ID A0A285QVX4_9ACTN Unreviewed; 3079 AA.
AC A0A285QVX4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:SOB85539.1};
GN ORFNames=SAMN06272789_5827 {ECO:0000313|EMBL:SOB85539.1};
OS Streptomyces sp. 1331.2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938835 {ECO:0000313|EMBL:SOB85539.1, ECO:0000313|Proteomes:UP000219030};
RN [1] {ECO:0000313|Proteomes:UP000219030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1331.2 {ECO:0000313|Proteomes:UP000219030};
RA Varghese N., Submissions S.;
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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; OBMJ01000001; SOB85539.1; -; Genomic_DNA.
DR Proteomes; UP000219030; 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:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0046483; P:heterocycle metabolic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 1.10.287.490; Helix hairpin bin; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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 Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
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; 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 InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 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; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
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; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
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; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000219030};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1699..1773
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2766..2841
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 3079 AA; 334899 MW; A5D0AEED9C278460 CRC64;
MTSSPFAVPR EPIAITGIGC RLPGHANDHR TYWRNLIEGR DCLTETPADR YDTGTLGSRD
RAKRGRLIGG RGGYIDGFDT FDPEFFGISP REAEHMDPQQ RKLLEVSWEA LEDGGLRPGE
LAGREVGVYM GAFTLDWKIL QFADLDFATI AAHTATGTMM TMVSNRISHC FDFRGPSVSI
DTACSSSLVA VHLACQSLLR GETELALAGG ALLHMAPQYT IAETKGGFLS ADGRSRAFDA
SADGYVRAEG VGVVVLKRLS DAQRDGDPVH AVILGSGVNQ DGRTNGITVP SADAQVTLIE
RVCAEAGVAP GSLQYVEAHG TSTPVGDPIE AAALGRVLGI GRRSGDRCYV GSVKTNIGHT
EAAAGVAGLI KTALALKHRR IPPHLNLERP NPGIDLAALP FEIPTEPVDW PEHRGPARAG
VNSFGFGGTN AHVLLEEPPS PGPAAPVAEP VRTILPLSTK DAAGLPELAA AVRQELAAGA
SPADLGHTLA HRRQHLPERL AVTYSTRQDL DEALAACERG EDHPQVVRGR ARERRQRRLA
WVFTGMGPQW WGMGRGLYET EAVYREAVTA VDREIRAQAD WSLLEELGRD EADSRMAGTW
LAQPANFAVQ VGLSALWRSH GLRPDAVVGH STGEVAAFHE AGVYDLADAV RVVLARSRLQ
QRLAGTGSML AVGLPEAEAE RRIRPYRTRV SLGAVNSPSA VTLAGDTEAL AELAEELTAQ
