ID M2Z4F7_9PSEU Unreviewed; 1449 AA.
AC M2Z4F7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:EME62127.1};
GN ORFNames=H074_09340 {ECO:0000313|EMBL:EME62127.1};
OS Amycolatopsis decaplanina DSM 44594.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1284240 {ECO:0000313|EMBL:EME62127.1, ECO:0000313|Proteomes:UP000054226};
RN [1] {ECO:0000313|EMBL:EME62127.1, ECO:0000313|Proteomes:UP000054226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44594 {ECO:0000313|EMBL:EME62127.1,
RC ECO:0000313|Proteomes:UP000054226};
RX PubMed=23558534;
RA Kaur N., Kumar S., Bala M., Raghava G.P., Mayilraj S.;
RT "Draft Genome Sequence of Amycolatopsis decaplanina Strain DSM 44594T.";
RL Genome Announc. 1:E0013813-E0013813(2013).
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EME62127.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOHO01000043; EME62127.1; -; Genomic_DNA.
DR RefSeq; WP_007029779.1; NZ_AOHO01000043.1.
DR PATRIC; fig|1284240.4.peg.1889; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000054226; Unassembled WGS sequence.
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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd08952; KR_1_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; 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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..457
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1303..1381
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1449 AA; 152454 MW; 78280985B92E8721 CRC64;
MATPEELVTA LRESVKENSR LAARNRELAD AAREPVAIIG MGCRYPGGVD SPEALWDLVA
AGRDAVSEFP ADRGWNLAEL FHPDPDHPGT SYAREGGFLH EAAEFDPEFF GISPREALAM
DPQQRLLLQI SWEAIERAGL DASALKGGAT GVFAGLMYHD YGSGVTELPE GVEGFLGTGT
AGSVLSGRVA YTFGFEGPAV SVDTACSSSL VAVHLAAQAL RAGECSLALA GGATVMAVPD
TFIEFSRQRG LAPDGRCKSF GAGADGTGWG EGAGVLLLEK LSDAVRNGHR VLAVVQGSAV
NSDGASNGLT APNGPSQQRV IRAALASARL STSDIDVVEA HGTGTKLGDP IEADTLLATY
GRERENPLWL GSVKSNIGHT QAAAGVAGII KMVEALRRGE LPRTLHADEP SPHVAWDSGA
VELLTEHRPW PETGRPRAAA VSSFGISGTN AHVILRQAPE PAPVETATAE RVRVPWVLSA
RTEAALPELA DRLLQTGGDP ADIAWSLATG RAALPYRAVV TGADEDELRT GLGALARGES
APGVVTGRAG SGKLAFLCTG QGAQRLAMGA GLATAFPVFG EEFARVAERL DAHTGFRLAE
VLACEDKTRI DRTDVAQPAL FAFEVAMAEL VRSWGVEPDF LLGHSIGDLA AAYIAGVWSL
DDAARLVAAR GRLMQAQPSG GVMVALQATE TELDLPGGVS IAAINGPSSL VLSGEETAVA
AVLEAFPGRR SKRLSVSHAF HSAQMDGMLD DFREVAASVS YAEPRIPVVS GDVRDPEYWV
RQVREPVRFA DGIATLHARG VRRFVEIGPD ASLTALGADC VSDGVFIATQ RKDRDEAAAA
DLARGRLFTA GVGLDWARIF DGTGATRVDL PTYPFRRDRF WLAAADRSAP PARRYEIVWR
PIEPMVTQEA WTVYAAEGNA WAEAAAKALD APLVTEVPET GPVLAFPADG AALAALLRDT
PAKIWCATGD PGVAAVARVA AIEQPRRWGG CVIVPDQTDA AARLSEVLGG PEDEVAIRED
GIFARRFVPA APAPATTWST SGTALITGGT GALGGFVAER LIRAGTEHLV LLSRRGEEAP
GAAELRERLE GLGARVSIHA CDTADRDALS TVVTGIDDLR VVVHTAGVLD DALLDDATPE
RFEAVARPKV TAARHLRELT KDLDALVLFS SVAGVLGNGG QAAYAAANAE LDALATQWRA
EGVKAVSIAW GPWAEGGMAE AVDDAVRRKG LRPMTPEAAA EEFVRAIAAD DTCVTIADFD
WPSFFEDFRA APMLAELPRP ETAVAEAPVA DLRSRLNGLI EPEQRRLLLK VARETVARVL
GHPDTSAIGP DRAFTELGFD SLTAVELRNR LDAATGLAVP ATLVFDHPTP QALAAYLWQE
LAGAAVNDID VDGLLDGLEA ALSRLDPGSD EHAKAGARLR KLAESLDGPG FTPSSDDELF
AFIDRQLGA
//
