ID I4B2G5_TURPD Unreviewed; 502 AA.
AC I4B2G5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:AFM11472.1};
GN OrderedLocusNames=Turpa_0821 {ECO:0000313|EMBL:AFM11472.1};
OS Turneriella parva (strain ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H)
OS (Leptospira parva).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Turneriella.
OX NCBI_TaxID=869212 {ECO:0000313|EMBL:AFM11472.1, ECO:0000313|Proteomes:UP000006048};
RN [1] {ECO:0000313|EMBL:AFM11472.1, ECO:0000313|Proteomes:UP000006048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H
RC {ECO:0000313|Proteomes:UP000006048};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of genome of Turneriella parva DSM 21527.";
RL Submitted (JUN-2012) 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}.
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DR EMBL; CP002959; AFM11472.1; -; Genomic_DNA.
DR RefSeq; WP_014801990.1; NC_018020.1.
DR AlphaFoldDB; I4B2G5; -.
DR STRING; 869212.Turpa_0821; -.
DR KEGG; tpx:Turpa_0821; -.
DR PATRIC; fig|869212.3.peg.796; -.
DR HOGENOM; CLU_032067_2_0_12; -.
DR OrthoDB; 312624at2; -.
DR Proteomes; UP000006048; Chromosome.
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 PRINTS; PR00469; PNDRDTASEII.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006048}.
SQ SEQUENCE 502 AA; 55798 MW; 367AC42FD6AA701C CRC64;
MATKVKENSQ PAQREHFDQA QHKHFDVLII GAGISGIGAA CYLKRELPGK SYAILERRQA
IGGTWDLFRY PGIRSDSDMN TFGFGFRPWT ETRVLSDGPS IKKYVEDTAK EYDVTRHIRF
GTRVTSAKFS SKDATWTLET QSETGGAAAT YTANFIIACT GYYNYDKGYQ PEFPGEKSFK
GQLIHPQKWP ENLDYAGKKV VVIGSGATAV TLLPAMADKT AHITMLQRSP TYIVSIPSND
FLSQTLRRFL PKSWVYQMAR VRNIALQRLI FMLAKARPDA IRRLILGGAK RELGDAVDIK
HFSPKYNPWD ERLCVVPDGD LFKTLKSGKA SVVTDQIETF TETGIKLKSG NELEADIVVS
ATGLNVELMG GVEVEVDGAK VPVTQRVTYK AVLVEGVPNA AIIFGYTNAS WTLKVDIACE
YICRLLKHMD KNHQRVVVAR AKDEVKTADT VMGGLNSGYI RRAIDKLPRQ GTHGVWKVSN
DYISDSAMLK FSPIADEALE FS
//
