ID   A0A1G8UQ33_9SPHI        Unreviewed;      1740 AA.
AC   A0A1G8UQ33;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:SDJ55952.1};
GN   ORFNames=SAMN04487898_103254 {ECO:0000313|EMBL:SDJ55952.1};
OS   Pedobacter sp. ok626.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1761882 {ECO:0000313|EMBL:SDJ55952.1, ECO:0000313|Proteomes:UP000198594};
RN   [1] {ECO:0000313|EMBL:SDJ55952.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK626 {ECO:0000313|EMBL:SDJ55952.1};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNEX01000003; SDJ55952.1; -; Genomic_DNA.
DR   STRING; 1761882.SAMN04487898_103254; -.
DR   Proteomes; UP000198594; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0043604; P:amide 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; cd19531; LCL_NRPS-like; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020459; AMP-binding.
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; IPR013217; Methyltransf_12.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR001031; Thioesterase.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   PRINTS; PR00154; AMPBINDING.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          1395..1470
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1740 AA;  197860 MW;  2523DA475EAA66C2 CRC64;
     MSNYTLTPIN FNPFEEEKEI DKIVFTNEPQ KEIWLSCIIG GDASNLAYNE SVSIDFNGMF
     YPEHFLEAIK KVVQRHEALR ATISANGETL IIYKNIPFEI SVEDISTQVD QKSILDTFIA
     DQMQYVFDLQ EGPLFKSYLH KLNETHYFFT IVKHHIIGDG WSTGVILEDL SKLYNAKVRD
     ENLSLPPAPQ ISKYAKEMAA FKFSPAYQLT QDYWLNMYKN EVPILDLPTD FPRPALRTYN
     AHRIDSNLPL ALISQLKEMG ARAGCSLVNT LLSAFEVFLY LQTNQDDIVV GLPAAGQSAT
     GDFGLVGHCV NLLPLRSIID TNSTFKTYLK NRKSAFFDAY EHQQFTYGQL VKQLNLKRDH
     SRIPLVPVVF NIDMGMDNLV DFDHLNYQLI SNPRAYETFE IFLNATGSKT AFTFEWSYNT
     QLFKPETIAR MAREFELLLQ MIVKDPDVII KEIALGNTGI WKEQLAIWNN TYSDYPKDEP
     FMSLIDKYEL ESPQKTAVVY KNESLNYIDL IEQSNQLANY LIDKGIKVGD IIALASDRSI
     DMLICLLGIL KSGAVYVPLD PEYPQDRIEF MLSDSNAKFL MVSRAYAGKF KSIASELVIE
     DLHNEVKHCP KKLRTVQVTG EDLAYILYTS GSTGKPKGVQ IKHHNLMNFL ISMQSEPGIT
     QDDRLLAITT ISFDIAGLEL YLPLISGAEL FICDTETARD GRLLLDLIKS ENITFMQATP
     STWRMMIDSG WTKSPLLKVL CGGEALPKEL AEILVDKSAE LWNMYGPTET TIWSTIKKIQ
     KENLVLTIGH PIQNTQIYIL NEENNLLAPG ITGEIFIGGE GVAAGYLNRI ELTKERFITD
     TFGHNPDGKL YKTGDLGKFL ENGEILYQGR IDQQIKIRGH RIELGEIETL LAEQKEIKQA
     VVIAKEDNLD HKRLVAYVIL VNHESTNNTP SWKDRWDTIY DMAAKSAENS APSDKKIDGI
     LLEQWENSED LVKQAAEWLQ VSADRIKALN AKHILEIGSG GGQLLFELAP NCESYMATDY
     AETAIEELKQ KLAAAPEKWK HVAANANAAD DFSKLIGASF DLILIHSVAQ YFPDTAYFLK
     VIEESVKRLS AGGCLFIGDM QGKNSLTMYH AMDHLSHAKN ETTLSEFKEV VNNRVRIEDE
     FVADPGFFYL LPKLLPNITG VDVQLRKGQS QNETTKYHYD VWIYVNSEHT TTKPDHRLLW
     EELKSIDLLE QQLQTHQGQI IEVRDIFNER TIKDYALVNW MSSADDHSTL LEIKKELQEP
     GKTGVNPDLF WRLGQQYGYH SHVRWSTDGT DGNFDIVFIP DNLPMALPEP PSLELLRELK
     PSDFARTPLS TNEVFLSKSM TEHIKDSLRK NLPDYMIPGD FVALKAFPLT PNHKIDKNAL
     PQPQSRLTQY DQVDEKLNEH EKIILDIWAS TLGLENIHIK DDFFELGGHS LLAVKVMAAI
     EKETGKRLPL ATLFENSTIE SLAKKIQTNA SEKWQALVPI RTKGTKDPIF LIHGGGLNVL
     LFKTIGEYLD EDQPVYGIQA LGLNHEMEIP NDLTEIAAHY VSEILKVNPN GPYLIAGYSL
     GGFIAFEIAK QLSEMGKIIK LLGVMDTYAG NQVHEDSTYN RILRKVKRQF FKIPVLIKSF
     IEFPKESFSY QQKLIKFKIR KIFIPDATIE ESIFTDYEKA IYKQYDRAHN NYKLTPFDVK
     ITLFRAKKRL YYLDDMVYLG WSEYAKKGID IYEVPGDHKT FLLPPMDKEF AMILQKALNS
//