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Database: UniProt
Entry: A0A318JHV7_9BURK
LinkDB: A0A318JHV7_9BURK
Original site: A0A318JHV7_9BURK 
ID   A0A318JHV7_9BURK        Unreviewed;      4271 AA.
AC   A0A318JHV7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:PXX46802.1};
GN   ORFNames=DFR42_101378 {ECO:0000313|EMBL:PXX46802.1};
OS   Undibacterium pigrum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Undibacterium.
OX   NCBI_TaxID=401470 {ECO:0000313|EMBL:PXX46802.1, ECO:0000313|Proteomes:UP000247792};
RN   [1] {ECO:0000313|EMBL:PXX46802.1, ECO:0000313|Proteomes:UP000247792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19792 {ECO:0000313|EMBL:PXX46802.1,
RC   ECO:0000313|Proteomes:UP000247792};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-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   -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC       family. {ECO:0000256|ARBA:ARBA00029443}.
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:PXX46802.1}.
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DR   EMBL; QJKB01000001; PXX46802.1; -; Genomic_DNA.
DR   Proteomes; UP000247792; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0018130; P:heterocycle biosynthetic 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:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd19535; Cyc_NRPS; 2.
DR   CDD; cd05931; FAAL; 1.
DR   CDD; cd05274; KR_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 4.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
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; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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; 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; IPR040097; FAAL/FAAC.
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; IPR013217; Methyltransf_12.
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; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
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; 2.
DR   Pfam; PF00668; Condensation; 2.
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; PF08242; Methyltransf_12; 1.
DR   Pfam; PF00550; PP-binding; 4.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 4.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 4.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 2.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        254..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          658..733
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          767..1186
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2151..2225
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          3605..3680
