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Database: UniProt
Entry: G2E6G5_9GAMM
LinkDB: G2E6G5_9GAMM
Original site: G2E6G5_9GAMM 
ID   G2E6G5_9GAMM            Unreviewed;       431 AA.
AC   G2E6G5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Flavodoxin/nitric oxide synthase {ECO:0000313|EMBL:EGV28326.1};
GN   ORFNames=ThidrDRAFT_3859 {ECO:0000313|EMBL:EGV28326.1};
OS   Thiorhodococcus drewsii AZ1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiorhodococcus.
OX   NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV28326.1, ECO:0000313|Proteomes:UP000004200};
RN   [1] {ECO:0000313|EMBL:EGV28326.1, ECO:0000313|Proteomes:UP000004200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ1 {ECO:0000313|EMBL:EGV28326.1,
RC   ECO:0000313|Proteomes:UP000004200};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA   Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT   "The draft genome of Thiorhodococcus drewsii AZ1.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC       hydrolase group 3 family. {ECO:0000256|ARBA:ARBA00007121}.
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:EGV28326.1}.
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DR   EMBL; AFWT01000040; EGV28326.1; -; Genomic_DNA.
DR   RefSeq; WP_007042572.1; NZ_AFWT01000040.1.
DR   AlphaFoldDB; G2E6G5; -.
DR   STRING; 765913.ThidrDRAFT_3859; -.
DR   PATRIC; fig|765913.3.peg.3926; -.
DR   eggNOG; COG0426; Bacteria.
DR   Proteomes; UP000004200; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd07709; flavodiiron_proteins_MBL-fold; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR045761; ODP_dom.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR016440; Rubredoxin-O_OxRdtase.
DR   PANTHER; PTHR43717; ANAEROBIC NITRIC OXIDE REDUCTASE FLAVORUBREDOXIN; 1.
DR   PANTHER; PTHR43717:SF1; ANAEROBIC NITRIC OXIDE REDUCTASE FLAVORUBREDOXIN; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF19583; ODP; 1.
DR   PIRSF; PIRSF005243; ROO; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; Iron {ECO:0000256|ARBA:ARBA00023004}.
FT   DOMAIN          275..413
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   431 AA;  47998 MW;  74435059B07D4CD8 CRC64;
     MTHLPSTSRN GMAEATEAVE IRPGLHWIGA LDPGLRTFDI ILRTANGTTY NSYLVRGSDG
     VAVIDTVKAE FADDFFARLE SVARYDEIKV IVLNHLEPDH TGALPELMRR APQARLHIST
     RAPAMLKALL KPSEEHPLEY QAVDTGDEVS LGDRTLRFLH TPFLHWPDTQ CTYLVEEATL
     FSGDVFGCHH CDSRMFNEQC GDFRFAFDYY YAHIMRPFKT HVMDALKLIE PLPLQIIAPT
     HGPILRDRPR RYLTRYRELS TSTFAERIGN EEPTLVVFYM SSYGNTARMA ESIRTGAEEA
     GARVSLYDLE GGEIQPFVDL VESADALAFG SPTINGDAVK PIWDLLSSLA VIELKGKLGA
     AFGSYGWTGE AVRMIEDRMR GLKMRVPVAG LRIKLIPTDE ELAECRDFGR ALASAIVSGE
     KGRVIDFADL G
//
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