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Database: UniProt
Entry: A0A069PW75_9BURK
LinkDB: A0A069PW75_9BURK
Original site: A0A069PW75_9BURK 
ID   A0A069PW75_9BURK        Unreviewed;      1366 AA.
AC   A0A069PW75;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KDR44780.1};
GN   ORFNames=BG61_01015 {ECO:0000313|EMBL:KDR44780.1};
OS   Caballeronia glathei.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=60547 {ECO:0000313|EMBL:KDR44780.1, ECO:0000313|Proteomes:UP000027466};
RN   [1] {ECO:0000313|EMBL:KDR44780.1, ECO:0000313|Proteomes:UP000027466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 50014 {ECO:0000313|EMBL:KDR44780.1,
RC   ECO:0000313|Proteomes:UP000027466};
RA   Liu X.Y., Li C.X., Xu J.H.;
RT   "Draft Genome Sequences of Four Burkholderia Strains.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KDR44780.1}.
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DR   EMBL; JFHC01000001; KDR44780.1; -; Genomic_DNA.
DR   RefSeq; WP_035941238.1; NZ_JFHC01000001.1.
DR   Proteomes; UP000027466; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR021817; DUF3400.
DR   InterPro; IPR022153; DUF3683.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; IPR009051; Helical_ferredxn.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   Pfam; PF02754; CCG; 2.
DR   Pfam; PF11880; DUF3400; 1.
DR   Pfam; PF12447; DUF3683; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 2.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027466}.
FT   DOMAIN          191..427
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1366 AA;  151024 MW;  7E8BFCF87E680F50 CRC64;
     MNAPQAFDPN GAAAAVALDV EPRLREIPYN YTSFSDREIV MRLLGDEAWA ALDELRSERR
     TGRSARMLYE VLGDIWVVRR NPYLQDDLLD NPKRRALLVE ALNHRLHEIE KRRKDDLSSH
     GDVAGRDRAA RVEVLVSAAR RAVDDFAAEF GRMAELRRRA SKVLGKCTQK DNIKFDGLSR
     VSHVTDATDW RVEYPFVVLT PDTEAEIAGL IKACFELGLT VIPRGGGTGY TGGAIPLTPF
     AAVINTEKLE QLGPVEMTDL PGVDRKVATI FSGAGVVTRR VTEAAEQAGF VFAVDPTSLD
     ASCVGGNVAM NAGGKKAVLW GTALDNLAWW RMVDPEGNWL EVTRLDHNLG KIHDIEVARF
     RLDWFDGSRA PGEKLIRTES LDIAGRTFRK EGLGKDVTDK FLSGLPGVQK EGCDGLITSA
     RWILHKMPAN TRTVCLEFFG QARDAIPSIV EIKDYLFETS KQGGAILAGL EHLDERYLRA
     VGYATKSKRN AFPKMVLIGD IVGDDADAVA HATSEVVRMA NGKSGEGFVA VNAEARKRFW
     LDRSRTAAIA KHTNAFKINE DVVIPLNRMG EYTDGIERIN IELSIKNKLQ LVDALEAFFR
     TGKLPLGKSD DANEIPSAEL LEDRVQQALD LLKRVKARWT FVGDKLDLPL REAQHYMVQL
     GYEALAEKLA DRVDAQPGAN VFHVAQDRTV RISWKQEIRA ELRQIFNGGE FKPILEEAQN
     IHKQVLRARV FVALHMHAGD GNVHTNIPVN SDNYEMLQDA HHAVARIMKL ARSLDGVISG
     EHGIGITKLE FLTEEEIGEF RAYKQRVDPN GRFNAGKLMA GADLRNAYTP SFGLMGYESL
     IMQQSDIGAI SDSIKDCLRC GKCKPVCATH VPRANLLYSP RNKILATSLL VEAFLYEEQT
     RRGVSIKHWD EFNDVADHCT VCHKCVTPCP VKIDFGDVTM NMRNLLRKMG KKKFNPGNAA
     GMFFLNATNP QTINLARTAM MGVGYKAQRV GHDLLKKFAK KQTANPPATV GKPPVVEQVI
     HFMNKKMPGN LPKKTARALL DIEDNKIVPI IRNPKATTVD SEAVFYFPGC GSERLFSQVG
     LATQAMLWEA GVQTVLPPGY LCCGYPQRGS GQYDKAEKIV TDNRVLFHRV ANTLNYLDIK
     TVVVSCGTCY DQLAGYEFEK IFPGCRIIDI HEFLLEKNIR LEGVKGTRYM YHDPCHSPIK
     TMDPVKLVND LMGAQNDGYR IEKNDRCCGE SGTLAVTRPD ISTQVRFRKE EEIRKGAAKL
     RDIPLVAQAG ANGSAAADLA NRAGNPAGVA PGPVQKAGDG AQPNGVDVKI LTSCPSCLQG
     LSRFNEDANI EADYIVVEIA RKVLGENWMA DYVARANDGG IERVLV
//
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