ID   A0A1I1W5X7_9BURK        Unreviewed;      1441 AA.
AC   A0A1I1W5X7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Amino acid adenylation domain-containing protein/thioester reductase domain-containing protein {ECO:0000313|EMBL:SFD90409.1};
GN   ORFNames=SAMN04489710_108136 {ECO:0000313|EMBL:SFD90409.1};
OS   Paracidovorax konjaci.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=32040 {ECO:0000313|EMBL:SFD90409.1, ECO:0000313|Proteomes:UP000199517};
RN   [1] {ECO:0000313|EMBL:SFD90409.1, ECO:0000313|Proteomes:UP000199517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7481 {ECO:0000313|EMBL:SFD90409.1,
RC   ECO:0000313|Proteomes:UP000199517};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; FOMQ01000008; SFD90409.1; -; Genomic_DNA.
DR   STRING; 32040.SAMN04489710_108136; -.
DR   OrthoDB; 6297021at2; -.
DR   Proteomes; UP000199517; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd17646; A_NRPS_AB3403-like; 1.
DR   CDD; cd05235; SDR_e1; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
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; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR01746; Thioester-redct; 1.
DR   PANTHER; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR   PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          967..1042
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1441 AA;  157703 MW;  208D811371E0EB34 CRC64;
     MRAIPLPAHR FELTSAQMGM WLGTRFASRD TNFNLAEAID IRGPFSPDRF LQALQSLCRE
     ADTIRLRVAD TPEGPRQWID PEFSGSVPVL DFRGEADPEA AAEQWMAQDC ARQVDVVQGP
     LWFSALLQLG PERHIWYQRG HHFAFDGFAG VVLARRAADL YTALVEGTPP PAASELAPLS
     ALIDEDRAYR GSERARRDRE YWMERFQDRP APLSLADRRS ANVGGLLRST AHWPAAQVAA
     ARGTAQQHGG TFPQFLIAAT AAYLYRMTGV SDLVIGVPVT ARYNDRMRRA PGMVANALPL
     RLAMRPDLLF IDLLREVGRQ MRQVLRHQAY RYEHLREDLE LLANNQQLFT TVINVEPFDY
     DLRFGDCPAA FRNLTNGTAQ DLGIFMYECG NGQDLQIDFD ANPALYTGPE LAAHQRRLLG
     LLDRLAHEPA QAIGRLDVLP PHERQTLLSG WNDTAHAQPE AHLAQLIDEG LSRDAGAVAL
     RFEGRSMTRA ELDLRAAAWA RRLTAMGAGP KRIVALAIPR SLELVVALVA VLRSGAAYLP
     IDPDFPPDRL AFMLEDAQPV CLMTCGELSE RFDARIPRFI TDGPEAEGVA EAPLRTGLQP
     SHPAYVIYTS GSTGQPKGVV VPHSAIANRL RWMQAEYALQ ADDRVLQKTP SSFDVSVWEF
     FWPLISGATL VVARPGGHRD TGYLAGLIAQ EAVTTVHFVP SMLDVFLRDP AAAACTTLRR
     VICSGEALPA PLAAQFHQTF DCGLHNLYGP TEAAVDVTAW ACGPQDGAGL ARIPIGRPIW
     NTQMYVLDPG LQPLPVGVTG ELYIAGDGLA RGYLNRPVLT AERFIANPHG PAGSRMYRTG
     DLARWRADGS LDFLGRSDHQ VKIRGLRIEP GEIEATLLRH PAVLQAAVVV HEDAHAGKLL
     VAYYVPADGA PLDSFALKAH VAQHVPDYMV PSAFVALDSL PLGPTGKLDR RALPAPLAPT
     ARNTYTAPRS AAEQTLAELW ARALKVEQVG IHDNFFELGG HSLMAIQLGM QVRERLHPEF
     PPAELYNRPT IAELAAWIEN NGGERPPVDL QAETVLPDHI RGREGAAPPV TAQRVFLTGA
     SGFVGSYLLA TLLRETTASV VCHVRAADEA AGARKIRRAL EERHLADAWD GARVEVVTGD
     LGAPQLGVTD EAMQRICGEC DAIYHCAAQV DYLHPYESLK PSNVDSVVTL LEWTQRGRPK
     VMHYVSTLGV IGLDPETPVV TEQAPLATPA GLVGGYAQSK WVADRLARAA QARGLPVAIY
     RLGSITGDNV HAACNQADVF WRVAQLYVDL EMYPDLDLPL NLTPVDDVAR AVVRLSRQQE
     SWGRIFHLLG SEPLHVGDVR DVFQQIGRPL QPTDLDTWLH HAHMRLAMTQ DQDLAALLAI
     LGAYDTDAVP PILCGAATQA RLQALGAPIQ SVDRQLLRRY FENLGFGVTE TAGQRPAAAL
     A
//