ID F4CTM3_PSEUX Unreviewed; 466 AA.
AC F4CTM3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=(R)-6-hydroxynicotine oxidase {ECO:0000313|EMBL:AEA28526.1};
DE EC=1.5.3.6 {ECO:0000313|EMBL:AEA28526.1};
GN OrderedLocusNames=Psed_6435 {ECO:0000313|EMBL:AEA28526.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA28526.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA28526.1, ECO:0000313|Proteomes:UP000007809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC {ECO:0000313|Proteomes:UP000007809};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; CP002593; AEA28526.1; -; Genomic_DNA.
DR RefSeq; WP_013678408.1; NC_015312.1.
DR AlphaFoldDB; F4CTM3; -.
DR STRING; 675635.Psed_6435; -.
DR KEGG; pdx:Psed_6435; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_018354_10_0_11; -.
DR OrthoDB; 9775082at2; -.
DR Proteomes; UP000007809; Chromosome.
DR GO; GO:0018530; F:(R)-6-hydroxynicotine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:AEA28526.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007809}.
FT DOMAIN 41..211
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 466 AA; 48600 MW; 39908E561B344FEB CRC64;
MTDTTTSTGT LDTLRAGFTG SVLTSADDDY ATARAPWNGA IAARPAVIAR CATPDDVGAA
LAHARREGLE IGVRGGAHSY GGAPLPEGGL TVDLSLLRHV VVDPAARRAR CGGGVTQGEL
DAATQQHGLA VTGGTISHTG VGGLTLGGGM GWLTRRCGLA VDNLRSAQVV LADGRCVRAA
PDSHPDLFWA LTGGGGNFGV VTEFEFALHP VGPIVHFGLL FWEIDRGAAA LRVARDVADA
LPRDCGALIA GFNAPPAPFV PEARHHTLGI ALLIAGLSDA QPQAAPLAEA RAALHPLFEV
GTDMPYTALQ QILDDAAPWG IHAYGKALYL DELSDAAIDV IAGRLPAKVS PMSLMPIFPL
GGAFADVAED DTAFGGRRSA RYAVNIDAAT PDPRLLPADR EWVRSTWDAL RPHAGDSGSY
VNFMTEFEPD RVAAAYGPVK FARLAAIKAS YDPDNVFHRN ANIPPA
//
