ID A0A1H6EQD8_9ACTN Unreviewed; 1216 AA.
AC A0A1H6EQD8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:SEH00067.1};
GN ORFNames=SAMN05444920_11546 {ECO:0000313|EMBL:SEH00067.1};
OS Nonomuraea solani.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1144553 {ECO:0000313|EMBL:SEH00067.1, ECO:0000313|Proteomes:UP000236732};
RN [1] {ECO:0000313|EMBL:SEH00067.1, ECO:0000313|Proteomes:UP000236732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7037 {ECO:0000313|EMBL:SEH00067.1,
RC ECO:0000313|Proteomes:UP000236732};
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; FNVT01000015; SEH00067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6EQD8; -.
DR OrthoDB; 3671989at2; -.
DR Proteomes; UP000236732; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic 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:0019752; P:carboxylic acid metabolic 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 GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd12117; A_NRPS_Srf_like; 1.
DR CDD; cd19543; DCL_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 1.
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 PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000236732}.
FT DOMAIN 878..952
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 676..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1216 AA; 130698 MW; F024065BBD775DD7 CRC64;
MSGRLADVLP LSPAQEGLLF HALYGGDDAY VVQARFAIDG QADPARLRAA LESLLDRHPN
LRACFRHKGL DRPVQLVPHR VRLPWTEVDP PSEAELERML EADRLRPFDV TRPPLVRATL
VGRRELVLTM HHLLVDGWSM PILAGELATL YAGDGVLPPA PAYKDYLTWL HAQDGERALA
EWRAALADLP GPTLVRPGAV AASLRQEVVE LELTRERSEA VRRRAREAGV TLNTLVQAAW
GQVLGRMTGR DDVVFGAVVS GRPPEVPGVE SMAGLFINAL PVRVRTGEPL SRLQDEQSRL
TPYHHVRLAD VQRGTGELFD TLLAFENYPR DGLSSPGIRL TDVHDATHYP LTVTVVAGER
LWLRLGHRAD LFTRAEAEAV AERLVTALES DELPPAESHR LLVTWNDTAR PETAGSVPER
FAAQAARTPD AVAVEHGGHA LTYAELDARS DRVAARLAIE PETPVAVLME RSPDLVVALL
AVLKAGGCYV PLDPGQPPAR LEWLLADSGA RVVLTSLDES GGPAFEGPPL RRDAAAYVMY
TSGSTGTPKG VVVTHANILE LAADRRFAGH RRVLLHSPHT FDAATYELWV PLLNGGTVVV
APPGPLRPDT IAGARLSAVW LTAELFRALT DLAPDALATV PEVWAGGDVL APDTVRRAAR
HGVQVVNGYG PTETTTFATS HRVGPEPGTG SVPIGRPLDN TRVYVLDPRL RPAPAGTVGE
LYVAGTGLAR GYLGRPGPTA ERFVADPFGG PGERMYRTGD LARWTFDGEL EFAGRADGQV
KIRGYRIEPG EVEAALESCP DVRRAVVITA SLGGAVRLVA YVVTDAIERV REQAAARLPQ
HLLPARYIPL DRLPLTAHGK VDRAALPAPE APSVTVTEPA TPREKELCGL FAQVLGGEAG
ADTDFFDAGG DSLLAMRLTA AIEAEIGIRT SIAALFEAPT PAKLAVRLDR TAPELDLSPL
LTLRAEGDRA PLFCVHPGRG IGWSYTALLP HLTPGRPVYA LQSPVLQAGV HTLPGGMREL
AEEYLARVRA VRPDGPYLLL GHSFGGLLAY EMAARLREDG QEVGLVASLD AVPWPPGFEA
EPAGLEQEAL TILLRTRTLH PYAQPGPLER ARVFAAVRDS EGPLSGMDDA GLSAVADTVA
GHLRLAVTYR PPPYDGTVLL FSATAQPGGL GSAVKTERWS PARVRVHELD CGHSDLLRPG
SAAEIAGVLE PILREW
//