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          4159..4235
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          4236..4271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4236..4265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   4271 AA;  465453 MW;  F68881A03C17025A CRC64;
     MLMRKAYKRT GKQGQFPPCQ LILRETMTNT PAISLSQHPT LVDWIEHHAQ HQPDAEALCF
     IGQRTGSTDT SADVRLTYAA LSRRVRNCAA SLQACTNPGD SALILFPSGI DYVVALLACF
     YAGVTGVPVN LPGAARVKRV LPKLGDITRD CSPALIISNQ QVTDASGSDL QAFANEHGLR
     LLQLEEMQEE NSQTWQRPVI NGAALAFLQY TSGSTGQPKG VINRHGPLLH NLEFLGRLTA
     VNTRQASDTV IASWLPLFHD LGLIMGILLP LAYGGRAVYM APMAFAADPL RWLELATRER
     ATALPCPSFA LRLCTDEAKT AALRLKDINL ASVTCLMPAA EPVLPAQIES FYTTFAANGL
     RRTAIKPAYG LAEATLLVTA HVDDHDPYFI DVDKAKLERG YAVVNPAHNE NTNTGMRRYT
     SNGNDFGGQD VRIVDPDTHA ALAEDQVGEI WINGPAVAGG YWNKPELNRD IFSACIASIN
     INEEDCKPYL RTGDMGFMHE GHLFVTGRLK DMLLFRGQCH YPNDIEVTSG RSHAAAVPES
     GAAFSITLRD EQTEHLVIVQ EVLKQTGGSY QHIVDTIRAS VAEEHQLSSH AIVLIRKGTL
     PRTTSGKVRR ATVRQAYLDG SLPVLHQHVL DAQQITEAPA DTALLDTLRP LSLAQRHQHL
     RNWLANEAAT ILGTVTARAI HPEASLFNYG LDSMSAARMV ASAAKSLGMS LPDNVIFDHP
     SLTELAVHLQ TVLVTQARLP LAADNSSSVS ATPDRDTGKA VPASTDKEAI AVIGMAFRLP
     GQDGQDANSD ETFWDMLEQG GCAIRPAPSE RFRTREDIPG FGAYLNHVDQ FDAAFFGMSP
     REAMNTDPQQ RLLLEVAWHA LEDAGQRPAA LRGSDTGVFV GIGTGDYGHL PFISGEPSHF
     DAYWGTGTSF AAACGRLSFS FGWEGPSMAV DTACSASHSA LHLAVQSLRA RESGLSLAAG
     VKLQLLPEVD LVLHKAGMLA LDGRCKTLDA RADGYVRGEG CVVLVLKRLS DALADGDVIR
     AVIRDTMVRQ DGAGSSLSAP NGAAQQRLLS LALKKAGLTP TDIDYIELHG TGTRLGDPIE
     YQSVADVFRG RDLDDPLWLG SVKTNIGHLE AAAGAAGLVK TILAIEHGKL PPAVELQEVN
     PLIDLDIIPA RVPAQTINWP MRQALRRAGV TSYGFAGTIA HVLLEQAPVM ASGKTSEKIT
     APQLFLLSAR SAESLRMLAS SHAENLAGCD NLPALARGMA RQREHHNLRA AVLASSFEEL
     ASGLQQLIAP GYTATEAIRN PRIGFLFTGQ GSQYSGMARE LYAQQRDFRQ ALDAVDAALA
     ADLGMSVITL MHDDAQNERL QQTAFAQPAL FALGYALAKM WQAFGVQPII VLGHSIGEFA
     AMVIAGSLTL EQAARLIVKR GALMQALPAG GAMLAARSTP EQALAVLAEL QADHGDEIAI
     AAFNGPQDVV FSGSVAAIEA VQALLTAQQL YARPLQVSHA FHSPLLDPML AAWESECARY
     VMQAPRIAVC SSLTGELLTQ APDASYWKNH ARQPVRFDQA LQNAASACDI LLEIGPNAIL
     SAVAQRNQAA QDWPHAVNCL ASLRRGGSDL VAIGDACAAL YVAGQDFHWD HVFAGSLPSP
     RILPRYPFER QSYWLDYDDD APRLPLQLQP QPERAAAKPV DLYIMQWESF TLAENGTHAS
     RYFLLGGDLT HTATLAAGLA ATGASTYSLT AGEWPLTATQ LEDSDVVIYL DGWHAQVECA
     ALADQQGWQL TEFVKVLQHL QKKPRILLPT NAGQAIAGTS GNPLQASLWG AARALALEYP
     GPRWLMADSD AGLLPFASAL PALLPLFGNE EAVALRNGLW LHPRLEPVSA QAHEVAEPPA
     LKRDGIYLVA GAYGALGRHA TDWLASRGAR HLVLLARRSA PSGWQARMDL LKAQGIQITH
     IDADVADADD MARVFANITS MEQDSGLSLA GVFHCAGTSR FNDLATITNE DYQTVSRAKI
     QGAWLLHEHT RSRELDYFVC FTSISGIWGS RLQIPYGAAN AYQDALARMR RHQGLPALAI