GVFARLLDVE VPYHSVRMDP IRDDLVAALA GIKPQDARLP LYLTAREGLA KGPELDGEYW
WQNVRNPVRF RAAVERMAED GHALFLELGP HPVLGHAIRE CAGQAHTVAS IRRRQDETAC
FTRSLAELHT LGVELTWDAL HPGGRPAPLP GYPWRRDRYW VEPKPVEQVR LGQVDHPLLG
RRTPSAQPGW TTALDPERLP YLNDHRIEGQ IVFPAAGYLE MAAQAVRALT GGTEVVLAEV
ELNRALFLSE AEPATVQLGY APEDARFTIA STPPGGEPVV HAGGRVRTGQ RRSYGPALDV
ATPQAHGRHL DGPDCYRQLA ERGYHYGPAF QAVQEVWTGP GEALARIRAT DLLGPDAADH
HLHPVLLDAC FQTLLATTLH APEVGSVRLP VSIEEVRLDE IGARPLWARA TVTRDSGDEL
VGDIALHSED GTPIGRITGF RVADVAQAPA TVGLATIDGW LTEPAWVQAS EAPADRTPGD
LLLLADEGGL AERLAALAAE RGARCHLVRP GTEYRHEDGH STVRPDSAED VQQLLADLDP
GYATVVHLWN LDLPALGSTA PDRLGPLATH GAYSLIALAQ ALPAARPDGR LHIVTRGTQP
AAPGDRVEPL GAPAWGIGRV LWQQELVTQR GTLIDLDPAV DTPAQAEALL AELTARDEQE
IALRAGARLT SRLRQAEGLT RPLPPVLRPD GSYLVTGAFG ALGRLLCRTL VRRGARRLIL
VGRTPLPERS QWAHTDPQTP AGERIAFLRE LQALGAEPLL APVDVTDEAA LTAWLADYRE
RQLPPIRGVF HLAGQVKDTL LAQMDRSSFD AGYTPKVVGG HLLHRLLRDE PLDHFVLFAS
VASLLTTAGQ TNYAAGNAFL DALAHHRRAD GLPALSLDWG PWATGMIEEL GLVAHYRDAR
GMSSLPPDAG TAVLERVLGQ DRAQLLVATV VDWPTFLAWY PEPPPLVADL AADAAEQAPA
ETGGFLDAYR TADPQSRREL VTERFTAAAA AVLRTGAERI DADTRLGAHG LDSLLAMELR
ARVHGELGVA LPVVALLSNG TVGDLVDLLT EGLAERLADG GPARAEIELH TDESRYPLTH
NQQALWFLRQ LHPDGFAYNI GGAVEVRAVL DPELVFAAFR FLVARHPGLR AAFTAEEGRP
VQRIREEAVA DTGLFDVEGR PWEEIHELIV REYRRPYDLA EDPLVRLRLF RRGPDRWVLM
KAVHHIVSDA ISTFTFIEEL FEVYEALRQG RTPELPPVAA RYLDFLNHQN RFLAGPDAQR
MLDYWRGHLP AEMPVLALPT DKPRPAVQTH NGASEFFRLD DELTSRVHEL ARANGATPFM
VLLGAYYLLL HRWSGQPDIV VGSPVTGRTQ EEFASVYGYF VNPLPLHISL AGEPTVPELL
ARVRESVLGG LDNQEYPFPL LVEQLGLQHD PSRSAVFQAM FILLTHKVAV ERFGYRLEYI
ELPEEEGQFD LTLSAYEDRS DGCFHCVFKY NSDLFEPATV QRLAAHYRNL LDAMTRAAEG
EPVGRLRMLD AAERREILTA FSGAERRIDH DTPVPELIAK AAAEHPEAVA VVAPGREETR
RLTYGELDRL SQRTALRLRE LGVGEGSVVA VCLDKSPELI TTLLGIWRAG AAYLPLDPGH
PADRLAHQLA DVGATLVVVD ERRPLPADLP ATPVTLEELD RPAAATGPLP AADPDRAAYV
IHTSGSTGRP KGVRVDHRNL AAVTAGWRAE YRLDTEARTH LQMAGTAFDV FSGDLARALG
TGGTLVLVDR ELLFDTARLY RVMREEAVDC GEFVPAVARA LLAHCEREGL RLDFLRLLIV
GSDSWKAVEH QRLRALCGER TRLVNSYGLT EASVDSTYYE GPADSLEPGR MVPIGRPFPN
SALYILDPYG EPVPAGVPGE LWIGGAGVAA GYPNDPEQTA RRFVTLELDG TPVRLYRTGD
LGHWDTAGTA HLLGRIDNQV KVRGHRIEPG EIEAHLTARP ELAQACVAVR QDAAGEAVLA
AYVVPAEGTV LDRRELRRHL AEHLPTVMIP SYLTELPALP LTPNGKVDLA ALPEPKADTA
GAQHEPPVTL YEIRVAEHWR NLLGLDEVGL QHDFFELGGS SIRLIELIHH LQTEFNISIP
VGQLFKVTTL HGMARTVEQI ITGELAGGQP HLWFNPEATE GRTVFCFPPA GGHGLVYRQL
AAHLPEHRIA SFNYLTGDDK TARYADLVEE LHPDGPYVLL GYSLGGNLAF EVAKELERRG
RTVSSVLLVD AYRVRDAFDL GEEHVAVFER ELHEHLHRHT GSRIVAQETL EQARDYLEFC
SRTPNTGTVA AHLDVVCERE RLAVHVGGEE GSWHGASTTG TAVYAGHGSH AEMLDGEHAA
RNAELAGAIL AGGTVDGRD
//
