ID K7WC21_9NOST Unreviewed; 606 AA.
AC K7WC21;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Flavoprotein {ECO:0000313|EMBL:AFW92928.1};
GN ORFNames=ANA_C10117 {ECO:0000313|EMBL:AFW92928.1};
OS Anabaena sp. 90.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=46234 {ECO:0000313|EMBL:AFW92928.1, ECO:0000313|Proteomes:UP000010101};
RN [1] {ECO:0000313|EMBL:AFW92928.1, ECO:0000313|Proteomes:UP000010101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90 {ECO:0000313|EMBL:AFW92928.1};
RX PubMed=23148582; DOI=10.1186/1471-2164-13-613;
RA Wang H., Sivonen K., Rouhiainen L., Fewer D.P., Lyra C., Rantala-Ylinen A.,
RA Vestola J., Jokela J., Rantasarkka K., Li Z., Liu B.;
RT "Genome-derived insights into the biology of the hepatotoxic bloom-forming
RT cyanobacterium Anabaena sp. strain 90.";
RL BMC Genomics 13:613-613(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003284; AFW92928.1; -; Genomic_DNA.
DR AlphaFoldDB; K7WC21; -.
DR STRING; 46234.ANA_C10117; -.
DR KEGG; anb:ANA_C10117; -.
DR PATRIC; fig|46234.3.peg.135; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1853; Bacteria.
DR HOGENOM; CLU_017490_2_1_3; -.
DR Proteomes; UP000010101; Chromosome chANA01.
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:UP000010101};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..606
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003912527"
FT DOMAIN 297..435
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 606 AA; 66527 MW; DFC57519F596A23E CRC64;
MKICPVPSKI GKLKILTFAP LLLCAFARNI IHTNHQSPMT TKPRDVQILP IGTDTIVLRS
RSWARLRFEI EYALAKGTTA NSYLIQGDKN ALLDPPGETF TEIYLQALQQ RFDVKKLDYV
ILGHINPNRA ATLKALLEIA PQITFVCSNP GAINLRAALE KDDLQILVMR GEDTLDLGKG
HHLQFIPTPN PRYADELCTW DRQTEILFSD KLFGAHICSD QVFDEGWEVF NEDRRYYFDC
LMAPHARQIE TALEKLADLP VRMYATGHGP IVRYGLIDIT KGYREWTKQQ TSADMTVALI
YASAYGNTAT LAQAIARGIT KAGVNVEAIN CEFTEPEEIK AAIEKSAGFV IGSPTLGGHA
PTPVQTALGI VLSTATNNKL AGVFGSFGWS GEAVDLIESK LKDAGYRFGF DTIRVKFKPN
EVTLQTCEEA GTDFAQALKR AAKKSVVAKQ PASNVEQAVG RIVGSICVVT ASQGDVKTGM
LASWVTQASF NPPGLTIAVA KERAMESLSY TNNKFVVNIL AEGKEIRKQF MKVYAPGQDR
FAGLDTQEAN NGGIILNGAL AYLECSVQSR MESGDHWLVY ATVDDGKVLN QDGVTAVHYR
KSASYY
//