     AWGPWGGGAG MSEVDEDLLQ LLRAAGIRRL APARYLATLD KLLSGEYITD NGTCVAVDVD
     WQQFVPLYAL YNPANTFERC LSASQANTIA VSATADTPSA LHDLDEQARQ AAVHAFVIAE
     LARTLRVTPA QLTPDIQLLK LGMDSILVMD FSRRCEAGLG VKCELKAIFE RNTPQGLTDY
     LLEQLGKQLP DSQPQKEAEQ IIADPANANT PFPLTELQHA YWIGRHSHYG LGGVACHAYL
     EADAPKGLDL DLLERCWNML VARHGALRLV IAEDGQQRVL PKVPDYVLRV ADLTDADQTT
     ADAHCTAWRE TMSHQVMDAA QWPLFDLRAS RLPGGAVRLH IGIDMLINDA TSGQIIWEEL
     AALYQAKADM QLAGLLPFQI SFRDYVLAKY VHSKQRHTER ESAKAFWLER IPVLPPAPQL
     PLRAEALRQT SPTFSRRQQQ LAAPLWQSLR DQAAQAGCTP ASLLITVFAE VLAAWSAEPQ
     FTLNLTIFDR LPWHADVPRL LGDFTAVTLL PLDCSEALPF GQRAAAVNGT VLEHLQHRAF
     SAVDVMREWN RGRERQDAIA MPVVFTSQLG MNDPTKGAAP DSALGNVVYG ISQTPQVWLD
     HQACELDGAL IYNWDAVDAL FQPGTLDAMF NAYHGLLEKL ATQPQSWQEA LPVLLPPSQQ
     AIRAQVNASA APMSDFCLDQ LFFEQAQSSP QAIAMIAHEQ QWSYAELADW SLRLTNALLQ
     YGAKRSDRVA VVMRKGPEQI AACLGILAAS CVYVPVDADV PAARLQAILD GSHIKLVLTQ
     ADCLPIVQEM CAGREVTVLD ASQAATQTWP ASLQQVERAV PDHAYVIYTS GSTGIPKGVL
     IDHRGAVNTV LDINRRFDIG HTDRVLGLSS LYFDLSVYDL FGIFAAGAAL VLPAASGTRD
     PAHWLDLLLR HRVTVWNSVP ALLELLLDEA EAAGASLAGL RQVFLSGDWI ALGLPARLRT
     QAPQARLVAM GGATEASIWS NWFIVPEVLP TQWRSIPYGY PLANQHYRVL DTRLRDCPDH
     VSGDLYIGGT GLAIAYENDA AKTAASFITH PVHGERLYRT GDLARYWCDG TLEFLGRRDF
     QVKIAGNRIE LGEIESALLS HPGVREAVAD AVGPARGNKR LAAWVVPNAA DTSLYDAFSG
     NPVLNNDRWV AVEQAGSQTF AQTYSTQQTE RLEQFWSLMD HIGLCMMRDT LLAAGATSGD
     HGQILQMLAP APDLVVLAQR WLNTLDLNAQ YDSESAWNNL TPTALDFGLS RAVLQRLRSG
     ATQRLEVLRG QVSALEVFYG ADDTLAPEQM TRMNPLSSLC TSALAAAIRS LTQHLGRPLR
     ILEIGARSGA ATRDLLAQLS DCAIDYTLTD PARSLVEQAE QAFAIQDSNP LHSIHCRVFE
     HERAAATQGV PEYEFDLLIA FNALHRSRNI PALLHRLRSL LNAGGMLIAP EITRNSDFQL
     ATVALLEGGY TQFEDRRKLN GNALLAADAW LDELVQAGFV ASAESGIGSN AGMHLLAARQ
     KDTVLRFAPR RLVEHLTTLL PAYMVPQTIL ELDALPLSAT GKVMRQQLPR PEMGGSRRIS
     RQAGNDAMPP ANDLVRIWQE LLGVADLHGD DDFFDLGGDS LIAVRLIERV RHGMNAHVAL
     SDLFDASSLS AFAERVAKAS PYEDSLPPLL PDVAARYAPF PLTDVQQAYW IGRDESFELG
     GVSTHLYAEI EVENLALADL ERGWQQVVTR HDMLRAVINA DGMQQVVQDL PAYHLASHDL
     RAASASEVSE WLEITRLELS HEVFDTARWP LFTVRAAQMT DSRVRLFVSL DNLVCDGRSM
     RTLLAEWSQF ARNPALQLPP LTASFRDYVM LTQQIELLPS YQRSLAYWHD KLSTLAPAPA
     LPLTQYAPED VSPPHFTRRE ASLTAQDTLA LQAQAAAHGV TVNAVLLAAY GEVLANWSAI
     PRFTLNLTLF NRPPVHQEID ALVGDFTSLV LLGFDAGITA SFAERAFSMQ RQIWADLEHM
     QVSAVRVLRE AARRNRRLNQ VAMPIVFTSG LGVASDGAAE LDWLGEFVYG ISQTPQVWID
     QQVVERDGAM VFNWDSVDAL FPEGLLDEMF QAYHGLLLNL AQDSDAWQSR VAMPVNRWPA
     STFKSVGDVS TATLPNTSPV IDDKLLRMVS NRLAALLGHD ELAPQTNFFE LGATSLDLIR
     LRQQLQADTG LVLSITEVFQ HTSIAALAAH LRSRDQSLES EDISSDEAGQ ARKRQRLDND
     RRRKRGQQSK A
//
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