ID Q81AM1_BACCR Unreviewed; 154 AA. AC Q81AM1; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 24-JUL-2024, entry version 114. DE RecName: Full=Flavodoxin {ECO:0000256|RuleBase:RU367037}; GN OrderedLocusNames=BC_3541 {ECO:0000313|EMBL:AAP10475.1}; OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP10475.1, ECO:0000313|Proteomes:UP000001417}; RN [1] {ECO:0000313|EMBL:AAP10475.1, ECO:0000313|Proteomes:UP000001417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB RC 9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417}; RX PubMed=12721630; DOI=10.1038/nature01582; RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G., RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.; RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus RT anthracis."; RL Nature 423:87-91(2003). RN [2] {ECO:0007829|PDB:6GAQ} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH CA(2+) AND FMN. RX PubMed=30142264; DOI=10.1021/acs.biochem.8b00674; RA Gudim I., Hammerstad M., Lofstad M., Hersleth H.P.; RT "The Characterization of Different Flavodoxin Reductase-Flavodoxin (FNR- RT Fld) Interactions Reveals an Efficient FNR-Fld Redox Pair and Identifies a RT Novel FNR Subclass."; RL Biochemistry 57:5427-5436(2018). CC -!- FUNCTION: Low-potential electron donor to a number of redox enzymes. CC {ECO:0000256|RuleBase:RU367037}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|ARBA:ARBA00001917, CC ECO:0000256|RuleBase:RU367037}; CC -!- SIMILARITY: Belongs to the flavodoxin family. CC {ECO:0000256|ARBA:ARBA00005267, ECO:0000256|RuleBase:RU367037}. 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; AE016877; AAP10475.1; -; Genomic_DNA. DR RefSeq; NP_833274.1; NC_004722.1. DR PDB; 6GAQ; X-ray; 2.50 A; A/B=1-154. DR PDBsum; 6GAQ; -. DR AlphaFoldDB; Q81AM1; -. DR SMR; Q81AM1; -. DR KEGG; bce:BC3541; -. DR PATRIC; fig|226900.8.peg.3635; -. DR HOGENOM; CLU_051402_4_2_9; -. DR Proteomes; UP000001417; Chromosome. DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:UniProt. DR Gene3D; 3.40.50.360; -; 1. DR InterPro; IPR010087; Flav_short. DR InterPro; IPR001094; Flavdoxin-like. DR InterPro; IPR050619; Flavodoxin. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR029039; Flavoprotein-like_sf. DR NCBIfam; TIGR01753; flav_short; 1. DR PANTHER; PTHR42809:SF1; FLAVODOXIN 1; 1. DR PANTHER; PTHR42809; FLAVODOXIN 2; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR SUPFAM; SSF52218; Flavoproteins; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:6GAQ}; Calcium {ECO:0007829|PDB:6GAQ}; KW Electron transport {ECO:0000256|RuleBase:RU367037}; KW Flavoprotein {ECO:0000256|RuleBase:RU367037, ECO:0007829|PDB:6GAQ}; KW FMN {ECO:0000256|RuleBase:RU367037, ECO:0007829|PDB:6GAQ}; KW Metal-binding {ECO:0007829|PDB:6GAQ}; KW Nucleotide-binding {ECO:0007829|PDB:6GAQ}; KW Reference proteome {ECO:0000313|Proteomes:UP000001417}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367037}. FT DOMAIN 11..151 FT /note="Flavodoxin-like" FT /evidence="ECO:0000259|PROSITE:PS50902" FT BINDING 17 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6GAQ" FT BINDING 18 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6GAQ" FT BINDING 19 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6GAQ" FT BINDING 21 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6GAQ" FT BINDING 22 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6GAQ" FT BINDING 65 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6GAQ" FT BINDING 69 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6GAQ" FT BINDING 99 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6GAQ" FT BINDING 104 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6GAQ" FT BINDING 106 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6GAQ" FT BINDING 131 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:6GAQ" FT BINDING 133 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:6GAQ" FT BINDING 139 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:6GAQ" SQ SEQUENCE 154 AA; 16939 MW; 95A1B6950744AF87 CRC64; MLEGDAKVAK ILIAYASMSG NTESIADLIK VSLDAFDHEV VLQEMEGMDA EELLAYDGII LGSYTWGDGE LPFEAEDFHD DLENIDLAGK KVAVFGSGDT AYELFCEAVT IFEERLVERG AELVQEGLKI ELAPEDEEDV EKCSNFAIAF AEKF //