FLAV_NOSSO
ID FLAV_NOSSO Reviewed; 170 AA.
AC P0A3E0; P11241;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Flavodoxin;
GN Name=isiB;
OS Nostoc sp. (strain ATCC 29151 / PCC 7119) (Anabaena sp.).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=1168;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1720613; DOI=10.1042/bj2800187;
RA Fillat M.F., Borrias W.E., Weisbeek P.J.;
RT "Isolation and overexpression in Escherichia coli of the flavodoxin gene
RT from Anabaena PCC 7119.";
RL Biochem. J. 280:187-191(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-37.
RX PubMed=2119231; DOI=10.1016/0167-4838(90)90091-s;
RA Fillat M.F., Edmondson D.E., Gomez-Moreno C.;
RT "Structural and chemical properties of a flavodoxin from Anabaena PCC
RT 7119.";
RL Biochim. Biophys. Acta 1040:301-307(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10388575; DOI=10.1006/jmbi.1999.2863;
RA Fernandez-Recio J., Romero A., Sancho J.;
RT "Energetics of a hydrogen bond (charged and neutral) and of a cation-pi
RT interaction in apoflavodoxin.";
RL J. Mol. Biol. 290:319-330(1999).
CC -!- FUNCTION: Low-potential electron donor to a number of redox enzymes.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC -!- INTERACTION:
CC P0A3E0; P21890: petH; NbExp=5; IntAct=EBI-593907, EBI-593915;
CC P0A3E0; P08165: FDXR; Xeno; NbExp=3; IntAct=EBI-593907, EBI-593948;
CC -!- SIMILARITY: Belongs to the flavodoxin family. {ECO:0000305}.
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DR EMBL; S68006; AAB20462.1; -; Genomic_DNA.
DR PDB; 1DX9; X-ray; 2.05 A; A/B/C/D=2-170.
DR PDB; 1FTG; X-ray; 2.00 A; A=3-170.
DR PDB; 1OBO; X-ray; 1.20 A; A/B=3-170.
DR PDB; 1OBV; X-ray; 2.10 A; A=3-170.
DR PDB; 1QHE; X-ray; 2.00 A; A=3-170.
DR PDB; 2KQU; NMR; -; A=3-170.
DR PDB; 2V5U; X-ray; 1.99 A; A/B=2-170.
DR PDB; 2V5V; X-ray; 1.88 A; A/B=2-170.
DR PDB; 3ESX; X-ray; 2.31 A; A/B=2-170.
DR PDB; 3ESY; X-ray; 2.39 A; A/B/C/D=2-170.
DR PDB; 3ESZ; X-ray; 1.94 A; A/B=2-170.
DR PDB; 5LJP; X-ray; 1.10 A; A=2-170.
DR PDBsum; 1DX9; -.
DR PDBsum; 1FTG; -.
DR PDBsum; 1OBO; -.
DR PDBsum; 1OBV; -.
DR PDBsum; 1QHE; -.
DR PDBsum; 2KQU; -.
DR PDBsum; 2V5U; -.
DR PDBsum; 2V5V; -.
DR PDBsum; 3ESX; -.
DR PDBsum; 3ESY; -.
DR PDBsum; 3ESZ; -.
DR PDBsum; 5LJP; -.
DR AlphaFoldDB; P0A3E0; -.
DR BMRB; P0A3E0; -.
DR SMR; P0A3E0; -.
DR IntAct; P0A3E0; 3.
DR EvolutionaryTrace; P0A3E0; -.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; TAS:UniProtKB.
DR GO; GO:0010106; P:cellular response to iron ion starvation; TAS:UniProtKB.
DR GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001226; Flavodoxin_CS.
DR InterPro; IPR010086; Flavodoxin_lc.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR PIRSF; PIRSF038996; FldA; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR TIGRFAMs; TIGR01752; flav_long; 1.
DR PROSITE; PS00201; FLAVODOXIN; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Flavoprotein;
KW FMN; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2119231"
FT CHAIN 2..170
FT /note="Flavodoxin"
FT /id="PRO_0000171600"
FT DOMAIN 5..165
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:5LJP"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:5LJP"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:5LJP"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:5LJP"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5LJP"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:5LJP"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:5LJP"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:5LJP"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:5LJP"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2KQU"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:5LJP"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:5LJP"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:5LJP"
FT TURN 92..97
FT /evidence="ECO:0007829|PDB:5LJP"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:5LJP"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:2KQU"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:5LJP"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:5LJP"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:5LJP"
FT HELIX 153..167
FT /evidence="ECO:0007829|PDB:5LJP"
SQ SEQUENCE 170 AA; 18964 MW; 069E8DEBA9E33302 CRC64;
MSKKIGLFYG TQTGKTESVA EIIRDEFGND VVTLHDVSQA EVTDLNDYQY LIIGCPTWNI
GELQSDWEGL YSELDDVDFN GKLVAYFGTG DQIGYADNFQ DAIGILEEKI SQRGGKTVGY
WSTDGYDFND SKALRNGKFV GLALDEDNQS DLTDDRIKSW VAQLKSEFGL
