ID N9GS88_ACIHA Unreviewed; 496 AA.
AC N9GS88;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=FAD-containing monooxygenase EthA {ECO:0008006|Google:ProtNLM};
GN ORFNames=F927_00537 {ECO:0000313|EMBL:ENW20061.1};
OS Acinetobacter haemolyticus CIP 64.3 = MTCC 9819.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217659 {ECO:0000313|EMBL:ENW20061.1, ECO:0000313|Proteomes:UP000017667};
RN [1] {ECO:0000313|EMBL:ENW20061.1, ECO:0000313|Proteomes:UP000017667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 64.3 {ECO:0000313|EMBL:ENW20061.1,
RC ECO:0000313|Proteomes:UP000017667};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter haemolyticus CIP 64.3.";
RL Submitted (FEB-2013) 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:ENW20061.1}.
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DR EMBL; APQQ01000012; ENW20061.1; -; Genomic_DNA.
DR RefSeq; WP_005086827.1; NZ_KB849812.1.
DR AlphaFoldDB; N9GS88; -.
DR PATRIC; fig|1217659.3.peg.526; -.
DR HOGENOM; CLU_032067_2_0_6; -.
DR Proteomes; UP000017667; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.
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 Pfam; PF13450; NAD_binding_8; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 496 AA; 55928 MW; F53FBDD8B1593429 CRC64;
MEKQVDVLII GAGISGIGLA VHLSKNCPQR QFEILERRDS FGGTWDLFRY PGIRSDSDMS
TFGFNFKPWA KDKVLASGPE IKGYLSEVID EFKLKEKIHF GHRVLSANYD SAKKKWLVEI
EDSNNKKQTW SANFVMGCTG YYNYDQGYAP QFPEQDKFKG QFIHPQHWPE NLDYTGKKVV
IVGSGATAIT LVPSMVKGGA GHVTMLQRSP TYIATVPSID FIYEKTRRFM SEETAYKFTR
ARNIGMQRAI YALAQKHPKT VRRLLLKGIE LQLKGKVDMK HFTPSYNPWD QRLCVVPDGD
LFKALRQGQA SIETDQIEKF TANGIQLKSG KHLEADIVIS ATGLEIQILG GVKGSIDGKP
MNTSHHMLYQ GVMVSDVPNM AMIIGYINAS WTLKVDIAAD YICRLLNHMD KNGFDEVIAH
ADPAQFEQDT IMGKLSSGYI ARAADIMPKQ GKQAPWKISN NYLADRKELK DAKFNDGVLQ
FRKRDEQVDR KPKLVS
//
