ID A1B808_PARDP Unreviewed; 423 AA.
AC A1B808;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=FAD-linked oxidoreductase {ECO:0000313|EMBL:ABL71652.1};
GN OrderedLocusNames=Pden_3584 {ECO:0000313|EMBL:ABL71652.1};
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL71652.1, ECO:0000313|Proteomes:UP000000361};
RN [1] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000490; ABL71652.1; -; Genomic_DNA.
DR RefSeq; WP_011749821.1; NC_008687.1.
DR AlphaFoldDB; A1B808; -.
DR STRING; 318586.Pden_3584; -.
DR EnsemblBacteria; ABL71652; ABL71652; Pden_3584.
DR GeneID; 75502976; -.
DR KEGG; pde:Pden_3584; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_003896_4_3_5; -.
DR OrthoDB; 9800184at2; -.
DR Proteomes; UP000000361; Chromosome 2.
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; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000361}.
FT DOMAIN 27..196
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 423 AA; 47243 MW; BC092154CAE52348 CRC64;
MNTSSHGMTV NDFGLEHAHW RNWVGNQSCV RAARAAPASE DELCALIAGA TGKGMNVRVA
GSGHSFTPVA LTSGLHLTLA KMKGVKHIDH ERRRVTASAG TTINELVKVL KAEGLSMINQ
GDIDSQAIAG ALTTGTHGTG AALPVLADAI VGMKLIQPDG SIITVDESTP DLLLAGRVSL
GLLGAISEMT LQLTDSYRLR ERIWREDFES AMEMHDELAA RHRHFSFFWC PYEQSRHCYC
LPDTSATSKS GRTTDVCEMK VMDITDEEPF EAEFEKVAYS SDVYPIEYVA NFHELEYAVP
REHGKDAVRA VRRLMLEEFP DAIYPIEYRF TAGDEAWMSP FHRQDSVTVS VSGEPGKDYW
DYLRAVDQIL RGYGARPHWG KMHFLTGQDV TDIYPRADDF RALRRKLDPQ GFYLNDHLSQ
LFR
//
