ID A0A0J1CQ34_9BURK Unreviewed; 1362 AA.
AC A0A0J1CQ34;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KLU22772.1};
GN ORFNames=EOS_29020 {ECO:0000313|EMBL:KLU22772.1};
OS Caballeronia mineralivorans PML1(12).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU22772.1, ECO:0000313|Proteomes:UP000035963};
RN [1] {ECO:0000313|EMBL:KLU22772.1, ECO:0000313|Proteomes:UP000035963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX PubMed=26205858;
RA Uroz S., Oger P.;
RT "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT Ability.";
RL Genome Announc. 3:e00798-15(2015).
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:KLU22772.1}.
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DR EMBL; AEJF01000173; KLU22772.1; -; Genomic_DNA.
DR RefSeq; WP_047895635.1; NZ_AEJF01000173.1.
DR PATRIC; fig|908627.4.peg.6487; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000035963; 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}.
FT DOMAIN 191..427
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 1362 AA; 150701 MW; 519BDAE9BED1284B CRC64;
MNAPQAFDPN GAAHAVALDT EPRLREIPYN YTSFSDREIV IRLLGEEAWA ALAVLRSERR
TGRSARMLYE VLGDIWVVRR NPYLQDDLLD NPKRRALLIE ALNHRLSDIE KRRKADLSQH
QDDAGRGRAA RVEVLISAAC RAVEDFKKEF EQTYDLRKKA SKVLGRVTEK DNIKFDGLSR
VSHVTDATDW RVEYPFVVLT PDTEAEIAGM IKACFELGLT VIPRGGGTGY TGGAIPLTPF
AAVINTEKLE QLGPVEMTDL PGVDHKVATI FSGAGVVTRR VTEAAEQAGF VFAVDPTSLD
ASCVGGNVAM NAGGKKAVLW GTALDNLAWW RMVDPQGNWL EVTRLDHNCG KIHDIPVARF
RLDWFDGSRA PGEKLLRTES LDISGSKFRK EGLGKDVTDK FLSGLPGVQK EGCDGLITSA
RWILHKMPAH TRTVCLEFFG QARDAIPSIV EIKDFLFETS KQGGAILAGL EHLDERYLRA
VGYATKSKRN AFPKMVLIGD IVGNDPDAVA QATSEVVRMA NGKSGEGFVA VNAEARKRFW
LDRSRTAAIA KHTNAFKINE DVVIPLNRMG EYTDGIERIN IELSIKNKLQ LVDALETFFK
NGKLPLGKSD DANEIPSAEL LEDRVQQALD LLQRVRERWT FVGEKLDMPL REAQHYMVQL
GYEGLAEKMA DRVDSQPGVR VFDVAQDRTI RISWKQEIRA ELRHIFNGGE FKPILEEAQN
IHKTVLRGRV FVALHMHAGD GNVHTNIPVN SDNYEMLQDA HVAVARIMKL ARDLDGVISG
EHGIGITKLE FLTEDEIAEF REYKQRVDPN GRFNAGKLLA GADLRNAYTP SFGLMGYESL
IMQQSDIGAI ADSIKDCLRC GKCKPVCATH VPRANLLYSP RNKILATSLL VEAFLYEEQT
RRGVSIKHWD EFNDVADHCT VCHKCVTPCP VKIDFGDVTM NMRNLLRKMG KKKFNAGNAA
GMFFLNATNP QTINLARTAM MGVGYKAQRL GNDVLKKFTK KQTAKPPATV GKPAVTQQVI
HFMNKKMPGN LPKKTARALL DIEDNKIVPI IRNPKTTTSD TEAVFYFPGC GSERLFSQVG
LATQAMLWEA GVQTVLPPGY LCCGYPQRGA GQFDKAEKIV TDNRVLFHRV ANTLNYLDIK
TVVVSCGTCY DQLAGYEFEK IFPGCRIIDI HEFLLEKNIK LEGVTGTRYM YHDPCHSPIK
TMDPVKLVNE LMGSANDGYK IEKNDRCCGE SGTLAVTRPD ISTQVRFRKE EEIRKGAAKL
RDIPLLAEAG ANGSNLANAS AGTAGAAPGS VLKAGDAQST GTDVKILTSC PSCLQGLSRY
NEDANIEADY IVVEIARKVL GASWMEDYVA RANDGGIERV LV
//
