ID A0A3D9SGP7_9ACTN Unreviewed; 2114 AA.
AC A0A3D9SGP7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:REE95072.1};
GN ORFNames=DFJ69_0451 {ECO:0000313|EMBL:REE95072.1};
OS Thermomonospora umbrina.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=111806 {ECO:0000313|EMBL:REE95072.1, ECO:0000313|Proteomes:UP000256661};
RN [1] {ECO:0000313|EMBL:REE95072.1, ECO:0000313|Proteomes:UP000256661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43927 {ECO:0000313|EMBL:REE95072.1,
RC ECO:0000313|Proteomes:UP000256661};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:REE95072.1}.
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DR EMBL; QTTT01000001; REE95072.1; -; Genomic_DNA.
DR OrthoDB; 4537517at2; -.
DR Proteomes; UP000256661; 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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd19535; Cyc_NRPS; 1.
DR CDD; cd05274; KR_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; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; 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; 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; 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 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; 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; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 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; SM00824; PKS_TE; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
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; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000256661};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:REE95072.1}.
FT DOMAIN 5..431
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1317..1392
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2114 AA; 225076 MW; C9DE34FB80E50451 CRC64;
MSADDGLVAV TGLACRFPGA SDAEAYWRLL AEGHEGLTRL GEEELAERGV PRRLRRDPAY
VPVAGLIDGQ DMFDPEPFGL TDGEAALLDP QQRLFLEICW RALEQAGHGG GRDAGSVGVF
AGAAQSAYLA SNLAGRWDPT GGGTDPVGSL QTAIATQTDY LPAQVAYRLD LTGPAVSVAT
ACSTSLVAVH MAVQSLVAGE CDTALAGGVS LIVPQGRGYL STPDGIYSED GRTRPFSAHG
TGIVYTQGVG AVVLRRLRDA QEDGDPILAV VHGSAVNNDG ADKTGFTAPS VRGQARAIAE
ALSIAGADPR GVGYVEAHGT GTRLGDPIEV AALRRVFGDT GPAWCGLGSV KSNVGHTNSA
AGIASFIKTV LAVRHGVLPA SLHAEPINDL LGLAGSPFEV VTRTRRWDGP ELAGVSSFGI
GGTNAHVIVG PAPQRPDPAP DPRPHPVVLS AHSPEALRRT AADLAGTKAP PADLAFTLQQ
GRVHLPHRLS VVAENGDLVE ALRKATPVRA PDGKPRLVFA FPGGGSARVG MGSALYDNER
AFRESVDECA ELFAGHLGFD IRAVIRGDEG RIRGPVHGLP ALFSVSLATA RLLGTWGVRP
DLVLGHSLGE YAAAVAAGAL ALEDAARLVA VRSRAMADAA GDGAMLAVPL GEDATRELLG
RHPAVDLAVV NAPDSCVVSG PRPAVDELEK ALVREGHEPT GLRFDGAAHS RLVDPALPRL
RAAAAGLTGS APTVPVVSTL TGDLVKGELG TAEHWVRQLR EPVRFSQALR TADPAVLVQV
GPGGALAALA QGNRLPGLRA ALTTLADDDL AALYETAGRL WTHGVDVDFG GMHRPGRRRV
AAPGMAFRRR RLWIDPPAEP VRQADDQPDE DEPLQIPVWT QATPLDPTTT LEGRWVVVGD
AQDIVIKALT AAGAEAVPFA HAAERPDEDW TGVIVIAEGR PERRHDPRAV EDGILAHARL
ASLFFTGQAR LLLQVTRGAH QVTGAERPDP AVAALHALPR VMAQEQPGAR WRILDLDERA
DLAEAVPSEL ADLVAGGGSG VESAVRGATR WIRGLRPWRP GRRDVAAGST ALITGGLGDV
GLTTAAHLAR KGLRVVITSR GGTPTGERAE SLRKLTDEGL SIEVRTLDAA DTEGTAALLE
ELAPLDLVVH AAGVVATADL QPLRRVGPDQ ITGHVHAKVT GALALRAAID RLPADRRPRD
VVLMSSAGTL VGGIGMGPYC AANRFLDALA EETPQDGTRW VSIVWDAWKV GPVGTERAVR
LTFALGARTG MDALDRVLAD RRVPVVAVST TDLRERAARA AYTAPVRVTA ESQAGETTLS
PAERAVAALW SELLGVEVTS ADTDFFALGG HSLLATRMLT ALRGEFGVEL RLRDLLSHPT
VGGLADLLHH AEPEAAPEPV ARKAVSADGT FPMTRVQHAY WVGREGGYAL GEIACHFYLE
YDCAGLDLVR YENAWRQVIA RHPMLRTIVT RQGRLKVLDH VPPYRIRVHD LTGLGEKERD
ERLARLRERV SRDPGPPDRW PLVQLQAARL PGGRVRLFIG VDVLICDAGS YWIIDREVRH
FYEHPGTRLP EPGIDFAACV AALGRAEEDD ARYWRDRLDT IPGPPPLPLA EHDGPPRFVR
RTARLTPGEW QALKREAARW RVTPTAVLLT AYGEALARWS GGDHFALTLT LFDRPAIHPD
VDKVVGDFTS LLVHEVDRRA VGSFAAQVRR TQQRLFADLD HRSYSALDLV ADGRGRVGSV
PVVFTSALGL EDLVGGEPDL QWVGEQVHAV SQTPQVWLDH QVLVQRGELL VQWDAVADLL
PDDEVDEVFA AYAARLKELA APSSAWGDGP DDDDILVPLR DGTGEQTLFL LHPSGGDVLC
YAELSRLLDE RFSIVALTDP GLAGRAAPAD LAGLARLYAD VIRRHRPRGP YLLGGWSMGG
SLGQEVARLL HDDGERIGLL LMLDSNDPTY ITPLPGDAEA EATVRLLGAF EAYLGVDLGV
GTEEGRAAAR TLPPEAVAAR LREHRLLGRG EDVRERVGVF ARHLRGLGDH TPRRLDDPAA
VTLLVRAERR ASRNSGIGMG VDDTPPGLPD LGWQRHLAGP PEVHGLDADH YGLLRPPTVA
RLADLINKAL SKNG
//
