FER1_HALMA
ID FER1_HALMA Reviewed; 129 AA.
AC P00217; Q5UZH4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Ferredoxin-1;
GN Name=fer1; OrderedLocusNames=rrnAC2526;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [2]
RP PROTEIN SEQUENCE OF 2-129.
RX PubMed=7378468; DOI=10.1016/0005-2795(80)90016-1;
RA Hase T., Wakabayashi S., Matsubara H., Mevarech M., Werber M.M.;
RT "Amino acid sequence of 2Fe-2S ferredoxin from an extreme halophile,
RT Halobacterium of the Dead Sea.";
RL Biochim. Biophys. Acta 623:139-145(1980).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=8612076; DOI=10.1038/nsb0596-452;
RA Frolow F., Harel M., Sussman J.L., Mevarech M., Shoham M.;
RT "Insights into protein adaptation to a saturated salt environment from the
RT crystal structure of a halophilic 2Fe-2S ferredoxin.";
RL Nat. Struct. Biol. 3:452-458(1996).
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 -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV47329.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY596297; AAV47329.1; ALT_INIT; Genomic_DNA.
DR PIR; A00221; FEHSX.
DR RefSeq; WP_004959486.1; NZ_CP039138.1.
DR PDB; 1DOI; X-ray; 1.90 A; A=2-129.
DR PDBsum; 1DOI; -.
DR AlphaFoldDB; P00217; -.
DR BMRB; P00217; -.
DR SMR; P00217; -.
DR STRING; 272569.rrnAC2526; -.
DR EnsemblBacteria; AAV47329; AAV47329; rrnAC2526.
DR GeneID; 40153420; -.
DR GeneID; 64824186; -.
DR KEGG; hma:rrnAC2526; -.
DR PATRIC; fig|272569.17.peg.3134; -.
DR eggNOG; arCOG02844; Archaea.
DR HOGENOM; CLU_1773154_0_0_2; -.
DR EvolutionaryTrace; P00217; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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 Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; SSF54292; 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; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7378468"
FT CHAIN 2..129
FT /note="Ferredoxin-1"
FT /id="PRO_0000189385"
FT DOMAIN 29..120
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 64
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:8612076"
FT BINDING 69
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:8612076"
FT BINDING 72
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:8612076"
FT BINDING 103
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:8612076"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1DOI"
FT HELIX 9..15
FT /evidence="ECO:0007829|PDB:1DOI"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:1DOI"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:1DOI"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1DOI"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1DOI"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:1DOI"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:1DOI"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:1DOI"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1DOI"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1DOI"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:1DOI"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1DOI"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1DOI"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1DOI"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:1DOI"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1DOI"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:1DOI"
SQ SEQUENCE 129 AA; 14538 MW; 68FF680231AA6C04 CRC64;
MPTVEYLNYE VVDDNGWDMY DDDVFGEASD MDLDDEDYGS LEVNEGEYIL EAAEAQGYDW
PFSCRAGACA NCAAIVLEGD IDMDMQQILS DEEVEDKNVR LTCIGSPDAD EVKIVYNAKH
LDYLQNRVI
