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Database: UniProt
Entry: F4XWR7_9CYAN
LinkDB: F4XWR7_9CYAN
Original site: F4XWR7_9CYAN 
ID   F4XWR7_9CYAN            Unreviewed;       582 AA.
AC   F4XWR7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Uncharacterized flavoprotein {ECO:0000313|EMBL:EGJ31027.1};
GN   ORFNames=LYNGBM3L_44810 {ECO:0000313|EMBL:EGJ31027.1};
OS   Moorena producens 3L.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Moorena.
OX   NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ31027.1, ECO:0000313|Proteomes:UP000003959};
RN   [1] {ECO:0000313|Proteomes:UP000003959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX   PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA   Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA   Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA   Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA   Gerwick W.H., Gerwick L.;
RT   "Genomic insights into the physiology and ecology of the marine filamentous
RT   cyanobacterium Lyngbya majuscula.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(2011).
CC   -!- FUNCTION: Mediates electron transfer from NADH to oxygen, reducing it
CC       to water. This modular protein has 3 redox cofactors, in other
CC       organisms the same activity requires 2 or 3 proteins.
CC       {ECO:0000256|ARBA:ARBA00025633}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavodoxin
CC       reductase family. {ECO:0000256|ARBA:ARBA00006098}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC       hydrolase group 3 family. {ECO:0000256|ARBA:ARBA00007121}.
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DR   EMBL; GL890944; EGJ31027.1; -; Genomic_DNA.
DR   RefSeq; WP_008187904.1; NZ_MKZR01000001.1.
DR   AlphaFoldDB; F4XWR7; -.
DR   eggNOG; COG0426; Bacteria.
DR   eggNOG; COG1853; Bacteria.
DR   HOGENOM; CLU_017490_2_1_3; -.
DR   OrthoDB; 9807946at2; -.
DR   Proteomes; UP000003959; 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:0016646; F:oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor; IEA:UniProt.
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; IPR002563; Flavin_Rdtase-like_dom.
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; IPR012349; Split_barrel_FMN-bd.
DR   PANTHER; PTHR32145; DIFLAVIN FLAVOPROTEIN A 2-RELATED; 1.
DR   PANTHER; PTHR32145:SF32; DIFLAVIN FLAVOPROTEIN A 4-RELATED; 1.
DR   Pfam; PF01613; Flavin_Reduct; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF19583; ODP; 1.
DR   SMART; SM00903; Flavin_Reduct; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF50475; FMN-binding split barrel; 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   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   DOMAIN          268..406
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   582 AA;  64076 MW;  1AD2E40E61BDB6BA CRC64;
     MNTTKPRDVQ PLYIATDTLI LRSRTWDRLK FEIEYALQRG TTANSFVIRA DQIALFDPPG
     ESFTEVFLKA LQERLDPKLI DYVILGHINP NRLVTLNALL KLAPNITFVC SNPGAKSLRT
     LFEKLEDKAI PEQELKILVM KGDDTLDLGK GHILDFIPTP NPRFPDQLCT YDSKTQILFT
     DKLFGAHVCG DQVMDEGWRV YDEDRRYYFD CLMAPHARQV ETALAKLDDF DAKLYATGHG
     PLVRYGFQEL TESYGKWSKQ QQAQEANVAL IYASAYGNTG AIAQAIARGI TKAGVSVESL
     NCEAADPEEI GAAVEKADGF IMGSPTLGGH APTQVQTALG MVLSSATKTK LAGVFGSYGW
     SGEAIDLLES KFRDAGYKFG FETIRVKFKP TDKDLKYCEE AGTDFAQALK KAKKARKPKQ
     PAGESSAART EQAVGRLIGS LCVVTTKQQD LTGAMLASWV SQATFTPPGL TVAVAKERAV
     ESLMHTGDNF VLNVLEDGKH LPLMKQFLKP FGPGEDRFGG IKIEESENGC PILSDALAYL
     ECTVENRMEC GDHWLVYGVV KNGKVLSDGV TALHHRKSGT YY
//
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