ID A0A1H1DGS3_9ACTN Unreviewed; 1835 AA.
AC A0A1H1DGS3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:SDQ75046.1};
GN ORFNames=SAMN04489765_1697 {ECO:0000313|EMBL:SDQ75046.1};
OS Tsukamurella pulmonis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC Tsukamurella.
OX NCBI_TaxID=47312 {ECO:0000313|EMBL:SDQ75046.1, ECO:0000313|Proteomes:UP000183053};
RN [1] {ECO:0000313|Proteomes:UP000183053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44142 {ECO:0000313|Proteomes:UP000183053};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNLF01000002; SDQ75046.1; -; Genomic_DNA.
DR STRING; 47312.SAMN04489765_1697; -.
DR Proteomes; UP000183053; 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; cd08955; KR_2_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; 3.40.366.10; 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; 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; 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; IPR009081; PP-bd_ACP.
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; 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; 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; 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.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SDQ75046.1}.
FT DOMAIN 25..452
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1715..1789
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1835 AA; 191410 MW; FFFC69291510A258 CRC64;
MFRMGEIAVK VGATHTTTGS ERAEREPIAV VGIGCRLPGG VRSAADFWDL LDAGRDAIVD
IPADRWSTER YYEPERTPGK SRVRRGGFLT DPVDEFDPAF FGISPVEASS MDPQQRLLLE
VAWESFEDAG LRAEDLERSQ TAVFTGGFTL DYSQMQFSSA AEPPNVAAHT ATGVVMTMLS
NRISHAFDLL GPSMSVDTAC SSSLVAIHLA CQSLWNGESE LALAGGVNLM LSPNFTVAAS
TGGFLSPTST SRAFDAAANG YVRGEGAALV VLKPLAQARA DGDRIYATVL GTAVSQDGRT
NGITVPNGAS QQRAIAAALA NAGVAADTVD YVEAHGTGTP VGDPIEANAI GEVYRGERPA
DRPLVIGSVK TNLGHLEAAA GVVGFIKSAL ALAHRRVPRH LHLDALNPAI DLDALRIRIA
TEPAPLRPEG TLRAGVNSFG FGGTNAHAIL ESVPVDGPRP AAAHPVEECD GVAVVLPLAA
RSEAALAGLA GAYAGLVESD GAVPVAGALV HRRSAHRAAR LAVIAAETAE ASEALRAAAD
GVPHQAVRSG SALADARPLA FVYTGMGPQW WGMARGLLQR NAVFRAAIDR CDAAIAPLTG
WSLAAELLAP EPDSRMAESV VAQIANFGVQ YALSRLWESF GVRPDLIVGH SSGEVAAALE
AGALSFDDAI TVIVHRARIQ HTVSGGGRLL SVAHGEAAAL DLPELARGEV EIAAVNSPDS
VALVGPLAAL DALALRLAAD GVFARLVPGD VPYHSRAMDP LEAEVRASLA GLAPGAPSIP
LYSTVTGTAV PVDGSAPHDA EYWWRNIRRP VLFGAATEAL LDAGAATFLE IGPTAVLGRA
IAETASAHGR TVATTASLRR DGDDAASFGA ALAELWVRGV DVDLTPLAPR APMRSLPAYP
WQRDRYWSEG EAGRRERLAD TVEPYLGDRA DGALPAWRRL LDGTAPRSLA DHVVHGATLF
PGAGYIEIAA EVARDEYGAS ACTLLDVAFE TALVHGGGGT YLVDTTLDAD SGRIAVHGRV
PGAGRWARHA TAVLRPAPSV APRIDLAPIT GTSFTEDVLY DRFRDAGFAY GPAYRLLHDV
TVGDGAATAR IREISAEPVA QRAPVLEPSV LDAAFQLLLP LAFERAAGTT LIPVGVDRVV
IHGRADGPVF ARATARVSPD PTAISGDVVL ATGDGQVLAE VEGFTVRVLD EVDGPPQRVG
TDWVYEQAWE PQAADAGERA PLDGVWLLLA DDGGVAAGLA ERLTAAGGTP VLLRAGAVAE
GALPPSDRRA LAAALERTVP DGRVRGIVHL WSLDASPDGD DPLRWPAHDA VLSVVHLAAE
LENRGIAAPT FLVTDGAQPI TGGVSEAELL QSSLLGIGRV LHHELMGLQA RLVDLDPHDR
YGSTDLLFDE LAVAGTDEDQ IAFRGGERLV PRLHASARSG GRIPARMRGD GAYLVTGGLG
ALGLLVIVAL AQRGAGHIVV TSRSGLPPRS EWDGLTDPAQ RDAVTAIRAA EAAGATVHVV
PVDVTDARAL ADGLADLHRS GVPPLRGVIH SAGAVDDQIL VRMTQEQVER VVRPKVLGAW
ALHRATATEP LDFFTLFSSI SAVIPSPGQG NYAAGNAFLD ALAHYRRAQG LPALSINWGP
WDAGMIASLG LRDLYGQRGI DLIDPETGMT LLAELLGSSE VQQGVVSAHW PTVIASYALR
PSLVAHLGRT EDAEGEDGES ILDRLAAAAG GERGAIVLDG VRLTVSRVLR MAAEHVPDDE
PLGRLGVDSM LATELRIRIE QQFQAAPSMA FLLDGASVAT IAAELTTLLD VAADDGAGDA
EVEDLAALLA DLDDDAVAAL LARSETTEPN AGGPR
//
