ID S3WZR4_9ACTN Unreviewed; 1430 AA.
AC S3WZR4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Phenyloxazoline synthase MbtB {ECO:0000256|ARBA:ARBA00016743};
DE AltName: Full=Mycobactin synthetase protein B {ECO:0000256|ARBA:ARBA00033440};
GN ORFNames=HMPREF1531_01870 {ECO:0000313|EMBL:EPH02562.1};
OS Propionibacterium sp. oral taxon 192 str. F0372.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=1203605 {ECO:0000313|EMBL:EPH02562.1, ECO:0000313|Proteomes:UP000014567};
RN [1] {ECO:0000313|EMBL:EPH02562.1, ECO:0000313|Proteomes:UP000014567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0372 {ECO:0000313|EMBL:EPH02562.1,
RC ECO:0000313|Proteomes:UP000014567};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Socransky S.S.,
RA Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Propionibacterium sp. oral taxon 192 str. F0372.";
RL Submitted (MAY-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:EPH02562.1}.
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DR EMBL; ATFL01000014; EPH02562.1; -; Genomic_DNA.
DR STRING; 1203605.HMPREF1531_01870; -.
DR PATRIC; fig|1203605.3.peg.1930; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_2_15_11; -.
DR OrthoDB; 2472181at2; -.
DR Proteomes; UP000014567; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; 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; cd19535; Cyc_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
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 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; IPR006162; Ppantetheine_attach_site.
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; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR Pfam; PF18563; TubC_N; 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; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000014567}.
FT DOMAIN 9..54
FT /note="TubC N-terminal docking"
FT /evidence="ECO:0000259|Pfam:PF18563"
FT DOMAIN 61..391
FT /note="Condensation"
FT /evidence="ECO:0000259|Pfam:PF00668"
FT DOMAIN 522..859
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 915..990
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT DOMAIN 1132..1233
FT /note="Thioesterase"
FT /evidence="ECO:0000259|Pfam:PF00975"
SQ SEQUENCE 1430 AA; 158005 MW; 4EFC64CDD0ABD0A5 CRC64;
MSDHIRHSLR RLRDQGIHVF VDEGRLRFRA SGQPMSESQK AFLVAHRDEI IDVLTSAPED
QQILPLTEIQ SAYLLGRDEA HLYGSVGCHV YFELEYPELD SRKVCRIWNQ LVARHEMLRT
VIRSDAMMEI LPSAPGQVRV PTHVDTDRHG KVVREIRDRL RGHKYPVDSW PFFTVELTST
PQMWVMHLDF DFMIADWASI WLLLEEFSTL IHGGALPEVK LTFSQYLELE SKMKEGTDYD
RDRRFWMDRL DTLPGAPKLP VLSIEQDQRC FDRLECQIDA VSWACLQESC RAQQTTPTAL
LATIYGMVLA KWSQENHFCI NLTLLNRMPL HPEVQRVVGD FTSVSLLELD FVGTENLVNQ
VRRTQRRMMR DLDHRRFSGV EVIREMARRR GRVDALLPFV FTSSIGVVSP GASTSVGAYG
RSETPQVFID CQVMDSDQGL RINWDYRLGI LPDRLVDDMF ATMSATVQAL CDDPDWNHPL
KLDLPAWQRA AREAANDTSA DIPARTLLAD WCEKLPLFAE CPAVIVDQTV WTHAELMSAA
RRYGALLNAR GLEPGEIIAV CGSKSPELVA AICGILLAGG AYMPLDPDQP LTRLRGILER
SGAHILIADD SVAGMTDWQG ETLALDPASG VDPGDDWTLP EVDPTQLAYV IHTSGSTGVP
KGVMITHDAA WNTIADVVDR WNMNAESRVL ALSRFSFDLS VFDIFGMLSC GGALVLPTPG
AWLDPADWAA LIRTHRVSVW NSVPAMAELL IRHMENHPKN RLDSLRIVLL SGDWIPVSLP
SRLGAHAPNA TVVGLGGATE ASIWSNYHIC LPEDAEKVSI PYGYPLSNQG FAVLGRDGDD
APVWVDGDLI ITGRGLACGL LGDPELTAER FPAHDGVRCY WTGDRGRYLP NGEIEFLGRL
DDQVKVHGFR IELAEVETAM VSMVEVGSAA AAIRRHGEEV HLLAAVVPAP GVESLHGDTV
RDHLAGLLPS YMVPSQVQVV EILPLTANQK VDRDLIASWF VPDETGESVQ AIIVDDPLGT
RVVEIVSECL SQVGIGEQVS YYDLGADSLV LAQLAGRLRD LLDAESPGHR GSFDVILRGL
LDEPTLSATI AMVRVLADNA HTTEAEVAPE NDGGIGKMSL LGGTPSDVVR LVPHAGLGTM
NAFRLLNAEL VGQDLGQVKV FTISDMEAYC ALDPAELVVR LGREYAQRVI DAGHTKVQLI
GYCMGGFIAL EIARSLMEKG IDVVDLTLID STPLTHRIED SIIMEAIFLP NFYITLGQVY
PHIDEQAVMD EVMNWFNECG GQLSAADVRA RLDAPITEVS RQLAELDALG VEQRFADYTA
AISAYTDQQI PAEMLAGYYS IYVHSFLASA ISPEPYFGKV TYLQASEGMS FMLADPGEII
DFWRQVFVAG MEIEQIPGNH ITCVEMADNA KVCAARLGRL LVEALEGEQR
//