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-JAN-2024, entry version 111.
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).
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}.
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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 OMA; FETTIHN; -.
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: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; 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};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU367037};
KW Flavoprotein {ECO:0000256|RuleBase:RU367037};
KW FMN {ECO:0000256|RuleBase:RU367037};
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"
SQ SEQUENCE 154 AA; 16939 MW; 95A1B6950744AF87 CRC64;
MLEGDAKVAK ILIAYASMSG NTESIADLIK VSLDAFDHEV VLQEMEGMDA EELLAYDGII
LGSYTWGDGE LPFEAEDFHD DLENIDLAGK KVAVFGSGDT AYELFCEAVT IFEERLVERG
AELVQEGLKI ELAPEDEEDV EKCSNFAIAF AEKF
//