ID A0A1A8ZHN1_9ACTN Unreviewed; 3127 AA.
AC A0A1A8ZHN1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:SBT43338.1};
GN ORFNames=GA0070621_1759 {ECO:0000313|EMBL:SBT43338.1};
OS Micromonospora narathiwatensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=299146 {ECO:0000313|EMBL:SBT43338.1, ECO:0000313|Proteomes:UP000198765};
RN [1] {ECO:0000313|EMBL:SBT43338.1, ECO:0000313|Proteomes:UP000198765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45248 {ECO:0000313|EMBL:SBT43338.1,
RC ECO:0000313|Proteomes:UP000198765};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT594324; SBT43338.1; -; Genomic_DNA.
DR PATRIC; fig|299146.4.peg.1822; -.
DR Proteomes; UP000198765; Chromosome i.
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; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
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; 2.
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; IPR006162; Ppantetheine_attach_site.
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; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 2.
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; 2.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000198765};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SBT43338.1}.
FT DOMAIN 36..449
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1173..1248
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1325..1750
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2985..3062
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 565..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3068..3107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3127 AA; 324139 MW; A78CCBA82F975671 CRC64;
MDDTDNAAAK RQDAQLKRAL ATIRTLRRRL DEQGGDQPVA IVGVGLRLPG GIDGAEAYWD
ALAAGRDLVG PMPSRRQGPF AAEWADLPQR GGFLDEVLDF DADFFGISPR EARALDPQHR
LLLEVAWEAL ENAASPADQL AGRPVGLYVG ITGQDYRDWL PGEPDAYWAT GNGHCFAAGR
LAYSLGLTGP AMAIDTACSS SLVAVHLAVQ ALRRGECEVA IAGGVNLIMS PRSTRLVVQT
RSLAPDGLCK AFDARANGFT RGEGAGALVL KPLARAVRDG DRIHAVIRGS AVNQDGRSSG
FTAPNVLSQV ALIEQALAGA GAGPADVGYV EAHGTGTALG DPIEMEALAT VLGRRNGGAP
LAVGSVKTNL GHLEAAAGVA GLVKAVLCVQ HRQVPPVVHL RTLNPRIDLG GTGIVVPDRL
VDWADGAGRL AGVSSFGMSG TNAHLLLGPV EPDELAERPT PPAGPVAGFV VSARTPVALR
ALAAAYAQRV LRLPAADFPA FAATANTGRS RLPVAAWVAA ADPAAAYAAL TALASGAPPV
EVDPAVLVAA ADRRAVLDLP TYPWQRQRHA PERPATGEPD RPTPAGHTHE VVWVELDRPS
AADHAGPLIL AGDDAPLLAD LASAAAARGR SGTLLSPDPV AVPAGWRTTP LPADAEGWAR
FWAGRPDGPA ETLVLVPAAH PVLDHAAPRH EVAPTAGRDA AGPAGAAAEP SDAGYGAAGP
AGAGPEATDP AGAGPEAAEP SDVGRAAEDP SDPVRRAADA VAAVTTAVAA VAVAGRRAVV
