ID A5W230_PSEP1 Unreviewed; 439 AA.
AC A5W230;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=FAD-linked oxidoreductase {ECO:0000313|EMBL:ABQ78190.1};
GN OrderedLocusNames=Pput_2050 {ECO:0000313|EMBL:ABQ78190.1};
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746 {ECO:0000313|EMBL:ABQ78190.1};
RN [1] {ECO:0000313|EMBL:ABQ78190.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F1 {ECO:0000313|EMBL:ABQ78190.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000712; ABQ78190.1; -; Genomic_DNA.
DR AlphaFoldDB; A5W230; -.
DR KEGG; ppf:Pput_2050; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_003896_4_3_6; -.
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; 3.30.43.10; 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 PANTHER; PTHR43762; L-GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR43762:SF1; L-GULONOLACTONE OXIDASE; 1.
DR Pfam; PF04030; ALO; 2.
DR Pfam; PF01565; FAD_binding_4; 1.
DR PIRSF; PIRSF000136; LGO_GLO; 2.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 43..212
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 439 AA; 48959 MW; 4024E57386989BD2 CRC64;
MATPPSDYKN NRQENDVSTS SNNMHINEFG LEHAHWRNWA GNQSCIRTAR GAPASEDELC
SMVSQASSNG MNVRVAGSGH SFTPVALTNG LHLTLANMSG VRHIDHERKR VTAAAGTTIN
ALGKTLRAAG LSMVNQGDID SQSIAGALTT GTHGTGLTLG NLASSIVGMK LVQPNGEILV
VDESTPDLLQ AGRVSLGVLG IVSELTLQVT DSFNLHERIW REDFESVMEK HDELARKHRH
FSFFWCPYEQ SRHCYCLPDT AATSTSGRTT DVCEVKVMDI TGHPIWESEF EKVAYSSDVY
PIEYLPNFHE LEYAVPLRHS KEALRAVRKL MLEDFPKAIY PIEYRFTAGD GAWMSPFFEQ
DSVTISVSGQ PGTDYWDYLR AVDQILRSYG ARPHWGKLHF LTGEDVSAIY PRAEDFRKLR
RQLDPQGIYL SEHLSPLFR
//
