FER_MASLA
ID FER_MASLA Reviewed; 99 AA.
AC P00248; O31125;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ferredoxin;
GN Name=petF;
OS Mastigocladus laminosus (Fischerella sp.).
OC Bacteria; Cyanobacteria; Nostocales; Hapalosiphonaceae; Mastigocladus.
OX NCBI_TaxID=83541;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PCC 7605;
RA He Z.-Y., Chitnis P.R., Nechushtai R.;
RT "Molecular cloning of the petF gene encoding ferredoxin I of the
RT thermophilic cyanobacterium Mastigocladus laminosus.";
RL (er) Plant Gene Register PGR98-027(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-99.
RC STRAIN=Cohn;
RA Hase T., Wakabayashi S., Matsubara H., Rao K.K., Hall D.O., Widmer H.,
RA Gysi J., Zuber H.;
RL Submitted (SEP-1978) to the PIR data bank.
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC reductase (FTR) and thioredoxin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; AF030002; AAC04840.1; -; Genomic_DNA.
DR PIR; A00252; FEMW.
DR PDB; 1RFK; X-ray; 1.25 A; A/B=2-99.
DR PDB; 3P63; X-ray; 2.30 A; A/B=2-99.
DR PDBsum; 1RFK; -.
DR PDBsum; 3P63; -.
DR AlphaFoldDB; P00248; -.
DR SMR; P00248; -.
DR EvolutionaryTrace; P00248; -.
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 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 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..99
FT /note="Ferredoxin"
FT /id="PRO_0000189340"
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"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1RFK"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1RFK"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:1RFK"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:1RFK"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:1RFK"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1RFK"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:1RFK"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1RFK"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1RFK"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1RFK"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1RFK"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:1RFK"
SQ SEQUENCE 99 AA; 10748 MW; 88C39489BA54EE97 CRC64;
MATYKVTLIN EAEGLNKTIE VPDDQYILDA AEEAGIDLPY SCRAGACSTC AGKLISGTVD
QSDQSFLDDD QIEAGYVLTC VAYPTSDCVI ETHKEEELY