LTRGARRTGP ADEVPATTHG PLHGLAPVLG LEFGAAFGGV VDLPWRPAPA DLDPALDLLA
APAGPVLEDL VAVRAGRILA ARLRDAGATP GRLPVRADAT YLVTGALGAV GRELVADLVR
RGARRLLLVG RRAESELDAG ARELLVRLRD DGIGVGYVGG GCDTADSRGQ VAAALRGMPP
LGGVLHAAGT IERVPAAELD SGRVAAALRA KVGGAWWLHE LTRDLPLDFF ILVSSVSALW
GTEGYAAYAA ANGGLDALAA YRRACGLPAV SIAYGPWAVS GMADGESRER FARIGVGALD
PATGCAVLRD EVPAPEGYLV ACPLDRQRLD SVLGGLRPRG LFASAPAGAS TAVAVASTVV
TVASTAVGVA SGAEREPSVA AELFALPVGA RPAAARGHVA RLLAAQLGHP EGHVIREDEG
FFDLGLDSIM AVDLARRLAE AFEVPLQVAD VFDHPTVHQF AAHLLALRDG PTNGTAPAVA
VGAGAADHAR GHAVDPTLNG GPAATEATAA LSIEAADHGV AATPIAVAPQ GGEQPAPVAA
VASPAEPAAI VGMAGRFPGA DTVEELWELL RSGRDAVDAV PPHRWSHRTF HAAGPDTGPR
ITTDQGGFLR DVARFDAAFF GIPTREAENL DPQQRLLLEC AWHALEDAGI DPSGLAGTRT
GVFVGVSNGD YARVLAGAGV DRLDAYYSTG TALNAVAGRL AYVLGLAGPA LAVDTACSSS
LVALHLAVRA LRAGEVDAAI VGGVNVIVDP LASVAVSRAH MLSPDGRCRT FSADANGFVR
AEGCGVVVLK RLADADRDGD AVLAVVRGSA VNQDGSSSGL TAPNGRAQEQ VITAALTDAG
VAGAAVDFLE AHGTGTSLGD PVEVGAAWRV LGPGRSPDRP LHLGSVKSNI GHCESAAGMA
SVIKTVLALR HGRIPANLHF TAPNPHIDWT GMDVRVVADE LPWPRTDRIR LAGVSGFGFT
GTNAHVLLAD PEPATTRHRH VDPADGTAPG GVPLLVPLSA PDPDGLRRLV DRWRDRVAAC
PEADLPALAA LAGSGRAHLP YRVALSGRDR ARLVAVAEPP ADPVAASRPP RIAFLFSGQG
SQFFGMGREL YETEPVFRAV FDECDRRLAP ALGRSLAELV FHGDDRTAIN DTRVTQPALV
TLEVALAELW RSWGVTPAVV MGHSVGEIAA AIVAGVLDLP AGLDLIAERA RLMQATRPGA
MLAVTATEQQ VRDLLAGTAL DVAAVNGPEA TVVSGLPEEI EALADRLRAD GVRHRALSVS
HAFHSRLLDP ALDEFRAVCA RLDHQPPTIP VISNLTGAVA GPDTYDADYW VRHARQPVRF
HTGAGRLAAL DVDVCLEIGP DRTLVNLVRA AGLAPGGGLA SSLRRGSADR AALLGAVAAL
YPLGQDVTWD RVQPRPRPGG RVEAPRYPFA ETRYWAPAAP AGEPAPAGAA ADAPAWGTPV
RSPALRGRVF HTERSTAYPP HLADHRLYGT VSVPGASQTA TVLSALAGDG TPPALADLVF
PRALVLHDGE RYELQVIEAE PEHGGRTVSV QSLVDPERNR WQEHLSARLL PDPPGEPRPV
PDLAAFQAAA ERHLAGTDFY QHFREMGYLL GPSFRWIDEV WIRGDEALVR YAQPDRMNEN
PAGWIIHPGL LDSCLQSTVT FGVAPHLTDG TAADAGRSGL AIPFAAARLI LARRPEHAGE
LWGHVRARHA TTGPDGGRQV HEADLHLFDG RGRTVLAVDG FRIRHAPREL LERSLRDTAV
HVHELTWTTP EPDRPAPAPT APARVAVLGG DGLPPLADAV AGRAELAAYP GEEPPDLVLD
LRFAAAEPQV SADAARQAVR RLVDDLRAAP ESVPYLVVCA DGAEAAPVRE ALWGMLAAVE
AEQPDRRLVR VVFAADADPG AAAGLLLDEV RRGLPETRLR IGGDGLQVAR LRPLPAAEAD
LPEAVTAGTA LVTGGLGALG LSVAGFLARQ GVPAITLVGR SAPDPAASAA IDQLTAGGTR
IRVVRGDVTD AEDCRRMVAE AERDGTIGSV WHLAGRTADG AFTQLTEAAF EEVFAGKAAG
ADRLLEAMAG RRPAALVHFS SVSAVLGSAG QANYAAANGY LAGLATRLRD RGLPAVSIDW
GPWTPRVKGG LAATEATRRA IDRLGVRALT DEEAETILRA ALTAGRDRLV AVAVDARAYV
ERAAGHPRAA LLLPLLDRGA RPAPVAAPAT PRGWLREELD RTAADEREDR LRAAVRRVAG
DALGDPGALD DEAGFADLGL DSIMVIDLRT RLSHALAADL PATVAIDHPT IAQVAAYAID
LLYPDDEPAG ESPRVDGWPA PAHDGPAHPG PAYPDAADDP AGTADDLADL SIDELVRAVR
ADLAMEE
//