AVEVPFHAQW EKLAEREPSA IAVEDEAKRL TRAEVNARAN RLARRLRTMG
VGPEVSVGLS LQRGVDLVVG LLGVLKAGGM YVPLDPGYPR ERLSYMLEDA AVKLLLTDEA
SLEQLPTASG VETLLLQDVE RSASDEPASD LKLAVAAEQC AYMLYTSGST GRPKGVQVPH
GALANFLRSM AERPGLSATD VLLAVTPLSF DIAGLELYLP LVTGARLVVA SQATSRDPER
LGRALAQHGV TVMQGTPSTY RLLLQHPEVL NRGFKALCGG EALPGDVCSR LLEREVALWN
MYGPTETTIW SAAGPVQDAA RVDLGTPVDN TDLYVLDEAL ELVPPGVSGE LYIGGAGLAR
GYWRRRSLSA ERFVPDPFST TPGARMYRTG DVVRRQADGR LLYQGRSDAQ VKIRGFRIEL
DEVEAWLSTH PSVRAAVVSS VEDERGGGAQ LVAYVVPAGA APSVEPLRAH LQERLPEYMV
PGQYMVLDEL PLTPAGKVDR KRLPRPTFDR ATLQTRYTPP TTTEEKQIAA LWKEVLRIER
AGLDDNFFDL GGNSLLLVNL HARMCAALAV DFTLTDLFSH PTVSAQAALV RRLGGDAGDR
ASEARERRVR RAARRGTETV DEAPGRDTDI AIVGAAGRFP GARTLDAFWH NLWAGIESIA
FYSAEELLAA GVPSDIVANP AYVRAKGELE DIDLFDAEFF GIPPREAAVL DPQQRLFLEC
AHEALENAGY GGEDRPGPVG VFAGAGINGY LLFNLHGRTR SLAGDYQLFI SSDKDFLATR
AAYKLNLTGP AITVQSACST SLAAVHMACR SLIEDQCDMA LAGGVAVSVP QRAGYMHQEG
MILAPDGHCR AFDANASGTV PGSGLGVVVL KRLRDALADG DCIHAVIKGS AMNNDGAAKV
GYTAPSVEGQ ARVIEEALEV AGVEPETIGY IEAHGTGTPL GDPIEIAALT RVFRTAPESP
PSCAIGSVKT NIGHLDIAAG IAGLLKTVGM LERGQLPPTL HFQKPNPALQ LDQSPFYVNA
EPRTWDRVGG PRRCGVSSFG IGGTNVHVVL EEAPQPTVTT APSERPAYLL PLSAREPQAL
RELAVRYQRH LEQHPDASPA DIAFTAGAGR RHFRERITLV GSSVEQWRRE LGAFLDGRAS
NAVSAGEVPG EGAPRIAFLF SGQGSQYAGM ALPLYRTQPV FRAALEQCDA LLRPHLRIPL
LDLLAAPQDG RSPLEQTLYT QPALLAVEHA LDRMWRSFGV FPSAVMGHSV GEYAAAISAG
VLTLSEGIEL IVERARRMHE LREAGAMATV FAKAERVLPL LARHEARLAI AAFNGPAEIV
ISGARDALED VLAQLTADGV ESRRLHVSHA FHSPLMDPML EGFAAVASKH RGSPPTIDFV
SNLTGALIAP STSVGPGYWA EHVRAPVQFY QGLQALRARG CTVMLEMGPH PTLLGIGRRA
LADRMALTWL PSLRREHRDW DVVLGSLAQL YTRGVPLDWR AIQPGARTAL PTYPFQRKRF
WIDPETTSSR VDRREGPVSA EVHPLLGRRL RLGLARHTLF EARYDGATTP YLRDHHYFGR
AVAPAVGYLL MAARAAGKLP LSLEGVKFSA ALALSEGEHR TVQTIVQRDD QERTSFQICS
FPDDDIRPET EPTVHAQGRI GRLVAPTASD APAAAAVAAA SGRHSVALDE IHARCAKAQT
GAGFYEVIAR QEVDMGPSLR WIETLHSGDG EALSRLRSPA AEDGADIDLH PGHLEAGLQT
LSIAAASRLS AVEAGVVYLP VAIERLHLHG SLAATRFAHA RLREGNDVHD GYTGDIHLLS
EDGAVLTELT GVRYRRVARE RLRPMEAQPA TPLHRIAWEP APAVAPPPGM VSSGPCWIFA
DEGNAGSSLR AHLERTGVHC HLIRRGERLD TPGPGIHTLD PDQPEQLDQL LDTLAQHGKP
RGIVILWPLD ESPGDPHPQQ GAGMGGALAA TQRLCSRALT LVQKLAPRWS AGDGRLWLVT
RGAQTVGTNP APVSPTQAAL WGFGRVLASE HPEFQSGLID LDPESSADEA SHLAAALLAS
TDEDQIALRG GRAHHARLRP QPDTLPVSGR RPVLGGGVHL ITGGLGGLGL LLGRWLAHAG
AETIVLMSRS TPGPEAIRAL DELKTGPARV RVMQVDVSRA DALSAALDTL RREEGPLRGI
FHLAGSLSDA VLLRQDPERL HAVLAPKVAG ASLLHALTLH DPLEHFVLFS SIAAVLGTPG
QANYAAANAF LDGLAQHRRA LGRPALSIQW GPWAGAGMAA EQGAADRRAA HGFESMPPEQ
ALALLERLLG GAAGDIGVFR VDWRLLLARL PTVPPLLVEQ LPAEARTARA PLASPAGAPE
TAAGPPAWIR SLEAALPEDR EGLLRARLLD LVRQSLGLAH DRPIDPRMPL HELGLDSLMA
VDLREAIGKS VGLRFPATLL FNHPSIEALV AFLRRELPIL AEPERAAPQE DVVTEALLRN
LQDLSEDEAE AQLLEKLALL EDL
//
