ID Q12F78_POLSJ Unreviewed; 1300 AA.
AC Q12F78;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=FAD linked oxidase-like protein {ECO:0000313|EMBL:ABE42814.1};
GN OrderedLocusNames=Bpro_0858 {ECO:0000313|EMBL:ABE42814.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE42814.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000316; ABE42814.1; -; Genomic_DNA.
DR RefSeq; WP_011481816.1; NC_007948.1.
DR STRING; 296591.Bpro_0858; -.
DR KEGG; pol:Bpro_0858; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_262983_0_0_4; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000001983; Chromosome.
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:UP000001983}.
FT DOMAIN 184..417
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 1300 AA; 144473 MW; FE3A6991539D9F4F CRC64;
MNAPTTLQEL NVFADDAKPG EARIREIPYN YTSFSDREVV IRLLGAPAWD LLNRLRDERR
TGRSARMLYE VLGDIWVVQR NPYLQDDLLD NPKRRKLLVD ALHHRLSEVG KRRTPDADPQ
RDAIVGELLD AARSAVSRFS ASFEEVAGLR RQTERKLRKL TLKDNIKFDG LSRVSHVTDA
TDWRVEYPFV VLTPDSEQEM AGLVKGCIDL GLTIVPRGGG TGYTGGAIPL TWKSAVINTE
KLEAMTEVEM VSLPGIAQPV ATVWTEAGVV TQRVADAAER GGFVFAVDPT SAEASCIGGN
IAMNAGGKKA VLWGTALDNL ASWRMVTPQA QWLEVTRLGH NLGKIHDAEM ASFELKYFEA
DGKTPVRTER LDIQGKTFRK EGLGKDVTDK FLSGLPGIQK EGCDGLITSA RWIVHRMPAH
TRTVCLEFFG NAKDAVPSIV EIKDFMFSEQ KRGGAILAGL EHLDDRYLKA VGYATKSKKH
GGLPKMVLFG DIAGDDADVV ARATSEVVRI ANSRHGEGFI AISPDARKKF WLDRKRTAAI
SRHTNAFKIN EDVVIPLPRM AEYTDGIERI NIELSLRNKI KLCDELETFF LKGNLPLGKS
DDANDIPSAE LLEDRVGQAL AMIAEVRALW AGWLEGVEAL FPQLQDHSLR ASWKTQIRAR
LQAIFSGAPF LPILEECNAI HKRVLKGRVW AALHMHAGDG NVHTNLPVNS DDYEMLQTAH
EAVARIMVLA RSLDGVISGE HGIGITKLDF LTDEELRPFT EYKQKVDPEG RFNKGKLLRN
QELNTQDGKR LPADLTNAYT PSFGLMGHES LIMQQSDIGA IADSIKDCLR CGKCKPVCAT
HVPRANLLYS PRNKILATSL LVEAFLYEEQ TRRGISIKHW EEFEDVADHC TVCHKCLTPC
PVDIDFGDVS MNMRNLLRKM GQKSFRPGNA AAMFFLNATN PQTIKFMRGA MVDVGFKAQR
LANDLLRKLA RKQTDRPPAT VGKAPVKEQV IHFINKKMPG GLPKKTARAL LDIEDKDYVP
IIRNPKNTTA ETEAVFYFPG CGSERLFSQV GLATQAMLWH AGVQTVLPPG YLCCGYPQRG
SGQYDKAEKI ITDNRVLFHR VANTLNYLDI KTVVVSCGTC YDQLQGYEFE KIFPGCRIID
IHEYLLEKGI TLRTDQPGKG YLYHDPCHSP MKLQEPMKTV KALLGDNVLK NERCCGESGT
LGVTRPDIST QIRFRKEEEL RKGEANLRAT GAVGEGENVK ILTSCPSCLQ GLSRYGDDLQ
NGLLEADYIV VEMANQILGK EWLPAYVEAA NHGGIERVLV
//
