FER2_LEPBY
ID FER2_LEPBY Reviewed; 99 AA.
AC P46035;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Ferredoxin-2;
DE AltName: Full=Ferredoxin II;
DE Short=FdII;
GN Name=fdxH;
OS Leptolyngbya boryana (Plectonema boryanum).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Leptolyngbyaceae; Leptolyngbya.
OX NCBI_TaxID=1184;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 18200 / UTEX 594 / PCC 73110;
RX PubMed=8106314; DOI=10.1128/jb.176.4.1037-1046.1994;
RA Schrautemeier B., Cassing A., Boehme H.;
RT "Characterization of the genome region encoding an fdxH-type ferredoxin and
RT a new 2[4Fe-4S] ferredoxin from the nonheterocystous, nitrogen-fixing
RT cyanobacterium Plectonema boryanum PCC 73110.";
RL J. Bacteriol. 176:1037-1046(1994).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions. Donates electrons to the
CC nitrogenase.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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; X71865; CAA50698.1; -; Genomic_DNA.
DR PIR; C49890; C49890.
DR AlphaFoldDB; P46035; -.
DR SMR; P46035; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR010241; Fd_pln.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR02008; fdx_plant; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Nitrogen fixation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..99
FT /note="Ferredoxin-2"
FT /id="PRO_0000189353"
FT DOMAIN 4..96
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 80
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 99 AA; 11053 MW; FB3EA0008CA4ED90 CRC64;
MATYQVRLIN KKRNLDITLP VDEDTTVLEA AEEAELDLPF SCHSGACSSC VGKVVEGEIN
QDDQTFLDEE QVAKGFVLLC VTYPRTDCTI RTHQEAYLV