ID A0A0N1G2M1_9ACTN Unreviewed; 615 AA.
AC A0A0N1G2M1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Pentachlorophenol monooxygenase {ECO:0000313|EMBL:KPI09205.1};
DE EC=1.14.13.50 {ECO:0000313|EMBL:KPI09205.1};
GN ORFNames=OK074_3366 {ECO:0000313|EMBL:KPI09205.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI09205.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI09205.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI09205.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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:KPI09205.1}.
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DR EMBL; LJCV01000244; KPI09205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1G2M1; -.
DR PATRIC; fig|1592327.3.peg.5548; -.
DR OrthoDB; 8670884at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0018677; F:pentachlorophenol monooxygenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.70.2450; -; 1.
DR Gene3D; 3.40.30.120; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43004:SF6; FAD_NAD(P)-BINDING OXIDOREDUCTASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF21274; Rng_hyd_C; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000313|EMBL:KPI09205.1};
KW Oxidoreductase {ECO:0000313|EMBL:KPI09205.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991}.
FT DOMAIN 10..346
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 379..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 66199 MW; 4E5BF0E31FBC6F41 CRC64;
MTTTPTATNT EVIICGTGAA GLTLAIDLAR RNVGFLLIDK APHPFVGSRG KGIQPRSQEV
FEDLGVIDRI VASGGEYPVQ RIHTADGPLD QVAVEMSEPT PEEPYQIPLL VPQFLTERRL
RERLAELGHA PHHSHELVGF EQDGDGVTAR IATPDGEQAV RAAYLIGADG GSSFVRKALG
IGFPGRTLGV RAIVADVYVD GVPSDAWHRW GEDTAGQVSL CPLYGTDMFQ LQAPVPFDVD
LDLTAEGLTA FFRARTGRDD VVIQAVSWAS AFQMNARLAD SYRNGRVFLT GDAAHCHPPT
GGQGLNTGVQ DAYNLGWKLA AVLGGAPETL LETYEQERRP IAEAVLGLSE RLLEAAKNRD
IHRGREVSQL DLGYLDSPLS LPNPGRDKGV LPGDRAPDAP VTGAGGLPTR LFTLFQGPHW
TLLGHDTDAT PAARPGLHIH TIGGARGDIL DSGDRVRDAY GLTAEQWVLV RPDGYVAAVV
DTADLAAVET HLDGVGVRRL TESTSRSTSR AMPKSTSEST SGSMSESTSE SMVSSTGSTP
RTRREHRQAR TAAEKRLATA QRELHQLSRQ VQRDLRSVRR HGETTAIVAR SNFAELAVQS
INRLTAGFRS DRADQ
//
