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Database: UniProt
Entry: A0A0Q4CPX5_9SPHN
LinkDB: A0A0Q4CPX5_9SPHN
Original site: A0A0Q4CPX5_9SPHN 
ID   A0A0Q4CPX5_9SPHN        Unreviewed;       495 AA.
AC   A0A0Q4CPX5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=FAD-containing monooxygenase EthA {ECO:0000313|EMBL:KQM27992.1};
GN   ORFNames=ASE58_06640 {ECO:0000313|EMBL:KQM27992.1};
OS   Sphingomonas sp. Leaf9.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1735674 {ECO:0000313|EMBL:KQM27992.1, ECO:0000313|Proteomes:UP000051210};
RN   [1] {ECO:0000313|EMBL:KQM27992.1, ECO:0000313|Proteomes:UP000051210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf9 {ECO:0000313|EMBL:KQM27992.1,
RC   ECO:0000313|Proteomes:UP000051210};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQM27992.1, ECO:0000313|Proteomes:UP000051210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf9 {ECO:0000313|EMBL:KQM27992.1,
RC   ECO:0000313|Proteomes:UP000051210};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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 FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
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:KQM27992.1}.
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DR   EMBL; LMKC01000002; KQM27992.1; -; Genomic_DNA.
DR   RefSeq; WP_055819025.1; NZ_LMKC01000002.1.
DR   AlphaFoldDB; A0A0Q4CPX5; -.
DR   OrthoDB; 312624at2; -.
DR   Proteomes; UP000051210; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR43872; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02570)-RELATED; 1.
DR   PANTHER; PTHR43872:SF1; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02570)-RELATED; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000313|EMBL:KQM27992.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   495 AA;  54481 MW;  F4F0955F0F3EF028 CRC64;
     MPTPAPPAPE LDVAIIGAGL SGIDAAWHLQ HRCPDRTYAI FEARGAIGGT WDLFRYPGVR
     SDSDMHTLGF PFRPWRGDKA IADGSDIRDY IEDTARAFGI DRHIRFRHRI VAADWSSDTA
     RWTLTCDVDG VVSTLRCRFL FMGCGYYDYA RGHAPDFAGQ GDFAGPIVHP QHWPQALDVA
     GKRVAVIGSG ATAVTLVPAL AARGAQVTMV QRSPSHIVAQ PARDRVARLL YRLFPERLAG
     RMARWKSAAL GLAAYQFARR WPRRMEALIL KGVRAELPDM ADVDRHFTPR YDPWDQRLCL
     VPDADLFAAL RDGSAIIATD TIRRFTPNGI ELGSGARVDA DIIVTATGLR LHLLGGIALT
     IDGAPFVPAD HLIYRGMMAS GVPNLVLALG YTNASWTLKI DLVSRRMCRM LNHMRRHGHD
     ICLPTPPGPD VARRPLLDFS SGYVTRAAAI SPAQGSRAPW RLRQNYFLDY ATLRFGSLAD
     GVLRFARAGT GSARD
//
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