ID I4MYN7_9PSED Unreviewed; 1010 AA.
AC I4MYN7;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Non-ribosomal peptide synthetase modules, amino acid adenylation, pyoverdine {ECO:0000313|EMBL:EIK94327.1};
GN ORFNames=PMM47T1_22298 {ECO:0000313|EMBL:EIK94327.1};
OS Pseudomonas sp. M47T1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK94327.1, ECO:0000313|Proteomes:UP000004339};
RN [1] {ECO:0000313|EMBL:EIK94327.1, ECO:0000313|Proteomes:UP000004339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M47T1 {ECO:0000313|EMBL:EIK94327.1,
RC ECO:0000313|Proteomes:UP000004339};
RX PubMed=22887683; DOI=10.1128/JB.01116-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL J. Bacteriol. 194:4789-4790(2012).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
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:EIK94327.1}.
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DR EMBL; AJWX01000025; EIK94327.1; -; Genomic_DNA.
DR RefSeq; WP_008373228.1; NZ_AJWX01000025.1.
DR AlphaFoldDB; I4MYN7; -.
DR STRING; 1179778.PMM47T1_22298; -.
DR PATRIC; fig|1179778.3.peg.4442; -.
DR eggNOG; COG1020; Bacteria.
DR OrthoDB; 9757559at2; -.
DR Proteomes; UP000004339; 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:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
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 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; 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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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; 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 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:UP000004339}.
FT DOMAIN 904..979
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1010 AA; 109019 MW; 5004AF7C43072B47 CRC64;
MTEVMELEHL ALSPEQRAVQ DTQVLHLWLG SAQAQDAQAL RHGFEQAVRG QWSLNCRFSH
HAGYRGLRQQ PLQEPAAGRW QFVDLRGDSN RQAALDSEVP AFELASGDGV AARLFAVGDS
DWRLHLSASA LVADHASLRL LARLMVGGAA GVDEESGHFG QFVEWRQAMA EDEDAPAGQA
YWAAHLRQAS ADQALQLPLR RLQGQPGQDH AVSALSVEQA HSLNALAESR QVRLDTLLQA
AWWALLARIG GQSQVLAGWL HDCRDDYDFF AASTGVYEKT LPLVLNIDSQ QGFARWLADC
SVLLDSHRGW QEHAPAQVPE ACLRAGFSVE TAAPAGWQAL RPRTWAFELG LQVQQGSHGQ
VAGLGVYTHA QHYRAGDAQG VLNQYLQLLE RLPDGIEQSI ERLLEPAADV ARLQGPSRPF
AESSPLARIA HWARETPQAA ALQSGVQVLD YFALNQRVEQ MAASLRGVGA GADTIVALAL
PRSAELVIAA LAVMRSGAAY LPLDPQWPQG RRQQLADTAQ PLLVVGEGAA LEGHRQLDWQ
AWLAEPATAL ELPLPAPEQA AYVLFTSGST GQPKGVVIEH RQLNNYVQAV SQALELNQCR
RFALTSTVAA DLGNTCLFGA FEQGACLVIA SAEDMQDAPS FARFLGANQV DCLKMVPSHL
AALLDDQPGA LPATVVLGGE ATPLALAERI RRQSPGTRLF NHYGPTEATV GVLCQRVDDD
AQALGTVLAN NVVVLLDDDR RRVPAGAVGE LYLGGAQLCR GYVQVDQSAF IDDPDSPGQR
LYRTGDRAVR RHNGSLELRG RADGQVKIRG FRVELGEVEC TLQGLAEAAV KVIADAEGVL
SLVAYVVCDE AGLAVLRQQV DNRLPEAMRP SRYMRLPSLP RLANGKIDRQ ALPEVQPDIP
AGRAPRDALE TLLAGHMAEL LGRESLDIDS DFFQAGGHSL TVIKLVAAIR KGLQLEVAPG
IVFDHPSVAS LAAALRERES APGQLEKAAG LRLKLAALSP AQREALLARR
//
