FERH_TRIV2
ID FERH_TRIV2 Reviewed; 99 AA.
AC P46046; Q3M641;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ferredoxin, heterocyst;
GN Name=fdxH1; OrderedLocusNames=Ava_3940;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8709854; DOI=10.1111/j.1365-2958.1995.mmi_18020357.x;
RA Schrautemeier B., Neveling U., Schmitz S.;
RT "Distinct and differently regulated Mo-dependent nitrogen-fixing systems
RT evolved for heterocysts and vegetative cells of Anabaena variabilis ATCC
RT 29413: characterization of the fdxH1/2 gene regions as part of the nif1/2
RT gene clusters.";
RL Mol. Microbiol. 18:357-369(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions. Donates electrons to the
CC nitrogenase 1.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- DEVELOPMENTAL STAGE: Expressed exclusively within heterocysts.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; Z46887; CAA86986.1; -; Genomic_DNA.
DR EMBL; CP000117; ABA23545.1; -; Genomic_DNA.
DR PIR; S49989; S49989.
DR AlphaFoldDB; P46046; -.
DR SMR; P46046; -.
DR STRING; 240292.Ava_3940; -.
DR EnsemblBacteria; ABA23545; ABA23545; Ava_3940.
DR KEGG; ava:Ava_3940; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_082632_7_3_3; -.
DR OMA; AYPRSNC; -.
DR Proteomes; UP000002533; 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 2: Evidence at transcript level;
KW 2Fe-2S; Electron transport; Heterocyst; 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, heterocyst"
FT /id="PRO_0000189303"
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; 10904 MW; A5DC9DDA32057E13 CRC64;
MATYQVRLIS KKENIDTTIE IDEETTILDG AEENGIELPF SCHSGSCSSC VGKVVEGEVD
QSDQIFLDDE QVGKGFALLC VTYPRSNCTI KTHQEPYLA