ID   FER2_AZOVD              Reviewed;         107 AA.
AC   P82802; C1DH09;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Ferredoxin, 2Fe-2s;
DE   AltName: Full=2FeAvFdI;
DE   AltName: Full=Iron-sulfur protein I;
DE   AltName: Full=Shethna protein I;
GN   OrderedLocusNames=Avin_01520;
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303;
RX   PubMed=19429624; DOI=10.1128/jb.00504-09;
RA   Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA   Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA   Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA   Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA   Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA   Dean D.R., Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT   to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-107, SUBUNIT, AND MASS SPECTROMETRY.
RX   PubMed=10439076; DOI=10.1007/s007750050317;
RA   Chatelet C., Meyer J.;
RT   "The [2Fe-2S] protein I (Shethna protein I) from Azotobacter vinelandii is
RT   homologous to the [2Fe-2S] ferredoxin from Clostridium pasteurianum.";
RL   J. Biol. Inorg. Chem. 4:311-317(1999).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions. Might be involved in nitrogen
CC       fixation.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC       Note=Binds 1 [2Fe-2S] cluster.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10439076}.
CC   -!- MASS SPECTROMETRY: Mass=22876; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10439076};
CC   -!- SIMILARITY: Belongs to the 2Fe2S Shethna-type ferredoxin family.
CC       {ECO:0000305}.
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DR   EMBL; CP001157; ACO76416.1; -; Genomic_DNA.
DR   RefSeq; WP_012698844.1; NC_012560.1.
DR   PDB; 5ABR; X-ray; 2.11 A; A/B=1-107.
DR   PDBsum; 5ABR; -.
DR   AlphaFoldDB; P82802; -.
DR   SMR; P82802; -.
DR   STRING; 322710.Avin_01520; -.
DR   PRIDE; P82802; -.
DR   EnsemblBacteria; ACO76416; ACO76416; Avin_01520.
DR   KEGG; avn:Avin_01520; -.
DR   eggNOG; COG3411; Bacteria.
DR   HOGENOM; CLU_126515_1_1_6; -.
DR   OMA; GICHKKE; -.
DR   OrthoDB; 1412344at2; -.
DR   Proteomes; UP000002424; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3D-structure; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Nitrogen fixation; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10439076"
FT   CHAIN           2..107
FT                   /note="Ferredoxin, 2Fe-2s"
FT                   /id="PRO_0000187247"
FT   BINDING         11
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         24
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         56
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         60
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   STRAND          6..11
FT                   /evidence="ECO:0007829|PDB:5ABR"
FT   TURN            24..28
FT                   /evidence="ECO:0007829|PDB:5ABR"
FT   HELIX           29..42
FT                   /evidence="ECO:0007829|PDB:5ABR"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:5ABR"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:5ABR"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:5ABR"
FT   STRAND          66..69
FT                   /evidence="ECO:0007829|PDB:5ABR"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:5ABR"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:5ABR"
FT   HELIX           82..89
FT                   /evidence="ECO:0007829|PDB:5ABR"
FT   TURN            90..93
FT                   /evidence="ECO:0007829|PDB:5ABR"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:5ABR"
FT   TURN            104..106
FT                   /evidence="ECO:0007829|PDB:5ABR"
SQ   SEQUENCE   107 AA;  11395 MW;  44A9DB807959F794 CRC64;
     MAKPEFHIFI CAQNRPAGHP RGSCGAKGAE GVYNAFAQVL IQKNLTNRIA LTTTGCLGPC
     QAGANVLIYP GAVMYSWVEP ADAAIIVEQH LLGGEPYADK LTPAEIW