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Database: UniProt
Entry: A0A1X7FEU9_9ACTN
LinkDB: A0A1X7FEU9_9ACTN
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ID   A0A1X7FEU9_9ACTN        Unreviewed;      1415 AA.
AC   A0A1X7FEU9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Nonribosomal peptide synthetase MxcG {ECO:0000313|EMBL:SMF50921.1};
GN   ORFNames=SAMN02745830_04072 {ECO:0000313|EMBL:SMF50921.1};
OS   Streptomyces sp. Amel2xC10.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1305826 {ECO:0000313|EMBL:SMF50921.1, ECO:0000313|Proteomes:UP000192930};
RN   [1] {ECO:0000313|EMBL:SMF50921.1, ECO:0000313|Proteomes:UP000192930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Amel2xC10 {ECO:0000313|EMBL:SMF50921.1,
RC   ECO:0000313|Proteomes:UP000192930};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FWZW01000008; SMF50921.1; -; Genomic_DNA.
DR   OrthoDB; 2472181at2; -.
DR   Proteomes; UP000192930; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR   GO; GO:0008610; P:lipid 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   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd05235; SDR_e1; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.50.12780; 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   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; IPR042099; ANL_N_sf.
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; IPR010080; Thioester_reductase-like_dom.
DR   NCBIfam; TIGR01746; Thioester-redct; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 2.
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.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192930}.
FT   DOMAIN          916..991
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1003..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1384..1415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1389..1415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1415 AA;  151628 MW;  CCAD75BB76B2B2C3 CRC64;
     MNRPLLAAQE GIWAGQQLDT GSPAYNTAEY LRITGPLDPA VFDRALHHVV AETEALNVTF
     HTDDTGRPRQ ITTPADAWRT HIADLTAEPD PHAAALAWMD QDMARPVDLT RGPVFGHALL
     RTAPREFLWY HRVHHIALDG FGLSLVARRV AEVYTALMAG EPVPEGGFGT LDAVLAEERA
     YRDSARHTAD RAYWTDRYAD DPPVVTPAGR SALPARTFHR QVTDLAPAAV RQLRTLAADM
     TVTWSEVLLA VTVARLHRLT RAPEIVLGLP VTGRLGSAAL RVPATVRNIL PLRVPVTPDD
     SLRVLAHRVA RELRSALPHQ RYRYEQLRRD LKRVGGGRRL SGTAVNIMPF AYDLTFAGHP
     STVHNVSAGP VDDLAVNVYD RGDGTGLRVA VDANPELYTQ TETAAFRDGL LGLLTEALAD
     PDSPLGEPRA PRAVTVLDGG PLPAPARPVL SLIADHAAHR GSAVAVEHAG NTLTYAQLCD
     AAADIARGLA ARGVGRGDVV AVDLPRGADA VTTVLGVLMS GAAYRPVDSS TARLAADVAD
     HTVFPLHGRP FASADTLTPP GPTDLAYVLH TSGSTGRPKG VAVGHAALAH FVAAATHRYG
     LRREDRVLHF APLHFDTSVE EIFLTLCAGA TLVIRTDDMT ESVPRFLDAC ARSRITVLDL
     PTAYWHEVAY AVSTGAATLP RDVRTVVIGG EPALPERVER WRAAVGTSIA LLNTYGPTEA
     TVVATVADLH DPGLAAGDVP IGLPLPGTSA AVVDGELYLL GPTLADGYRP EVPDSVRFAP
     LTALPDGPRA YRTGDLVRIG EDGRLRHLGR ADSEFKISGH RVQPAEVESA LLTHPRIREA
     AVAGQVLPDG TRRLVAHVVA PAPVPSPAEV REHLRARVPA VLIPSAVEFV DRLPRTGTGK
     IDRAALTEPR PRRTPSAGSP LERTVTGIWR AILGTDTVAV DDDVFDLGAQ SLQVIQAANR
     LGVALGRDVK VAWLFQHPTA AALAGFLTDG GADDGPSPAA FLTDSRLDPG IRPGPGRAPR
     PASAPRRILL TGATGFVGTH LLARLLADTE AEIVCTVRAP GVTAADARLR EALRHHGITL
     DDSASARLTA LPADLALPDL GLPQGTSAEL AATCDAIFHN AASVSILRDY ATLRAANTES
     TRQLLRLAAV NSTPLHYIST LSVAPPVGRR PEVPEAFLPP HGQLRHGYQQ SKWASERLLE
     QAAERGLPVT VHRLGRVVGP ARTGHVNERD FLWSVLRAGI PEGIVPQLFE DEVWTPVDFV
     AGCVVHLSLH TDPRSTGPVF NHATLPRVRL ADVYDWVREY GYPVRPLPPR HWRARMPRTS
     DAAATTLAFL DSTDTDTDTD TDLTLGRIRA DRVRTALEGT GITCPPIDRA LFFRSLDHCV
     RAGTLPAPSR PRTTAQQPGT HGHFAPTTAT EHISK
//
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