ID D2ATG9_STRRD Unreviewed; 1835 AA. AC D2ATG9; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 02-SEP-2026, entry version 101. DE RecName: Full=Phenyloxazoline synthase MbtB {ECO:0000256|ARBA:ARBA00016743}; DE AltName: Full=Mycobactin synthetase protein B {ECO:0000256|ARBA:ARBA00033440}; GN OrderedLocusNames=Sros_3767 {ECO:0000313|EMBL:ACZ86689.1}; OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / OS KCTC 9067 / NCIMB 10171 / NRRL 2505 / NI 9100). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Streptosporangiales; OC Streptosporangiaceae; Streptosporangium. OX NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ86689.1, ECO:0000313|Proteomes:UP000002029}; RN [1] {ECO:0000313|EMBL:ACZ86689.1, ECO:0000313|Proteomes:UP000002029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100 RC {ECO:0000313|Proteomes:UP000002029}; RX PubMed=21304675; DOI=10.4056/sigs.631049; RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T., RA Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L., RA Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N., RA Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Streptosporangium roseum type strain (NI RT 9100)."; RL Stand. Genomic Sci. 2:29-37(2010). CC -!- COFACTOR: CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; CC Evidence={ECO:0000256|ARBA:ARBA00001957, ECO:0000256|PROSITE- CC ProRule:PRU00258}; CC -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis. CC {ECO:0000256|ARBA:ARBA00005102}. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. CC MbtB subfamily. {ECO:0000256|ARBA:ARBA00007380}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001814; ACZ86689.1; -; Genomic_DNA. DR STRING; 479432.Sros_3767; -. DR KEGG; sro:Sros_3767; -. DR eggNOG; COG1020; Bacteria. DR eggNOG; COG2226; Bacteria. DR eggNOG; COG3319; Bacteria. DR HOGENOM; CLU_000022_2_15_11; -. DR Proteomes; UP000002029; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0000036; F:acyl carrier activity; IEA:TreeGrafter. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro. DR GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IEA:TreeGrafter. DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProtKB-ARBA. DR CDD; cd12114; A_NRPS_TlmIV_like; 1. DR CDD; cd02440; AdoMet_MTases; 1. DR CDD; cd19535; Cyc_NRPS; 1. DR FunFam; 1.10.1200.10:FF:000016; Non-ribosomal peptide synthase; 1. DR FunFam; 3.30.559.10:FF:000023; Non-ribosomal peptide synthetase; 1. DR FunFam; 3.40.50.12780:FF:000012; Non-ribosomal peptide synthetase; 1. DR FunFam; 3.30.559.30:FF:000006; Yersiniabactin polyketide/non-ribosomal peptide synthetase; 1. DR Gene3D; 3.30.300.30; -; 2. DR Gene3D; 1.10.1200.10; ACP-like; 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; 1.10.10.1830; Non-ribosomal peptide synthase, adenylation domain; 1. DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR010071; AA_adenyl_dom. DR InterPro; IPR029058; AB_hydrolase_fold. DR InterPro; IPR036736; ACP-like_sf. DR InterPro; IPR045851; AMP-b_sf. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_synth/lig_dom. DR InterPro; IPR042099; ANL_N_sf. DR InterPro; IPR023213; CAT-like_dom_sf. DR InterPro; IPR001242; Condensation_dom. DR InterPro; IPR057737; Condensation_MtbB-like. DR InterPro; IPR013217; Methyltransf_12. DR InterPro; IPR020806; PKS_PP-bd. DR InterPro; IPR009081; PP-bd_ACP. DR InterPro; IPR006162; Ppantetheine_attach_site. