FERH_NOSS1
ID FERH_NOSS1 Reviewed; 99 AA.
AC P11053;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ferredoxin, heterocyst;
GN Name=fdxH; OrderedLocusNames=all1430;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2467184; DOI=10.1007/bf00337722;
RA Boehme H., Haselkorn R.;
RT "Molecular cloning and nucleotide sequence analysis of the gene coding for
RT heterocyst ferredoxin from the cyanobacterium Anabaena sp. strain PCC
RT 7120.";
RL Mol. Gen. Genet. 214:278-285(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=8329401; DOI=10.1021/bi00077a033;
RA Jacobson B.L., Chae Y.K., Markley J.L., Rayment I., Holden H.M.;
RT "Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S]
RT ferredoxin from Anabaena 7120 determined to 1.7-A resolution.";
RL Biochemistry 32:6788-6793(1993).
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 -!- MISCELLANEOUS: This ferredoxin is expressed by heterocysts and differs
CC from the ferredoxin expressed in vegetative cells.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; X13522; CAA31873.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB73387.1; -; Genomic_DNA.
DR PIR; AC1985; AC1985.
DR PIR; S04543; S04543.
DR RefSeq; WP_010995602.1; NZ_RSCN01000040.1.
DR PDB; 1FRD; X-ray; 1.70 A; A=2-99.
DR PDBsum; 1FRD; -.
DR AlphaFoldDB; P11053; -.
DR SMR; P11053; -.
DR STRING; 103690.17130777; -.
DR EnsemblBacteria; BAB73387; BAB73387; BAB73387.
DR KEGG; ana:all1430; -.
DR eggNOG; COG0633; Bacteria.
DR OMA; AYPRSNC; -.
DR OrthoDB; 1885467at2; -.
DR EvolutionaryTrace; P11053; -.
DR Proteomes; UP000002483; Chromosome.
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:0043158; P:heterocyst differentiation; 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 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Electron transport; Heterocyst; Iron; Iron-sulfur;
KW Metal-binding; Nitrogen fixation; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..99
FT /note="Ferredoxin, heterocyst"
FT /id="PRO_0000189301"
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 ECO:0000269|PubMed:8329401"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:8329401"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:8329401"
FT BINDING 80
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:8329401"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1FRD"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:1FRD"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:1FRD"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:1FRD"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:1FRD"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1FRD"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:1FRD"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1FRD"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1FRD"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:1FRD"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1FRD"
SQ SEQUENCE 99 AA; 10949 MW; E47E1A32437A4D03 CRC64;
MASYQVRLIN KKQDIDTTIE IDEETTILDG AEENGIELPF SCHSGSCSSC VGKVVEGEVD
QSDQIFLDDE QMGKGFALLC VTYPRSNCTI KTHQEPYLA
