ID A0A0W0XV53_9GAMM Unreviewed; 627 AA.
AC A0A0W0XV53;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Oxidoreductase, FAD-binding protein {ECO:0000313|EMBL:KTD48442.1};
GN ORFNames=Lrub_0793 {ECO:0000313|EMBL:KTD48442.1};
OS Legionella rubrilucens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=458 {ECO:0000313|EMBL:KTD48442.1, ECO:0000313|Proteomes:UP000054608};
RN [1] {ECO:0000313|EMBL:KTD48442.1, ECO:0000313|Proteomes:UP000054608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA-270A-C2 {ECO:0000313|EMBL:KTD48442.1,
RC ECO:0000313|Proteomes:UP000054608};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
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:KTD48442.1}.
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DR EMBL; LNYT01000007; KTD48442.1; -; Genomic_DNA.
DR RefSeq; WP_058530916.1; NZ_LNYT01000007.1.
DR AlphaFoldDB; A0A0W0XV53; -.
DR STRING; 458.Lrub_0793; -.
DR PATRIC; fig|458.5.peg.826; -.
DR OrthoDB; 581532at2; -.
DR Proteomes; UP000054608; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06217; FNR_iron_sulfur_binding_3; 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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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:SF6; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR PRINTS; PR00371; FPNCR.
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 Coiled coil {ECO:0000256|SAM:Coils}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000054608};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 180..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 286..391
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 543..627
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 37..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 111..145
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 40..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 70097 MW; 260BC0C96DE3C5FB CRC64;
MRFQYIKKFI HLRWVQTFSI SFLLTVASVS FTQTTTEEHA AHHQGGEKEK EGEGMSGMMK
NIGTPSKDLY PSLMNLPTLS TEKRLAIQQM AHQRITSGIA LMKGGLNELL LASSKNDYVK
MQEALEKLRE GIAQYESALA ALRALSEGKN PRDIALQWFK REMNLLPSSP QARNVLGGPF
FHLTIIALFG LFFLVMIWMY FFKMRRAAAL LDRLTKQNAA APLDDSPQSS KAAEPTPSLS
VEPIKPSQVS KLPSETAPTT PPTCPAHKCP VPQFPVMRSL TEPEEKWEGT LRVCRIFQEA
PEIKTYHLAS LHEVALPFTY YPGQFITLTA VINGKTVRRS YTMASTPTQL HYCAITVKRE
EHGLFSRYLH DEIKEGDVLD VMGPNGKFTF TGEEAKSIVL ICGGVGITPM MSIIRYLTDI
GWHNDIYLLY CCRTTSEFLF REELEQLQER YLNLHVYASM LRSEGAVWMG LQGLFTKNII
SHLVPDIASH RIHVCGPPAM MDAILAILKE LNVPTDLILT EAFGPEKKPE IAQEDFVKAD
TRAMVSFRKS EKMVPILPDR TLLEIAEANG IAIDYACRTG QCGLCKVTLL SGEVTMACED
ALSKEDKQQG LILACQAKAT KNIEVDA
//