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR001031; Thioesterase. DR InterPro; IPR041464; TubC_N. DR InterPro; IPR044894; TubC_N_sf. DR NCBIfam; TIGR01733; AA-adenyl-dom; 1. DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1. DR PANTHER; PTHR45527:SF10; PYOCHELIN SYNTHASE PCHF; 1. DR Pfam; PF00501; AMP-binding; 1. DR Pfam; PF00668; Condensation; 1. DR Pfam; PF08242; Methyltransf_12; 1. DR Pfam; PF00550; PP-binding; 1. DR Pfam; PF00975; Thioesterase; 1. DR Pfam; PF18563; TubC_N; 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 SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS00455; AMP_BINDING; 1. DR PROSITE; PS50075; CARRIER; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. PE 3: Inferred from homology; KW Ligase {ECO:0000256|ARBA:ARBA00022598}; KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450, ECO:0000256|PROSITE- KW ProRule:PRU00258}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000002029}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}. FT DOMAIN 1431..1512 FT /note="Carrier" FT /evidence="ECO:0000259|PROSITE:PS50075" FT REGION 1508..1533 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1508..1519 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1466 FT /note="O-(pantetheine 4'-phosphoryl)serine" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00258" SQ SEQUENCE 1835 AA; 200928 MW; F70BCDABB5ABDB7D CRC64; MTAGAGKPGG GERAAAGRLV AELERQGVRL WEEDGRLRFR APQGVLTDER RALLSAHKEA VLDHLSRPGP EVTPQPEDRH EPFPLTDVQA AYVLGRRDAF DYGGTACQVY AELAFPELDP PRLEAAWRAL VRRHDMLRAV VHVDGYQQVL ADVPDYRIEV TDLRGEPAGR VSGHLDEVRA AMDHRVYDAD AWPLFELRVT RTDGQALLHV SIDFLIADYL SIQLLLTELK RLYLDPDHPL PPLEIGFRDY LLAARRLREG AAYERDRDYW EGRVDELPGP PELPVRDNAA AEAGRRFTRH QVTLDAGQWE RFRARSGAHG VTPSTAVLAA FAEVVARWSR RPRFSLNLTL LNRQPLHPQV GGLVGDFTTV SLLAVDGEAG AAFHGRARAL QDRLWEDLDH RLYSGVEVMR EIARRRGRGA ALMPVVFTST IGLSDEASGH EGMNGLAEVV YGRSQTPQVW IDCQAVVEGG ALEVRWDVRD GVFPPGLVED AFGAMEELLR ALATSDEPWD SACPVALPAV QAGRRDRVNA TTEPLPRGLL HEAVVAQALR EPGRAAVVTG ERTLTYGELL ARAVGVAETL KARGFEQGAL AAVMMDKGWE QVVAVLGTLL AGGAYLPVDT GQPPARRARI LADAGVRHVL TQSWIRDRPE GADLVDVDLL LPSALPAPQP AADPGDLAYV IYTSGSTGDP KGVMISHRAA LNTVADVNRR FAVTAEDRVL GLAGLGFDLS VYDIFGPLSL GGALVLPDAE GRGDPAHWAR LIAGHGVTVW NSVPAQLQML DHYLGSQPEP DLPSLRLAML SGDWIPIALP GRVRGRLPGL ELISLGGATE AAIWSIYHPI GEVRDGLRSI PYGTPLANQA FHVLDEALRP CPDWVPGELY ISGAGLALGY LGDEDRTAQR FIRRPGTGER LYRTGDLGRY HDDGTIEFLG REDRQVKIRG HRIELAEVEA AIQSHPAVAA VHVLLDGTGM ERRLAAFAEP VRRAASGDDP AAELAAAAAA AADPHTTHID RAELMEFIGR LDRAAVIGMM WALRRRGLFG STSERTTTEQ VLAATGAAPR HHRLVRRWLR VLEREGVIAG DGDGFRATRV IEAADLARAW QAVEELQRED SYKAVLIDYF KESTERLPEL LRDELDPLPL LFPEGRLEIS EAAYRENIIS RYVNHAAIAV LRGIAARHDG PLRVIEVGAG VGGTSAQMIP ALAEFDVDYL FTDVSPFFLN EARERFGERP WVRYGLFDIN EDYREQGYAP NDFDVVLCAN VLHNSRHAGR VLAGLREMLR PGGWLVFIET TKDSYQIMTS MEFMMPEKDP RKWDYEDLRK GRDQTFLGRE EWLGLLTGAG ADTTLCLPGP DDVTGPLGQN VFAARFKSDR ARLGVAGLAE HLADRLPEYM IPSHTQVVDA LPLTGNGKVD HAALRSWLPR AASGRAAAGG EPRDDLERRL AAVWAEVLGL VRVDREEDFF ELGGDSLVVA KLAARLREEV AETRDLFWDD LVRQILHRPT VAALAEHVRR ARDEEESGPR GEASPLVPLG GDEDGGDGAL RVLVHEGSGT LAPYRALARL LAAKGGPLVG LAITEVERYL AEEPEGLIER RAARYARALL DTGSSRFHVV GYCMGGLLAT EVARHLTEAG AAVESLTVIS SYTLPRIIED ELVVEYVFAR VMGIDPADAG YPGDEATMSR VFELLLAEDP ERVPAGRVAG LTGDPALESA AADFRRLAGL SQRERLAAIG RAATETRSDP EVERHVNSLF QVVRHSLLAV GTHTPEPYAG DITFLRQLGD TRFLPWLRDD MTGFWRELCL GDLEVVDVPG DHFTCLQPPN VDEVATFLAT SQAAR //