ID A0A0E4H8D1_9BACL Unreviewed; 4177 AA.
AC A0A0E4H8D1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Amino acid adenylation domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PRIO_1736 {ECO:0000313|EMBL:CQR54131.1};
OS Paenibacillus riograndensis SBR5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus;
OC Paenibacillus sonchi group.
OX NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR54131.1, ECO:0000313|Proteomes:UP000033163};
RN [1] {ECO:0000313|Proteomes:UP000033163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg D.;
RL Submitted (MAR-2015) 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: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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DR EMBL; LN831776; CQR54131.1; -; Genomic_DNA.
DR RefSeq; WP_046501881.1; NZ_LN831776.1.
DR STRING; 483937.AMQ84_29515; -.
DR KEGG; pri:PRIO_1736; -.
DR PATRIC; fig|1073571.4.peg.1821; -.
DR HOGENOM; CLU_000022_0_0_9; -.
DR Proteomes; UP000033163; 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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05930; A_NRPS; 2.
DR CDD; cd17646; A_NRPS_AB3403-like; 1.
DR CDD; cd19531; LCL_NRPS-like; 2.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 3.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.980; -; 6.
DR Gene3D; 1.10.1200.10; ACP-like; 4.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 3.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 3.
DR InterPro; IPR010071; AA_adenyl_domain.
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; 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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 3.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 3.
DR Pfam; PF13193; AMP-binding_C; 2.
DR Pfam; PF00668; Condensation; 3.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 4.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 4.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 3.
DR SUPFAM; SSF47336; ACP-like; 4.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 6.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 3.
DR PROSITE; PS50075; CARRIER; 4.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 975..1050
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1076..1499
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1986..2061
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3025..3101
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 4064..4139
