ID W7INP7_9PSEU Unreviewed; 1303 AA.
AC W7INP7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000313|EMBL:EWC62023.1};
DE EC=2.3.1.39 {ECO:0000313|EMBL:EWC62023.1};
GN ORFNames=UO65_2672 {ECO:0000313|EMBL:EWC62023.1};
OS Actinokineospora spheciospongiae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC62023.1, ECO:0000313|Proteomes:UP000019277};
RN [1] {ECO:0000313|EMBL:EWC62023.1, ECO:0000313|Proteomes:UP000019277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EG49 {ECO:0000313|EMBL:EWC62023.1,
RC ECO:0000313|Proteomes:UP000019277};
RX PubMed=24604655;
RA Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA Hentschel U.;
RT "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT Bacterium Actinokineospora sp. Strain EG49.";
RL Genome Announc. 2:e00160-14(2014).
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:EWC62023.1}.
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DR EMBL; AYXG01000093; EWC62023.1; -; Genomic_DNA.
DR STRING; 909613.UO65_2672; -.
DR PATRIC; fig|909613.9.peg.2672; -.
DR eggNOG; COG3319; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR Proteomes; UP000019277; Unassembled WGS sequence.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR036291; NAD(P)-bd_dom_sf.
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; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001031; Thioesterase.
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; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:EWC62023.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000019277};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EWC62023.1}.
FT DOMAIN 944..1019
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 628..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1303 AA; 134702 MW; 16FF17DA60F0199F CRC64;
MRERIGKWSD VLAVAAVNSP GSCAVAGDPA TLDKMVAEFE AEGVRARRIP GVDTAGHSPQ
VDGLREQLLA DMAPVLPTSS QVPFFSTVTG ELFDTAGMGA EYWYRNMREP VEFEAALRAA
LPGTAVVVEV SPHPVLSVAI SEVIEDAASE AGVVGSLRRD EGGLDRVARS LGEAWTHGAP
VDWSSVVPSG ALVDLPTYPF QRQRYWLDVP EVAGDPAGYG LGAADHPLLG AVVALADSDG
LLLTGRLSLR THDWLADHAV WDTVLLPGTA FVELAAHAGA RVGCEAVEDL TLEAPLLFTD
DAVSVQITVG APDDTGARPV SIHSRADDDE PWTRHATGTL TATPATPDFD LTAWPPPGAE
PVDVTALYPE LAAAGLAYGP VFQGLRAAWR DGTDVCAEVA LPEDTAAAGF GLHPALLDAA
LHATAATAGA EDSGRMSLPF AWRGVRVHAT GAGALRVRLS PVDGGVALRV ADAAGLPVAT
VEQLAVRPVT PDQLLPAASP LRDALFQLDW VPLTAGAADT RPLDTHVVPA SAEGSAAEAT
ALTGLVLSRL QEWLADPATA DRRLAVVTRG AAAVAGSDAT DLAHAAVWGL VRSAQSEHPD
RLVLVDLEAD TGVEAVVPTA LATGEPQVAV RGGTPHGPRL ARPAAPEEGA GWSFTPGGTV
LVTGALGTIG ALVARHLVTA HGVRHLLLTS RRGAAAPGAA ELVAELADLG ATATVAACDT
ADREAVDALI ASVPAEHPLT AVVHSAGVLD DGVLTDLTPE SLERVMRPKA HAALNLHEST
KDLDLTAFVL FSSAAGVFGN PGQANYAAAN AFLDAFAAHR RSLGLPATSV AWGYWADRSG
MTGDLVDADL DRIARAGIGA ITTGEGLSLF DAVGALDSSA RDRALLAPVK LDLPALRAQA
GPLGVPPLLS GLIRALPQRT TAAPAGADAL RRRLAGVPDA ERGPVVLAFV REQVAAVLGM
TGPEAVAPTA AFPELGFDSL TAVELRNRLG AAAGVRLPTT VVFEHPTPAA LAEHLAGLVT
DAPGATRAPV GEASTFGPMA KKAIDAKRLQ EFVGLLVMAS SFRPTFTDPA EVGRPQALVP
VAAGPAEVPT LVCVPSVLAM SGPHEYARFA AALRGTRPVS ALPLPGFLPG ERMPATIDAL
IRSLADTLLR DLGGAPFALA AHSSGGPIAH ALAGHLETLG SPPSALALID TYPRNQKVFN
GIQPKLADGM AGEDNGVGGD LRMTAMGGYF DMFGTWNAKP ITTPTLLLRA ADPLPAWRRD
SAWRATWKLD HTSEETPGDH FSMMDEHAAT TALRVHEWVT TQS
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