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FLAV_SYNE7
ID   FLAV_SYNE7              Reviewed;         170 AA.
AC   P10340; Q31MZ8;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Flavodoxin;
GN   Name=isiB; OrderedLocusNames=Synpcc7942_1541;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3121586; DOI=10.1128/jb.170.1.258-265.1988;
RA   Laudenbach D.E., Reith M.E., Straus N.A.;
RT   "Isolation, sequence analysis, and transcriptional studies of the
RT   flavodoxin gene from Anacystis nidulans R2.";
RL   J. Bacteriol. 170:258-265(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-56, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=6406674; DOI=10.1016/s0022-2836(83)80277-0;
RA   Smith W.W., Pattridge K.A., Ludwig M.L., Petsko G.A., Tsernoglou D.,
RA   Tanaka M., Yasunobu K.T.;
RT   "Structure of oxidized flavodoxin from Anacystis nidulans.";
RL   J. Mol. Biol. 165:737-753(1983).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   PubMed=10610791; DOI=10.1006/jmbi.1999.3151;
RA   Drennan C.L., Pattridge K.A., Weber C.H., Metzger A.L., Hoover D.M.,
RA   Ludwig M.L.;
RT   "Refined structures of oxidized flavodoxin from Anacystis nidulans.";
RL   J. Mol. Biol. 294:711-724(1999).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
RX   PubMed=10610792; DOI=10.1006/jmbi.1999.3152;
RA   Hoover D.M., Drennan C.L., Metzger A.L., Osborne C., Weber C.H.,
RA   Pattridge K.A., Ludwig M.L.;
RT   "Comparisons of wild-type and mutant flavodoxins from Anacystis nidulans.
RT   Structural determinants of the redox potentials.";
RL   J. Mol. Biol. 294:725-743(1999).
RN   [6]
RP   STRUCTURE BY NMR.
RX   PubMed=1907844; DOI=10.1021/bi00245a008;
RA   Clubb R.T., Thanabal V., Osborne C., Wagner G.;
RT   "1H and 15N resonance assignments of oxidized flavodoxin from Anacystis
RT   nidulans with 3D NMR.";
RL   Biochemistry 30:7718-7730(1991).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox enzymes.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC   -!- INDUCTION: By iron stress.
CC   -!- SIMILARITY: Belongs to the flavodoxin family. {ECO:0000305}.
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DR   EMBL; M19116; AAA22050.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57571.1; -; Genomic_DNA.
DR   RefSeq; WP_011242314.1; NC_007604.1.
DR   PDB; 1CZH; X-ray; 1.86 A; A=2-170.
DR   PDB; 1CZK; X-ray; 1.90 A; A=2-170.
DR   PDB; 1CZL; X-ray; 1.80 A; A=2-170.
DR   PDB; 1CZN; X-ray; 1.70 A; A=2-170.
DR   PDB; 1CZO; X-ray; 1.85 A; A=2-170.
DR   PDB; 1CZR; X-ray; 1.90 A; A=2-170.
DR   PDB; 1CZU; X-ray; 2.00 A; A=2-170.
DR   PDB; 1D03; X-ray; 1.85 A; A=2-170.
DR   PDB; 1D04; X-ray; 1.85 A; A=2-170.
DR   PDB; 1OFV; X-ray; 1.70 A; A=2-170.
DR   PDB; 6KIF; EM; 3.30 A; P/X/p=2-170.
DR   PDBsum; 1CZH; -.
DR   PDBsum; 1CZK; -.
DR   PDBsum; 1CZL; -.
DR   PDBsum; 1CZN; -.
DR   PDBsum; 1CZO; -.
DR   PDBsum; 1CZR; -.
DR   PDBsum; 1CZU; -.
DR   PDBsum; 1D03; -.
DR   PDBsum; 1D04; -.
DR   PDBsum; 1OFV; -.
DR   PDBsum; 6KIF; -.
DR   AlphaFoldDB; P10340; -.
DR   BMRB; P10340; -.
DR   SMR; P10340; -.
DR   STRING; 1140.Synpcc7942_1541; -.
DR   DrugBank; DB03247; Flavin mononucleotide.
DR   PRIDE; P10340; -.
DR   EnsemblBacteria; ABB57571; ABB57571; Synpcc7942_1541.
DR   KEGG; syf:Synpcc7942_1541; -.
DR   eggNOG; COG0716; Bacteria.
DR   HOGENOM; CLU_051402_1_0_3; -.
DR   OMA; ICGIPTW; -.
DR   OrthoDB; 1961680at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1541-MON; -.
DR   EvolutionaryTrace; P10340; -.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
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; Stress response; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6406674"
FT   CHAIN           2..170
FT                   /note="Flavodoxin"
FT                   /id="PRO_0000171644"
FT   DOMAIN          4..165
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   CONFLICT        55
FT                   /note="C -> S (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   HELIX           14..26
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   TURN            29..31
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   STRAND          32..36
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   HELIX           42..47
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   STRAND          49..54
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   TURN            59..61
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   HELIX           65..70
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   HELIX           71..76
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   STRAND          83..89
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   TURN            92..97
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   HELIX           101..112
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:1CZL"
FT   STRAND          138..144
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   TURN            146..148
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:1CZN"
FT   HELIX           153..167
FT                   /evidence="ECO:0007829|PDB:1CZN"
SQ   SEQUENCE   170 AA;  18778 MW;  7291AEF23DCA0345 CRC64;
     MAKIGLFYGT QTGVTQTIAE SIQQEFGGES IVDLNDIANA DASDLNAYDY LIIGCPTWNV
     GELQSDWEGI YDDLDSVNFQ GKKVAYFGAG DQVGYSDNFQ DAMGILEEKI SSLGSQTVGY
     WPIEGYDFNE SKAVRNNQFV GLAIDEDNQP DLTKNRIKTW VSQLKSEFGL
 
 
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