ID S4MK35_9ACTN Unreviewed; 1801 AA.
AC S4MK35;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Phenyloxazoline synthase MbtB {ECO:0000256|ARBA:ARBA00016743};
DE AltName: Full=Mycobactin synthetase protein B {ECO:0000256|ARBA:ARBA00033440};
GN ORFNames=STAFG_6995 {ECO:0000313|EMBL:EPJ35955.1};
OS Streptomyces afghaniensis 772.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1283301 {ECO:0000313|EMBL:EPJ35955.1, ECO:0000313|Proteomes:UP000015001};
RN [1] {ECO:0000313|EMBL:EPJ35955.1, ECO:0000313|Proteomes:UP000015001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=772 {ECO:0000313|EMBL:EPJ35955.1,
RC ECO:0000313|Proteomes:UP000015001};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Fiedler H.-P.,
RA Goodfellow M., Mueller M.;
RT "Draft Genome Sequence of Streptomyces afghaniensis, Which Produces
RT Compounds of the Julimycin B-Complex.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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 -!- 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:EPJ35955.1}.
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DR EMBL; AOPY01001595; EPJ35955.1; -; Genomic_DNA.
DR RefSeq; WP_020275844.1; NZ_KE354365.1.
DR PATRIC; fig|1283301.3.peg.6943; -.
DR HOGENOM; CLU_000022_2_15_11; -.
DR OrthoDB; 2472181at2; -.
DR Proteomes; UP000015001; 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:0017000; P:antibiotic 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:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd19535; Cyc_NRPS; 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_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; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
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; PHENYLOXAZOLINE SYNTHASE MBTB; 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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000015001};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1407..1488
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1801 AA; 193266 MW; 479BB5241A2E6CF9 CRC64;
MSAAELVSHL AAAGVELWEE DGRLRFRAPQ GALTDELRER LSADRDAVLA HLRDPFAEPL
VPDPDGRHLP FPLTEVQSSY LLGRTDAFAH GGIGCHAYLE YELPGTVPPE RAADAWRALV
ERHDALRTVY HPDGQQVLKE LPPYEIPVAG AEQAEGIRGE LAQRTYDPAV WPLFDLRLTH
SPERLLVHLS VDLLVTDFSG VQQLLGELEQ LCVEPDRALA LVPVSFRDHV LAERRLRDSA
RWARDRAYWL DRLDDLPAAP ELPVLPEERG ADVRFRRLAD RLTADESAAL RRAAAARDLT
VSTVLLAAYA EVIGRWSARP RFTLNLPVFA KRPVHPDIGR VVGDFTSVTL LAVEPDAGKG
FAQRARALGG RLFEDLDHGL YSGVEVLREA ARRSDRHALM PVVFTSTLQG TEVPATGPGR
VVYGVTQTPQ VWIDCQVMES GGEILLGWDV REGVLPEGLA DDAFAAFASL VRELAVSDAP
WDSADPVRLP RTQAARHAAT NATARPLPEG LLHERVFAAA VAHTDRPAVI APDRTLTYAE
LTGYARAVTA RLRAAGVAPG ERVAIVMDKG WEQVPAVLGV LDAGCVYVPV DTVHPPARRA
LVLASSGAVA VLTQAGLGDA YELPTIAVDA LEPSEAVESR RVDPGEAAYI IYTSGSTGEP
KGVVVSHRAA LNTVADIDER FGVGAGDRVL GLAQLGFDLS VYDLFGPLAH GGAVVLPDPE
RRGDPSHWAD LAARHRVTLW NSVPAQLQML HDYLASGAGA ADVAGLSGLR LGLLSGDWIP
VRLPDRIRAL LPGLRLISLG GATEAAIWSI HHPVEQPVDP GRPSILYGRP LANQTFHILD
EALRPRPDWV PGELCIGGSG LALGYHGDPE TTARRFVTHP VTGERLYRTG DLGRWLPSGD
IEFLGREDGQ VKIRGHRIEL AEIEAALTGH PAVGAAAVLA VGGDPLQRRL VAFAEPARIA
DDSRTGGAAE VLARRARQAA DAFEVAEPER IAEFARLLDE ASVASMLDAL RARGLFAGPD
AAHTAEDVVA VAVPRHERVL RRWLRVLHGE GLLERDPATG RYRLRAEPPS AAPAWDRVAA
VWSDDLGPSE LLAYLRANAD QLDALMDDRI AAVDLLFPEA RMETADAAYR ENVMSAYLNR
VLAEALRTAA EERTPGRPLR VLEVGAGTGA STAGALAALD GLPVEWLFTD VSPFFLDRAR
ERFGPDTRLR YGLYDVDGDP AGQGLALQSF DVVLCAGVLN NARDTGAALT SLRSLLVPGG
LLLVTEPTRE HYEILISQAF MMTGAEDLRR ADGADATFVT REQWLRLFAE AGGENELCLP
QRGHPLEPLG QHVFAVRFNT GRAAVDPVDV GDHLADRLPV YMLPAALHVV DALPLTPNGK
VDRKALAARA AVTAEEQPTA AGEEAAGPAD ELEERLASVA ALALGVAAVP RDRSLFDLGA
DSLVLAQLSA RLIEEVPQAA DQQFDTLLRE LLNRPTVADL ARHLRGTDTP EAGTGEVSAL
VALGDEPQEG GALHVLVHEG IGTMAPYREL SARLAGHGPL VGLAVGDVQA CTDIPAEEFV
ERLAAEHVRR LTATGADRFR LTGYCLGGQL ATEVARQLTE SGAHVEQLTV VSSSPPAFVC
EDELLIEHAF ARVLGADPAA AGYPDDEEEL GAALRAVLDA TPGRVPAGAF AALCGEPRLE
AVARRMRALA DIPQPERLAA IAATLGGDGD TAHLPGLYRV FRHAFAAASL HTTQPYAGDI
TLVRPRGRLR FLAGFGQEAD ELWREVCLGD LTVTDVDGDH FSCLRAPHVD QVVAAAVAET
P
//
