ID A3JMY8_9RHOB Unreviewed; 1513 AA.
AC A3JMY8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:EBA05086.1};
GN ORFNames=RB2150_13391 {ECO:0000313|EMBL:EBA05086.1};
OS Rhodobacteraceae bacterium HTCC2150.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA05086.1, ECO:0000313|Proteomes:UP000004731};
RN [1] {ECO:0000313|EMBL:EBA05086.1, ECO:0000313|Proteomes:UP000004731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA05086.1,
RC ECO:0000313|Proteomes:UP000004731};
RX PubMed=20889754; DOI=10.1128/JB.01088-10;
RA Kang I., Oh H.M., Vergin K.L., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of the marine alphaproteobacterium HTCC2150, assigned to
RT the Roseobacter clade.";
RL J. Bacteriol. 192:6315-6316(2010).
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:EBA05086.1}.
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DR EMBL; AAXZ01000001; EBA05086.1; -; Genomic_DNA.
DR eggNOG; COG0223; Bacteria.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG2141; Bacteria.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000004731; Unassembled WGS sequence.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd08700; FMT_C_OzmH_like; 1.
DR CDD; cd08649; FMT_core_NRPS_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12230; -; 1.
DR Gene3D; 3.40.50.980; -; 3.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.20.20.30; Luciferase-like domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
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; IPR024011; Biosynth_lucif-like_mOase_dom.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR NCBIfam; TIGR04020; seco_metab_LLM; 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; PF00296; Bac_luciferase; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PRINTS; PR00154; AMPBINDING.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 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:UP000004731}.
FT DOMAIN 1403..1479
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1375..1402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1513 AA; 165832 MW; 901E9A2FF18AE8AD CRC64;
MNALMIGNGS LLIQCAQIWL DRRQEISGII SENAEIREWA ARKEIPVFAD YSQVDIVSVD
WLFSVANLKM LPASFLKIAK IGALNFHDGP LPCYAGLNAP VWALLNHEKR HGITWHLMQD
RADTGDIVEQ RIFEIPAGET ALSLNAKCYA AGIDGFTALV DPLIAGNLAP ESQDTQNRHY
FGRNARPKAA GVLDFTTSAQ DVVRFVNALD HGNYANPLAV AKIIIEDQVF LVGNASAIDD
QTGNAGTVLK TGVNELTIAC HNGAVALSDI KSVYRHALDV SKLVQSGDKL TQVSRDEIDR
LLAPLAKAEA DLVQELSKIE NTDQSFVRDR NLPENWQSSH IVLKGDADKR LALINIFARC
HGQSHVALAV ETEFQNPLIC SWMPLATPKA ETTIKMALEA TKTCHGETIK RGAFVADLFA
RTPNLRETKT PIFGITHMSA GICGTAISFE INENCTVLHF DENQIDRASV DIYAARLLEL
QNTDASINIV DIPRLNPIEL DLVLNQWNDT KKAYDNCPIH KQFETIAAKS PDETALVFEE
QQLSFQTLNN RANTVALTLE KMGVKLGDRV GIHLKRSPEM IIALLATLKV GAAYVPLDPN
YPSDRIAHYV NDSGAKIIIT QTDLMSELPS HDAQTVDIKT ISLDTAANNP NTAVTKDDLA
YLIYTSGSTG TPKGVMVEHG NVANFMSAMD DRVSYENGDS WLAVTSLSFD ISVLELLFTL
TRGIKLILSS DDSRLLISNG KPKTSAMDFS LYYWGNDDET SANKYDLLLK GAQFADQNGF
VAVWTPERHF HAFGGPYPNP AVTGAAVAAV TNNIAVRAGS CVAPLHHPAR IAEEWAVIDN
LTNGRVGLAM ASGWQPDDFV LRPENTPPDN KPALFETIKT VRRLWEGEAV EFPTAKGTPH
AVVTQPRPLS KTLPIWVTSA GNPETWVEAA NLGANVLTHL LGQSVAEVGE KIEIYHDALR
AAGHDPKDFK VTVMLHTLIG EDREVVREIA REPMKDYLRS AAGLIKQYAY AFPAFKKTKG
AETTFDLGSL EPDELKAILD FAFTRYFEDS GLFGTPDDAA RRVAELQAIG VGEVACLIDY
GIDTNQVLEG LRPLAAVVAE TNATTEMAPD DFSIAAQIER HNISHLQCTP SMARMMLADQ
SARQAFGGLK HVLLGGEALP DDLVQDVKTV TNASLSNMYG PTETTIWSTS ENVQSGSEAI
VNIGTPIANT QVYVLDGAKN PVAVGEEGEL YIAGDGVTRG YWQRPELTNE RYVPNPFTNG
RMYQTGDLVK WRSDGKLDYV GRADQQLKLR GYRIELGEID AAISKLKNVD QAVVVAREDR
PGDVRLVAYL MAASPIKTLD LRQHLLGVLP DYMVPSHFVQ VDHFPLTPNK KIDRKALPAP
KVAQPTSDQA KPLPKLNHPQ NNASKTDLLR EIGAIWMDIL GVTSVNPQDN FFDLGGHSLL
AVQTHRAIRD QLNLANLSIT DIFRFPTLDG LCAQLATPDD DTKPITSAPK TTRNDTMSRR
RAMRAARLQK IKN
//
