ID A0A0Q8PX71_9ACTN Unreviewed; 434 AA.
AC A0A0Q8PX71;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=FAD-linked oxidoreductase {ECO:0000313|EMBL:KRB75882.1};
GN ORFNames=ASE01_12565 {ECO:0000313|EMBL:KRB75882.1};
OS Nocardioides sp. Root190.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB75882.1, ECO:0000313|Proteomes:UP000050886};
RN [1] {ECO:0000313|EMBL:KRB75882.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB75882.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB75882.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB75882.1,
RC ECO:0000313|Proteomes:UP000050886};
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 -!- 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:KRB75882.1}.
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; LMIA01000010; KRB75882.1; -; Genomic_DNA.
DR RefSeq; WP_056752688.1; NZ_LMIA01000010.1.
DR AlphaFoldDB; A0A0Q8PX71; -.
DR STRING; 1736488.ASE01_12565; -.
DR OrthoDB; 9800184at2; -.
DR Proteomes; UP000050886; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2520; -; 1.
DR Gene3D; 3.30.70.2530; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR007173; ALO_C.
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; IPR010031; FAD_lactone_oxidase-like.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR01679; bact_FAD_ox; 1.
DR PANTHER; PTHR43762; L-GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR43762:SF1; L-GULONOLACTONE OXIDASE; 1.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR PIRSF; PIRSF000136; LGO_GLO; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000050886}.
FT DOMAIN 11..181
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 434 AA; 47129 MW; 3E8DDD029478CF2F CRC64;
MSTWRNWSGL ESASGLEQVT PATREEVVGI VSGARAAGRT VKAAGTGHSF TAIARPEHVQ
LLPDRMRGIV AVDRDAMTVT ALAGTQLKVF NVELERLGLS LHNMGDIAEQ TLAGAVSTGT
HGTGGRAAGL AAQVVGFELV TGTGEVLSVS ATENPDVLSL GRAGLGALGV IVTLTFAVEP
LFLIRAVEQP MSWDDAFAAF DDLTAAHDHV DMYWFPHTDR VLTKRNTRLG TDLAGVEPLP
RWRAWLDDDL LSNTVFGTQT AALNLAPRAI PAANRFASRL LGARSYTDVA HRVFTTERRV
VFREMEYAVP REAGLTALRE CRAAFERSGL TVSFPVEIRV APADDVALST SYGRDSFYLA
FHTHRRADHT AYFALLEPIM RAHGGRPHWG KVHTLGAADL APLYPRFDDF VALRNRLDPD
RVLTNPYLDR VLGA
//
