ID K9YHQ6_HALP7 Unreviewed; 570 AA.
AC K9YHQ6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Flavin reductase domain protein FMN-binding protein {ECO:0000313|EMBL:AFZ45925.1};
GN OrderedLocusNames=PCC7418_3821 {ECO:0000313|EMBL:AFZ45925.1};
OS Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Halothecacae; Halothece cluster; Halothece.
OX NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ45925.1, ECO:0000313|Proteomes:UP000010481};
RN [1] {ECO:0000313|Proteomes:UP000010481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003945; AFZ45925.1; -; Genomic_DNA.
DR RefSeq; WP_015227796.1; NC_019779.1.
DR AlphaFoldDB; K9YHQ6; -.
DR STRING; 65093.PCC7418_3821; -.
DR KEGG; hao:PCC7418_3821; -.
DR PATRIC; fig|65093.3.peg.4034; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1853; Bacteria.
DR HOGENOM; CLU_017490_2_1_3; -.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000010481; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000010481};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 257..395
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 570 AA; 62819 MW; 5A859C7DB0348064 CRC64;
MQPRDTQVLP IAAQTTVYRS RTWERLKFEI EYGLQRGTTA NSYLIQGDKT ALFDPPGESF
TEIFLTALKQ RISLSDIDYI ILGHVNPNRA ETLKAILKII PDVTLVCSNP AAISLQKLLG
ETSVNYQVIK GEETLDLGQG HCLEFLLTPT PRWSDQLCTY DPKTGILLTD KFFGAHVCGE
QIFDEGWQVY QEDRRYYFDC LMAPHASQVE SILDKFQGKS AQIYGTGHGP IVRYGFHELT
NAYREWLQGQ QSQATKVALL YASAYGNTAT IANAIARGVT KAGVAVESIN CEFTDPETIK
SVLQNTTGFI IGSPTLGGHA PTQVQTALGV ILSNAEKNQL AGVFGSYGWS GEAIDLLEQK
IKDAGFRFGF DPIRVKFKPT DSTLKYCEEA GTDFAQKVKR KQKKQVARQN VTDSQAARTE
QALGRVVGAL CVVTAQKGEL ANGMLASWVS QATFSPPGVT VAVAKERAIE SLMHVGSPFV
LNILPEGKQL QKQFMKNYSP GEDRFAGIET EEAENGCPIL KQALAYLELQ VQNRMECGDH
WLVYGVAKSG KVLDTEKVTA VHHRNSGSHY
//
