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Database: UniProt
Entry: A0A059KPW8_9BURK
LinkDB: A0A059KPW8_9BURK
Original site: A0A059KPW8_9BURK 
ID   A0A059KPW8_9BURK        Unreviewed;       374 AA.
AC   A0A059KPW8;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=FAD linked oxidase domain-containing protein {ECO:0000313|EMBL:KDB53481.1};
GN   ORFNames=X805_09360 {ECO:0000313|EMBL:KDB53481.1};
OS   Sphaerotilus natans subsp. natans DSM 6575.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Sphaerotilus.
OX   NCBI_TaxID=1286631 {ECO:0000313|EMBL:KDB53481.1, ECO:0000313|Proteomes:UP000026714};
RN   [1] {ECO:0000313|EMBL:KDB53481.1, ECO:0000313|Proteomes:UP000026714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6575 {ECO:0000313|EMBL:KDB53481.1,
RC   ECO:0000313|Proteomes:UP000026714};
RX   PubMed=24965827; DOI=10.1111/1574-6941.12372;
RA   Park S., Kim D.H., Lee J.H., Hur H.G.;
RT   "Sphaerotilus natans encrusted with nanoball-shaped Fe(III) oxide minerals
RT   formed by nitrate-reducing mixotrophic Fe(II) oxidation.";
RL   FEMS Microbiol. Ecol. 90:68-77(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KDB53481.1}.
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DR   EMBL; AZRA01000024; KDB53481.1; -; Genomic_DNA.
DR   RefSeq; WP_037478777.1; NZ_AZRA01000024.1.
DR   AlphaFoldDB; A0A059KPW8; -.
DR   STRING; 34103.SAMN05421778_10586; -.
DR   PATRIC; fig|1286631.3.peg.924; -.
DR   eggNOG; COG0277; Bacteria.
DR   Proteomes; UP000026714; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
FT   DOMAIN          1..178
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   374 AA;  40004 MW;  FA269E97A9F7FB9B CRC64;
     MSIKALDSLI ERVRVAREAR GTLAIRGGGT KSFYGEPVQG RLLDVRCLNG ITRYEPSELV
     ITARAGTPIA EVEAELARRN QYLAFEPPRY PDIERPGQRG GTVGGMVATG LAGPSRAAVG
     GVRDYVLGLT LLTGKAEVLS FGGQVMKNVA GYDVARMVTG SLGILGVICE VSLKVMPVPS
     YTSTLRFDCS EGEALDLMQR WAGQPLPVNA TAWWQGALVV RLAGATAAVA SANQKMGGEP
     IDNALAQRFW LGMRDQTDDF FVDARRSLAD GAALWRLSLP AGAPPVPLPG EQLIEWGGAQ
     RWWVTRESAA RVRQIAAASG GHATLFRARD KAVASSGLGV FTPLKAPLDR IHQELKQAFD
     PDGVFNPGRL YPGL
//
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