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 4139..4177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4156..4177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4177 AA; 469698 MW; EB87A331B2661D8D CRC64;
MKKLDANQVS DIISLSSMQE GMLFHYLKEP GSSLYFEQVS LHIASRVDLS AFEAAWQHVV
SSNEMLRAVF RWEGVKEPVQ IILKERSQFL QIIDVSSQGI GERSEFITKV MEDDRNSPFD
LTEGAFRVCL YQFAEADYHM IMSHHHILFD GWSTGIILNE FMESYQLFLN QQQPSAALKK
RYKEFIGLTR NKDKAEQERF WAGYLQEVHP VWLQDILPAS PSGQQAEGKK QLRLELPLFL
YEEIKQEGKY SVSCYLYTAW ALLQAFYTDS RDIVFGTTIS GREEALHGWE ETVGLFINTL
PLRLRIDPEE TFKGLLEKVF VSLNARKEYG STPLRDIKRY SGMPFEKELF DTILVIENYP
LQNNLNSRNM LIDSFSYREE TNYPLSIFIT LWNSIEIVVD YSSQMYSEAF IHEAAARYQL
ILSSLVQHPE APVASADFLF PEEQRKLLLE FANTEVMVPA DKTIHQLFEE QADREPDRIA
LHYAGQIYSY RQLNEQANQL ANFLTGKGIQ PNQLVGICMD RRPELLIAML GILKSGGAYV
PIDPILPEER IAAMVQDGQI EVIITVQKYT DALMGMNGKQ PVRQTLLCMD QDALQGHYGL
QDILRFPHEA GIHPSTPENL AYVIYTSGST GAPKGVMVSH GNVVNFIFGM DKRIGFRPDD
KVLALTTYSF DIFVLESLLP LCLGLNLVLA PDWVQKDPDA ILRLIEQESI DILQATPSRM
RMLVDSSLAG CLQQPGKILI GGEGFPEDLY QSLRKITDQQ IYNVYGPTET TVWSTVQELE
DTLSIGKPIA NTGIYILSKD KHLRPLGYPG ELCISGKGVA QGYLNQPGLT SDKFITNPYH
PGERLYCTGD YAYWLPDGRL QFVGRNDGQV KIRGHRIEIE GIEGTIKSYP AVKDAVVIEV
EEAGDAALAA YLVTGSGFVR EDFQAFLKSK LPYYAVPANL YPIGEIPYTS NLKVDRKALA
QMKTARMVPS GKLVEPRSKL ENEVAEIWKK VLKLESVGIF NRFFDIGGDS VKVIHLCNEL
KARLNMEIPV QTIFDYPTIH EFVSYCNETM TRTTGEARQQ PAEPKAFQPP ILDFQDTDVA
IIGMAGRFPG AADKEQFWSN LVSGKEAIKF YTDEELKALG MDSELLNNPK YVRAKGKLDD
SDCFDADFFG YTVAEAKWMD PQIRLLHECA WHALEDAGYE PESYPGAIGL YIGSSYNIYW
VPEKFSPSLY ASDQYQIYNM NSNSFATLIA YRMNLRGPAI TVQTACSTSL VAIDRAYKDL
LFGDCDIAVA GGAAVTLLDE MGYIHQEGMV LSKDGHCRAF EKKATGTVTG NGVGLVVLKR
LKNALADGDH IYSIIKSTAV NNDGNRKAGY SAPSAEGQAA VIQKAIQRSG IGSEQIHYIE
AHGTGTVLGD PVEIEGLKRA FNTSKKNYCG LGSVKTNIGH LEAAAGIAGL MKTSMSLQQR
MFPASLNCDE INARIVLEDS PFYVNTRLLD LRNEDNYPLR AGVSSFGQGG SNAHVILEEA
PQVDSGPAQR RFQIMTLSAK TELALNNLKG KVRESFRRSP GVHLADAAYT LKVGRKSFAH
RSAFLCTETK EAIDILTAKE TAKRWEAVVS EQAPSVVFMF SGQGAEYVNM ALDLYRHEPV
FRDKLSECLT ILQEISGLRY QDFLFPDGRE QQAERHIHRQ SVSQPLHFAL EYSLAWLLMN
WQVEPLSMIG YSIGEYVAAC LAGVFSLRDA LFLTYHRGVL MEKLPEGLMI TVPLQEADLL
QILPPVLSVA AVNDESCIVS GSKDSIAAFE ALLKSRKLIS MRLQISHAGH SKMLDSMISE
FRECVQRVTC NPPAVPFVSS LTGDVITPEE AASPEHWVRH LREPVRFAEG FKKLAPQENT
LFIEIGPGRN LCTLVQRFML PDRKQKLLDT IRVERKKAAD DEYLLRTVAQ LWVNGVSVDW
SRFYSGEQRR RVPLPGYPFE KKRYWLRDFR YGMGSPAVEA GAVQVPNDLP EAPVESEASR
