ID G8RIG1_MYCRN Unreviewed; 845 AA.
AC G8RIG1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=2-polyprenylphenol hydroxylase-like oxidoreductase {ECO:0000313|EMBL:AEV74676.1};
GN OrderedLocusNames=MycrhN_4174 {ECO:0000313|EMBL:AEV74676.1};
OS Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV74676.1, ECO:0000313|Proteomes:UP000005442};
RN [1] {ECO:0000313|EMBL:AEV74676.1, ECO:0000313|Proteomes:UP000005442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB3 {ECO:0000313|EMBL:AEV74676.1,
RC ECO:0000313|Proteomes:UP000005442};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003169; AEV74676.1; -; Genomic_DNA.
DR RefSeq; WP_014212426.1; NC_016604.1.
DR AlphaFoldDB; G8RIG1; -.
DR STRING; 710685.MycrhN_4174; -.
DR KEGG; mrh:MycrhN_4174; -.
DR PATRIC; fig|710685.3.peg.4187; -.
DR eggNOG; COG0543; Bacteria.
DR eggNOG; COG0654; Bacteria.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_023917_0_0_11; -.
DR OrthoDB; 4307358at2; -.
DR Proteomes; UP000005442; Chromosome.
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; cd06209; BenDO_FAD_NAD; 1.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; IPR047683; BenC-like_FAD_NAD-bd.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43422; THIAMINE THIAZOLE SYNTHASE; 1.
DR PANTHER; PTHR43422:SF3; THIAMINE THIAZOLE SYNTHASE; 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; SSF51905; FAD/NAD(P)-binding domain; 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 Reference proteome {ECO:0000313|Proteomes:UP000005442}.
FT DOMAIN 4..95
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 102..204
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 845 AA; 94111 MW; 6A633380AB2F7A16 CRC64;
MDAHQITVRY SDGTQKNMPV QPDQSILDAA EEHGVAIVNE CQSGICGTCV ATCTSGDYEM
GRTEGLSDVE RAARKILTCQ TFAESDCEID LQYPVDDNAA RLVTGCGVVT AVSQLSSTTA
ILRVDVSGMA DSIVYKAGQF AQLQIPGTEA WRNYSYAHPC DGRDELEFII RLLPDGVMSN
YLRDRAKPGD RIALRCSKGG FYLRPVVRPV ILVAGGTGLS AVLAMAQSLD ADIGQPVHLL
YGVTTSEDLC KLDELEALTK RIPGLTVQTI VSQAGVDWDG PVGLVTDLLD ADMLEDDDAD
IYLCGPSAMV EATRNWLDSN GIHRIGLYYE KFVPSGATRR RTPARLDYSQ LDLADVRRRG
QRTAVVIGGS IAGIAAAKVL SESFERVIVL EKDGRHSRRE GRPGAAQGWH LHHLLTAGQI
ELERIFPGIV DDMVREGAFK VDMADQYRIR LGGTWKKPGT SDIQIVCAGR PLLEWCVRRR
LDGENRIEFR YEAEVGDLVY DRGSNTVIGV AIDRDGELDV VPAEFVVDAS GKNTRIPEFL
DRIGIGAPEV EQDIINCFYS TMQHHVPPER QWQDKVMVIC YAYRPYEDTY AAQYYTDSSR
TILSTSLVAY NCYSPPRTAQ EFREFANLMP SPVVGENIDG LEPASPIYNF RYPNMLRLRY
EKKNNLPRAL LVVGDAYTSA DPVSGLGMSL ALKEVREMQL LLARYGAGHA ELPRRYYRKI
SKMADTAWFV IREQNLRFDW IKGVRDKRPF YFGALTWYMD RVLELVHDDL DTYREFLAVV
HLVKPPAALM MPKVAGRVLG KWARTRLSGQ KTLIERNYSD RTVPGVDHLI QTDQMAVGLA
GTPTH
//
