ID A0A1K2CP76_STRAR Unreviewed; 2422 AA.
AC A0A1K2CP76;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Amino acid adenylation domain-containing protein/natural product biosynthesis luciferase-like monooxygenase domain-containing protein {ECO:0000313|EMBL:SFY12284.1};
GN ORFNames=SAMN02787144_1011107 {ECO:0000313|EMBL:SFY12284.1};
OS Streptomyces atratus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1893 {ECO:0000313|EMBL:SFY12284.1, ECO:0000313|Proteomes:UP000181909};
RN [1] {ECO:0000313|EMBL:SFY12284.1, ECO:0000313|Proteomes:UP000181909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK807 {ECO:0000313|EMBL:SFY12284.1,
RC ECO:0000313|Proteomes:UP000181909};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; FPJO01000011; SFY12284.1; -; Genomic_DNA.
DR RefSeq; WP_072486588.1; NZ_FPJO01000011.1.
DR STRING; 1893.SAMN02787144_1011107; -.
DR OrthoDB; 5478077at2; -.
DR Proteomes; UP000181909; Unassembled WGS sequence.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic 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 CDD; cd05930; A_NRPS; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.20.20.30; Luciferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR005814; Aminotrans_3.
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; IPR024011; Biosynth_lucif-like_mOase_dom.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
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 InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR NCBIfam; TIGR04020; seco_metab_LLM; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00296; Bac_luciferase; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Monooxygenase {ECO:0000313|EMBL:SFY12284.1};
KW Oxidoreductase {ECO:0000313|EMBL:SFY12284.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 1907..1984
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1499..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1874..1906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2422 AA; 264158 MW; EC5FE7154441EA85 CRC64;
MNEQENLTAT LDRDLAAMAG LAQRVTEQID AGRAMAGSTQ QPQAHGPRVV IAPDAGMVRS
TSPRTQQEHL DDLVRRYTAR TAASRQLAQR HRRRLADSRA VVGFRKSTKE MLYPVAARRA
EGARIEDIDG NSYTDITMGF GVLLFGHEPG FVREAVREHL SRGIRLGPRS VETGGAAELL
CELTGMERVA FANSGTEANA AAIRLARAAT GRDRIVTFQG SYHGHADQVL GRPAGHGAQE
GTVPVSRGIP HSAVSELTVL EYGSEEALRA IERDAARIAV VVVEPVQSRH PSLQPAAFVR
RLRELTARHG IVLMFDEMLT GFRPALRGAQ ELYGVTPDLA TYGKLLGGGF PIGAVAGRSD
IMDGIDGGYW TYGDDSGPTA DTTFFGGTYL QHPVSMTAAL AVLTHLKEHS PHLQERLNAR
TTELATGLND FFEAEEFPLR MGWFGSQFRF EHRADMELLY YHLMLRGVHV WEWRNFFLST
AHTDGDIEHV ADAVRGSLRD LRKAGFFRTG GAPSRTRRPA PGQAAVTPAA AWPVPPAEAV
VEAVADAPPV PVAAPDSAAH TTPRRADFSL YFFGDYPDDG PGPKEGRYEL LMEAARFADR
HGFEALWMPE RHFNSFGGLF PNPAVLVAAL SRETRRIRLN AGSVVLPLHD PIRVAEEWSM
ADNLSGGRVG LGVASGWNAN DFVFFPERFG PHKQEMYDRL EQVRSLWRGE TLRRTTGDGE
REIRLFPRPV QTMPPLCTAV VANPESYERA AAHDLGIVTN LMTQDIDQLR DNIARYRRAR
ARHGLDPDAG RVAVLLHTYL SEDHETARAE AFAPMARYMQ ASLSLFSGVT NSLGVTTDLR
SLSEDDLDVV FRRAYGRYCD QRALIGDVDT VLPVVEAVVD AGADEIVALV DFGVSADQLR
AGLPRLDALR RRHRERQTPA PGAPLSPGQE RIWFLERLLP ERTAYNEVKA IRLRGALDTE
ALHTALRRLV ARHEGLRTVF RQAGDSAVQL VREAAEPDFG VVDGTLRAEA AVQEALATES
TRRFDLENGP LFVSRVVRTA VDEHVLVLSF HHIVVDAASA TVLCRDLSAF YRAERDGTEA
GLPALTWSYA RHAREQRAAA DGPDTAQDLA HWLRVLGGDL PVLELPTDRP RPAEMTSEGR
AVFRSLDPGL SEQVRQLSRG HRATLFMTLV AGWAAMLQRV TGQEDIVIGI PVSDRPQRAE
ELIGFFVNTL ALRVDLAGDP GFATLLDRVR TAALDAYDHA GTPFEKVVRV LAPPRRTDRT
PVFQVCAEFQ SAEPFRLDLP GIEAVALDAG PDKALTDLTV YFTDRPEGVR CHLEYNAELF
EPGTIDMFFT VFRDLLAAAV GKPGTPLSLL ARAAVEGDEV PESWEHGPVR PVADTTVHDW
IARQAAEHPA RTAVVGEDAV LTYRELDERA GRLAAVLAEH RADGDQESLV AVWLPRSAEL
VVALLAVLRA GCAYVPLDPS LGAVRATQVI AESGARTVIS GADGSEDLRL PGSVTVVAPD
AAPTGDPGAG SRPASDTGGS SPFSACSVIY TSGSTGTPKG VVLTHRGLVD LCQWHHERFA
FTGDDRSAVV CSQSFDASLL EIWPALTAGG TIVVAGEPIR RDPLALARWY ADQDIAFSVL
PTALGEQVLR LPVADQPPLR HLLLGGEALR SRPRPEAPYE TLNIYGPTET TVLCVVDTVS
PGADGPVPDE GADVIAIGRP ADNVTLRVVD ASDKPVPIGA VGELFVGGPG VAAGYLHRPD
LTEGRFAAAP EAGAEARYYR TGDLVRWTAD GRLVFVGRTD DQVKIRGFRI EPEEVAQVLG
RLDGVRRAAV VGRRRANGEA FLAAYVVPTE PGCDSTAEQR SRTDRWAEEL SHHLPEYMVP
RAWRVLTELP LTGNGKVDRT QLPSADPFLP ADGEGARRAD GPSPEAGPLT AVENGLRDLW
AAEFGLTPSG IDQDVSLFDL GGHSLTTMRL VNRIREAWGI EYPLSRLYQE PTLRAMTEFV
HGAGSRRVVR RGPASHQQSR FASLHSRHAK PQVFNVALRI TFSGRLDPGS LHTALQQLTE
RHEALRTRLV REGLSSWRQE VLESRPLDLP VDDLTSRPEP ERQAQVRRLA EQATETPLDL
FEGDVLSTRL LRTGAEEWVL LLVMHHCTCD GWALTTLLKE LAALYRTAVT GTGHGLSPAA
PQQVEYAHWQ VAHEAATGGR RTDYWLEELA DAPFTVDLPL DRPRPDTLSG RGGVVEFTVP
AEIRADVERL AVRRATTPFV VTAAALGRLL AAKAEQEDVV MNISYAGRES REFESLVGCT
AIGFALRVRD ARAGSFAALT DRVTRTTVLG MEHAMPPRRV APAMRERRGV DIPDGLAIGL
AYESSLDTGI ELPGLTTTVA EIAPAASRSE FIMVLTPAGD VLRGAVEYSA DLWDRATVET
WTREYVRLLR DKVREALADG TS
//
