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Database: UniProt
Entry: I2DQC6_9BURK
LinkDB: I2DQC6_9BURK
Original site: I2DQC6_9BURK 
ID   I2DQC6_9BURK            Unreviewed;      1339 AA.
AC   I2DQC6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=FAD/FMN-containing dehydrogenase {ECO:0000313|EMBL:AFJ86852.1};
GN   ORFNames=MYA_2492 {ECO:0000313|EMBL:AFJ86852.1};
OS   Burkholderia sp. KJ006.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=416344 {ECO:0000313|EMBL:AFJ86852.1, ECO:0000313|Proteomes:UP000010108};
RN   [1] {ECO:0000313|EMBL:AFJ86852.1, ECO:0000313|Proteomes:UP000010108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KJ006 {ECO:0000313|EMBL:AFJ86852.1,
RC   ECO:0000313|Proteomes:UP000010108};
RX   PubMed=22843575; DOI=10.1128/JB.00821-12;
RA   Kwak M.J., Song J.Y., Kim S.Y., Jeong H., Kang S.G., Kim B.K., Kwon S.K.,
RA   Lee C.H., Yu D.S., Park S.H., Kim J.F.;
RT   "Complete Genome Sequence of the Endophytic Bacterium Burkholderia sp.
RT   Strain KJ006.";
RL   J. Bacteriol. 194:4432-4433(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP003514; AFJ86852.1; -; Genomic_DNA.
DR   RefSeq; WP_014723624.1; NC_017920.1.
DR   KEGG; buk:MYA_2492; -.
DR   PATRIC; fig|416344.3.peg.2535; -.
DR   HOGENOM; CLU_262983_0_0_4; -.
DR   Proteomes; UP000010108; Chromosome 1.
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}.
FT   DOMAIN          191..427
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1339 AA;  148676 MW;  9D9F99B18EA0F428 CRC64;
     MNAPQVFDPH GAATAVAADP APRLREIPYN YTSFSDREIV IRLLGEDAWS VLDELRAERR
     TGRSARMLYE VLGDIWVVRR NPYLQDDLLD NPKRRALLIE ALNHRLTEIG KRRRADLTEH
     RDDAGRERAG RVEMLEAAAQ RAVDEFADEF DKMADLRRRA TKALGRCTQK DNIRFDGLSR
     VSHVTDATDW RVEYPFVVLT PDTEAEIAAL IKACFELGLT VIPRGGGTGY TGGAVPLTPF
     SAVINTEKLE QLGAVELTEL PGVAHKVPTI FSGAGVVTRR VTEAAEAAGY VFAVDPTSLD
     ASCIGGNVAM NAGGKKAVLW GTALDNLAWW RMVDPDGNWL EVTRHEHNQG KIHDIAVARF
     ELKWFDGAYA PGEKLLRTEM LEIEGRRFRK EGLGKDVTDK FLAGLPGVQK EGCDGLITSA
     RWVLHKMPAH TRTVCLEFFG QAREAIPSIV EIKDYLFETA KQGGAILAGL EHLDERYLRA
     VGYATKSKRN AFPKMVLIGD IVGDDADAVA QATSEVIRMA NGKSGEGFVA VSAEARKRFW
     LDRSRTAAIA KHTNAFKINE DVVIPLNRMG EYTDGIERIN IELSLKNKLQ LVDALEAFFR
     GGNLPLGKTD DANEIPSAEL LEDRVQQALE LLKRVRARWE FVRDRLDQPL REAQHYLVQL
     GYEALAEKFA DRADEQPGAS VFHVTQDRTI RISWKQEIRA ELRAIFNGGA FKPILDEAQA
     IHKRVLRGRV FVALHMHAGD GNVHTNIPVN SDNYEMLQDA HAAVARIMTL ARSLDGVISG
     EHGIGITKLE FLTDDEIAEF RAYKQRVDPN GRFNKGKLLD GADLRNAYTP SFGLMGYESL
     IMQQSDIGAI ADSVKDCLRC GKCKPVCATH VPRANLLYSP RNKILATSLL VEAFLYEEQT
     RRGVSIKHWD EFNDVADHCT VCHKCATPCP VKIDFGDVTM NMRNLLRKMG KKKFNAGNAA
     GMFFLNATNP QTINAARTVM MGVGYKVQRF ANDMLKKVVT KQTQHPPATT GRPPVVEQVI
     HFVNKKMPGN LPKKTARALL DIEDNKIVPI IRNPKSTTVD SEAVFYFPGC GSERLFSQVG
     LATQAMLWEA GVQTVLPPGY LCCGYPQRGS GQYDKAEKIV TDNRVLFHRV ANTLNYLDIK
     TVVVSCGTCY DQLAGYEFDK IFPGCRIIDI HEFLLEKGMK LDGVTGTRYM YHDPCHTPIK
     TMDPVKLVNE LMGAEKDGYR IEKNDRCCGE SGTLAVTRPD VSTQVRFRKE EEIRKGAAKL
     RGIPVMADGA PAPAAASGPD VKILTSCPSC LQGLSRYNED ANLEADYIVV EIARQVLGEN
     WMADYVARAN NGGIERVLV
//
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