ID A0A2M9JD38_9ACTN Unreviewed; 1823 AA.
AC A0A2M9JD38;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phenyloxazoline synthase MbtB {ECO:0000256|ARBA:ARBA00016743};
DE AltName: Full=Mycobactin synthetase protein B {ECO:0000256|ARBA:ARBA00033440};
GN ORFNames=CG740_02680 {ECO:0000313|EMBL:PJN04811.1};
OS Streptomyces sp. CB01201.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2020324 {ECO:0000313|EMBL:PJN04811.1, ECO:0000313|Proteomes:UP000231916};
RN [1] {ECO:0000313|Proteomes:UP000231916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01201 {ECO:0000313|Proteomes:UP000231916};
RA Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA Shen B.;
RT "Discovery of the Leinamycin Family of Natural Products by Mining
RT Actinobacterial Genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJN04811.1}.
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DR EMBL; NNBJ01000001; PJN04811.1; -; Genomic_DNA.
DR OrthoDB; 2472181at2; -.
DR Proteomes; UP000231916; 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:0008610; P:lipid 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; cd12114; A_NRPS_TlmIV_like; 1.
DR CDD; cd19535; Cyc_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 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; 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; IPR020459; AMP-binding.
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; IPR013217; Methyltransf_12.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF18563; TubC_N; 1.
DR PRINTS; PR00154; AMPBINDING.
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.
PE 3: Inferred from homology;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 1423..1504
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1823 AA; 197704 MW; E375C0E1682E66B0 CRC64;
MNIAGLLAEL EAAGVELWEE SGRLRFRAPQ GALTDERREA LRAHKEQVLG HLRAERTRST
VVHHPDDRHT PFPLTDVQTA YLLGRKDLFA YGGVACHAYG ELRFTSLDPA RMEQAWQLLI
ERHDMLRAVV DEEGSQRVLT AVAPYRIEVT DLREAPPEHA GRALAAQRDA MDHEIRPAGV
WPLFELRATL FADHALLHVS LDFLIADYVS INLLLDELRT LYADLSAPLP ELPVTFRDYL
LAERGLRQST RYERDRAYWL DRVDELPPAP AFPMRDAPAA EGPARFVRHR LALSQPQWQA
LRDTATARGL TPSGAVLAAY AEVIGRWCNR QRFTLDLTLL NRLPLHPQVG SLVGDFTSVE
LLEVDRSSGA TFAERGKQLV GRLFEDLDHR LFTGVEVMRE IARRRGQDAA LMPVVFTSAI
GLGDAASAPA DHTEGRLVHG ISQTPQVWID CQVMEDREGL SLNWDVREGV LADGVVEAMF
ASFRTLVERM AADPGVWDLA VPTELPAEQS ARRTVANATE GPLSEALLHE GPFAAAAHSP
ENPAVISGDR VLTHGEVAAR AHAVAAALKG AGCAPGDLVG VVMDKSWEQV VAVLGTLLAG
AVYVPVDTHQ PEARREQMLR DAKVGCALVR SGRTVLPEGV TAIEVDTLDP APTAPVARLR
APDDLAYVIY TSGSTGSPKG VMISHRGAVN TIDDINERFA VGPDDRVLAL ANLGFDLSVY
DVFGVLAAGG ALVLPDPDRR ADPSHWADLV ARHGVTLWNS VPAQLHMVNE YLGTEPVPLP
SLRLALLSGD WIPVSLPDSI RAKVPGLTVT SLGGATEASI WSILHPIDEV TPGLPSIPYG
RPLTNQRFHV LDAAMEPCPD LVAGELYIAG IGLALGYLGD EARTAERFLT HPRTGERLYR
TGDLGRYLPD GEIEFLGRDD RQVKIRGHRI ETAEVEAALR SHPAVADCVV LVEGERPWER
RLMAFAETAR VPAGAAERDS ALVEAVTADG EEVRAGVNAE QVVGFARRLD EAALLAMMDV
LQTSGLFATA DDRHSLETIL LSAAVAPKHH RLVRRWLAAL EREGYVERSS KDGAYRALRR
AEPGSVDEAW VRVDEALPTA QDGSELLSYF RTATAHLPQL LRDEQDPVQL LFPEGRLEIQ
EAAYTEGFLN SYLNRVATSV VQRIAQEHAP RGTLRLLEVG AGVGGVSVEA VPRLAGTDCS
YLFTDVSQFF LNKAAERFTD FPWVDYQLFD MNEEYRPQGI EPNSLDVILC GNVMHYSRNA
SVVLDRMREM LAPGGWLIFI ETTRDNYQIL TSMEFLFDAT NGDFEDVRKG ADQTFVARDQ
WLDLIAGAGG ETVVCLPDTK DPLSTIGMHV FAVQFKQDRV PVNAAEVLGH VAERLPEEMV
PAHLQLVDAL PLTDNGKTDR RTLASWLLPR GAVEQRAGAG DRVPMTDLEQ RIQAAWCTVL
GTTAVGREET FYEAGGDSLL AAQVVGVLRE EVAEAKHTFF DELLREVLNG ASVARLAALL
ATGQIDGEQS AARESESASA APAAFLGGGD DDGVWATCAE GFGTAERYAA LCAPLEDAGP
LLDLSAGHPL TDYADATSAV LIERIAHDRA KTLRATGHTR FHLVGAHVGG VLAAETARLL
AEGGAEVDLT VISSYPLPAV VEDDAFAEYL FALGAGLDPA ALGLPGDTLT GPALAAVLAA
TPGRVPDGAL SRLDGPHAEL AQSFGQYAAR PEQERLAALA AALGTDAQDL RPRLRAGRAL
ADACAVHRPE AYAGDLTLVL HTDEIALWPT LRADMTEWWS AGCLGEVRRI DAPGTHFDCL
DPARAARIAA LLTDVRTEKE NQA
//