VQAEPKAMSS EAAILAQMVA DIIGGTTIGE DDDLFERGFD SLKVISFISK TADAFRVQLT
MHEVFQNPTI RELLPVIQRQ APGQAVVIPK APEAACYPVS SQQKRLYALQ QFDEDSTAYN
IPGAFVLQGK LDRERVQAAC DGLIRRHEAL RTSFELNGQA LVQKIDPHAA LAIAYSDLPG
AGIEETLQGF VQPFRLDQAP LIRIRLVRVE NESHVLQIDM HHIISDGLSI ELLIRDFLAY
YEGRTLAEPR LQYKDYAVWQ QNRESAFWKE ERAFWLEQYK DGYELLNLPT DFRRPPIKQF
AGALRPFAWT EEISGPLQAF CQTHQITPYM LLLSCFTILL SKYSGQKEVL VGTPVGGRFG
VDTEDTVGAF VNTLALRSRP DGAKVVIDYL QEVREYCLHA FDHQGYPFEE LVQDIEKERD
VSRNPLFDTM FAWEQRDRSQ LHISGLQVQR YDFHSGIAKF DLMLQAWEEQ GEMGFSIEYA
TALFKDSTIQ RMGGHYQQIV RQVLQSPGRT IRELSLLGTE EAEQVQYGFN QTEAGYDLSQ
SIITLIEQQA EKRGDETAVV WEGQSLTYCE LNERANQVAR LLRDRGCQRD EIIGILAERS
PAMIIGLLGI EKAGCAYLPL DPDYPAERIG YLIQDSGLKL ILTQTAFADR VAALGVTAVN
VEEEAVYAGY ERDNVALDIL PHHLAYVLYT SGSTGKPKGV LLTHGGLVNR LRWMAEAYGM
DEREVVLQKT TYTFDVSVWE LFLPLMTGGV LCLAKPGGEK DPDYLVQLIR SQGITTLHFV
PSMLSGFVHA LPEHATMGQL KRCICSGEEL TLEVKERFFR RIEGVELHNL YGPTEATIDV
SFCEVHPADP LIPIGKPVAN TRLYIVSEEG GLVPVGIPGE LCIGGVQLAK GYLNRPELTA
EKFKTLPGLP EERLYFTGDL ARWREDGNIE YLGRKDTQIK LRGYRIELGE IESAIQKYDS
RIETAVVVSQ GAQAESKVLC AYFTARERIE TEALREYLRR ELPGYMVPVF YTQLDTLPHT
SSGKADRKAL AEAAVGHSRK EPVTEVISSK EGQMLENIFR ETLGCGNISP SDSFFELGGN
SLAAIVLKAR ISEAFHIHVT ILDIFANPTI RELLPVIQRQ APGQAVVIPK APEAACYPVS
SQQKRLYALQ QFDEDSTAYN IPGAFVLQGK LDRERVQAAC DGLIRRHEAL RTSFELNGQA
LVQKIDPHAA LAIAYSDLPG AGIEETLQGF VQPFRLDLAP LIRIRLVRVE NESHVLQIDM
HHIISDGLSI ELLIGDFLAY YEGRTLAEPR LQYKDYAVWQ QNRESAFWQE ERAFWLEQYK
DGYELLNLPT DFRRPPIKQF AGELRPFTWT EEISGPLQAF CQTHQITPYM LLLSCFTILL
AKYSGQQEVL VGTPVGGRFG VDTEDTVGAF VNTLALRSRP DGAKVVLDYL QEVREYCLHA
FDHQGYPFEE LVQDIEKERD VSRNPLFDTM FAWEQRDRSQ LHISGLQVQR YDFHNGIAKF
DLMLQAWEEQ GEMGFSIEYA TALFKDSTIQ RMGGHYQQIV RQVLQSPGRT IRELSLLGTE
EAEQVQYGFN QTEAGYDLSQ SIITLIEEQA RKRGDETAVV WEGQRLTYRE LNERANQVAR
LLRDQGCQRD EIIGILAERS PAMIIGLLGI EKAGCAYLPL DPDYPAERIG YLIADSGLKL
VLTQTAFASQ AAALGVTAVD VEEEAIYAGY ERDNVALDIL PHHLAYVLYT SGSTGKPKGV
LLTHGGLVNR LRWMAEAYEM DEREVVLQKT TYTFDVSVWE LFLPLMIGGV LCLAKPGGEK
DPDYLVQLIR SQGITTLHFV PSMLSGFVHA LPENASLGQL RRCICSGEEL TLEVKERFFR
RIEGVELHNL YGPTEATIDV SSCEVHPADP LIPIGKPVAN TRLYIVSEEG GLVPMGIQGE
LCIGGVQLAK GYLNRPELTA EKFRTLPGLP EERLYFTGDL ARWQEDGNIE YLGRKDTQIK
LRGYRIELGE IESAIQKYDS RIETAVVVSQ GAQTESKVLC AYFTARERIE TEALREYLRR
ELPSYMVPVF YTQLDTLPHT SSGKADRKAL SQMEVCIEKE RYVHPKTMLE KQMSQLWKEV
LHIDKVGLRD DFFQIGGDSL SVIILHQQVK QHVDAEISIA NLYRYRTIEA LLDYLSHKQN
SPARHTASNA GRRELLLQGN EKRAQRLSKR KGINRDE
//
