ID   FERH_MICDP              Reviewed;          99 AA.
AC   P28610;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Ferredoxin, heterocyst;
GN   Name=fdxH;
OS   Microchaete diplosiphon (Fremyella diplosiphon).
OC   Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Microchaete.
OX   NCBI_TaxID=1197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1581559; DOI=10.1007/bf00019219;
RA   Schrautemeier B., Boehme H.;
RT   "Coding sequence of a heterocyst ferredoxin gene (fdxH) isolated from the
RT   nitrogen-fixing cyanobacterium Calothrix sp. PCC 7601.";
RL   Plant Mol. Biol. 18:1005-1006(1992).
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   -!- 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}.
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; X63011; CAA44739.1; -; Genomic_DNA.
DR   AlphaFoldDB; P28610; -.
DR   SMR; P28610; -.
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   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; Heterocyst; Iron; Iron-sulfur; Metal-binding;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..99
FT                   /note="Ferredoxin, heterocyst"
FT                   /id="PRO_0000189333"
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;  10950 MW;  420E5B70D20E0706 CRC64;
     MATYQVRLIN KKEDLDSTIE IDEDTTILEG AAENGIELPF SCHSGSCSSC VGKVVEGEVD
     QSDQIFLDDE QMSKGFALLC VTYPRSNCTI KTHQEPYLV