ID B9L560_THERP Unreviewed; 335 AA.
AC B9L560;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Xylene monooxygenase electron transfer subunit {ECO:0000313|EMBL:ACM06651.1};
GN OrderedLocusNames=trd_A0924 {ECO:0000313|EMBL:ACM06651.1};
OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OG Plasmid Tros {ECO:0000313|Proteomes:UP000000447}.
OC Bacteria; Thermomicrobiota; Thermomicrobia; Thermomicrobiales;
OC Thermomicrobiaceae; Thermomicrobium.
OX NCBI_TaxID=309801 {ECO:0000313|EMBL:ACM06651.1, ECO:0000313|Proteomes:UP000000447};
RN [1] {ECO:0000313|EMBL:ACM06651.1, ECO:0000313|Proteomes:UP000000447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27502 / DSM 5159 / P-2
RC {ECO:0000313|Proteomes:UP000000447};
RC PLASMID=Tros {ECO:0000313|Proteomes:UP000000447};
RX PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA Eisen J.A.;
RT "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT Thermomicrobium roseum.";
RL PLoS ONE 4:E4207-E4207(2009).
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DR EMBL; CP001276; ACM06651.1; -; Genomic_DNA.
DR RefSeq; WP_012642638.1; NC_011961.1.
DR AlphaFoldDB; B9L560; -.
DR KEGG; tro:trd_A0924; -.
DR eggNOG; COG0543; Bacteria.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_7_0_0; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000000447; Plasmid Tros.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Monooxygenase {ECO:0000313|EMBL:ACM06651.1};
KW Oxidoreductase {ECO:0000313|EMBL:ACM06651.1};
KW Plasmid {ECO:0000313|EMBL:ACM06651.1}.
FT DOMAIN 11..101
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 104..208
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 335 AA; 36756 MW; 2DCB516357A2308F CRC64;
MTVRRFLSTA SRSTLVVGPY RIPVADGETL LDALRRSGLW VPYECGWGSC GTCKAQLLSG
EIRYRSRPSC LRPHDHRLHR IALCVAEAVS DEIAVKPLRV SHEPQPHLAT LDAVATLTDR
YWLADDLFEL TLSLDRPVDY RPGQYAILEL GGARRCYSML DPAPTEGARC LRFLLRVLPG
GALTPQLAEL PMGSELPVQV PYGGAYLRPA RSYLFVAGGT GIAPILAIVR ALSPTERKQA
RLLYGAATPR HLAYLDELRM LLGHQNVIVS VDRPTGSWRE RVGPITLALP GILSETDREH
VRCYLAGPPG MLAAAEEQIR AAGIEANRIH VDAFA
//
