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Database: UniProt
Entry: A0A0Q6X1G3_9BURK
LinkDB: A0A0Q6X1G3_9BURK
Original site: A0A0Q6X1G3_9BURK 
ID   A0A0Q6X1G3_9BURK        Unreviewed;      1292 AA.
AC   A0A0Q6X1G3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KQV94591.1};
GN   ORFNames=ASC87_26205 {ECO:0000313|EMBL:KQV94591.1};
OS   Rhizobacter sp. Root1221.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX   NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQV94591.1, ECO:0000313|Proteomes:UP000051465};
RN   [1] {ECO:0000313|EMBL:KQV94591.1, ECO:0000313|Proteomes:UP000051465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1221 {ECO:0000313|EMBL:KQV94591.1,
RC   ECO:0000313|Proteomes:UP000051465};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV94591.1, ECO:0000313|Proteomes:UP000051465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1221 {ECO:0000313|EMBL:KQV94591.1,
RC   ECO:0000313|Proteomes:UP000051465};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQV94591.1}.
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DR   EMBL; LMDI01000027; KQV94591.1; -; Genomic_DNA.
DR   RefSeq; WP_056665785.1; NZ_LMDI01000027.1.
DR   STRING; 1736433.ASC87_26205; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000051465; 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:InterPro.
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; 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; 2.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051465}.
FT   DOMAIN          183..377
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1292 AA;  143213 MW;  CE6722381B8086BC CRC64;
     MNAPLPLNHI AAAADAAHHA PRLREIPYNY TSFSDREIVI RILGPRAWEL LNRLREERRT
     GRSARMLYEV IGDVWVVQRN PYLQDDLLDN PKRRGQLIEA LNHRLNEVQH RRDPAADQER
     DASVGELLDA ASRAVKAFAD QFKQVAELRR RATKVLGRHT AKDNIKFDGL SRVAHVTDAT
     DWRVEYPFVV LTPDTEAEMA ALVKHCIELG LTIIPRGGGT GYTGGAVPLT WNSAVINTEK
     LEAMTEVEHV RLPGLDRDVA TIWTEAGVVT QRVADAAERA GFVFAVDPTS AEASCVGGNV
     AMNAGGKKAV LWGTALDNLV SWRMVTPEAK WLEVTRLDHN LGKIHDVAVA TFELKYFDAS
     GKTLERVERL EVPGRTFRKE GLGKDVTDKF LAGLPGIQKE GCDGLITSCR WVVHKMPAHT
     RTVCLEFFGN AKDAVPSIVE IKDFMFAEAK AGGAILAGLE HLDDRYLKAV GYATKSKRGG
     LPKMVLVGDI AGDDADVVAR ATSEVVRLAN GRAGEGFVAV SADARKKFWL DRKRTAAISK
     HTNAFKVNED VVIPLPRMGE YTNGIERINI ELSLRNKLAL VDALEDFFLK GNLPLGKSDD
     AGEIASAELL EDRVQQALAM LRDVRSLWQQ WLHQLDVEQA DNGRTFFFDL QDHTLRASWK
     TQIRGPLQRI FAGSALSPIV DACVRIHKEV LRGRVWVALH MHAGDGNVHT NIPVNSDNYE
     MLQTAHEAVA RIMVLARSLD GVISGEHGIG ITKLEFLTDD ELRDFTDYKQ RIDPEGRFNK
     GKLLRGAGLK ADLTNAYTPS FGLMGHESLI MQQSDIGDIA NSMKDCLRCG KCKPVCATHV
     PRANLLYSPR NKILATSLLV EAFLYEEQTR RGVSIKHWEE FEDVADHCTV CHKCLTPCPV
     KIDFGDVSMN MRNLLTKMGK KSFRPGNKMA MMMLNATNPE TIKLLRMGMV DVGFKAQRLA
     NNLLRGLAKK QTAAPRSTVG TAPIKEQVIH FINKKLPGGL PKKTARALLD IEDKDYVPII
     RDPKATTAET EAVFYFPGCG SERLFSQVGL ATQAMLWHAG VQTVLPPGYL CCGYPQRGSG
     QFDKADKIIT DNRVLFHRVA NTLNYLDIKT VVVSCGTCYD QLQGYQFDKI FPGCRIIDIH
     EYLLEKGITL QGQGGYLYHD PCHTPMKLQD PMKTVKALVG DNVLKSERCC GESGTLGVTR
     PDVATQIRFR KEEELKKNEA ALRATGAEGD LKILTSCPSC LQGLSRYGND LNNGLLEADY
     IVVEMANKIL GPDWMPDYVK RANDGGIERV LV
//
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