ID A0A073CHC3_PLAAG Unreviewed; 574 AA.
AC A0A073CHC3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Flavoprotein {ECO:0000313|EMBL:KEI67103.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:KEI67103.1};
GN ORFNames=A19Y_2141 {ECO:0000313|EMBL:KEI67103.1};
OS Planktothrix agardhii NIVA-CYA 126/8.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI67103.1, ECO:0000313|Proteomes:UP000027395};
RN [1] {ECO:0000313|EMBL:KEI67103.1, ECO:0000313|Proteomes:UP000027395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI67103.1,
RC ECO:0000313|Proteomes:UP000027395};
RX PubMed=24907328; DOI=10.1128/AEM.01188-14;
RA Christiansen G., Goesmann A., Kurmayer R.;
RT "Elucidation of insertion elements encoded on plasmids and in vitro
RT construction of shuttle vectors from the toxic cyanobacterium
RT Planktothrix.";
RL Appl. Environ. Microbiol. 80:4887-4897(2014).
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; CM002803; KEI67103.1; -; Genomic_DNA.
DR RefSeq; WP_026796440.1; NZ_CM002803.1.
DR AlphaFoldDB; A0A073CHC3; -.
DR STRING; 388467.A19Y_2141; -.
DR PATRIC; fig|388467.6.peg.2088; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1853; Bacteria.
DR HOGENOM; CLU_017490_2_1_3; -.
DR Proteomes; UP000027395; 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 Oxidoreductase {ECO:0000313|EMBL:KEI67103.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027395};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 261..399
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 574 AA; 63964 MW; CA00E7A5BB2437E9 CRC64;
MDNQKPRDVQ VFLIGNNTKI VRSRTWERLK FEVEYSLQRG TTANSYIIEA DQTAIIDPPG
ESFTQNYIEA LQTRVNLEQL NYIILGHFNA NRGATLKALL ELSPNITFVC SNPAALALRE
YFETENLKIL TIKGEETLDL GQCHQLQFVL TPTPRWPDAI LTYDQATEIL FSDKLFGAHV
CGDQVFDEGW SVYSDDRRFY YDCLHAAQAK YVLSNLDKIK ELPPIKFYGT GHGPLVKHGK
TELTNLYRDW SEKQKSQDLT VALLYASAYG NTATVAQAIA KGLTKSDIAV ELINCEYAKS
SEIQEALEKC DGFIIGSPTL GGHAPTQIQT ALGVILNTAS TNKLAGVFGS YGWSGEAIDL
LESRLKDAGY KFGFEPIRVK FTPTDVTLQT CKEAAIDFAQ TLKRTQKRRA FRPTATSAGA
DRTAQALGRV VGSLCVVSGR RGEMYSAMLA SWVSQATFNP PGFTVAVAKD RALEPLTHIG
DRFVLNILQE GKQLRKHFLK RFEPGENRFV DIETEETSTG CLILKDALAY LDCEVKNRME
CGDHWVIYAT VHQGQVLNSD GVTAVHYRKT GTQY
//
