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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//