FER_HALSA
ID FER_HALSA Reviewed; 129 AA.
AC P00216; Q9HN15;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ferredoxin;
GN Name=fdx; Synonyms=fer2; OrderedLocusNames=VNG_2293G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8510664; DOI=10.1007/bf00281602;
RA Pfeifer F., Griffig J., Oesterhelt D.;
RT "The fdx gene encoding the [2Fe-2S] ferredoxin of Halobacterium salinarium
RT (H. halobium).";
RL Mol. Gen. Genet. 239:66-71(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [3]
RP PROTEIN SEQUENCE OF 2-129, AND ACETYLATION AT LYS-119.
RX PubMed=670159; DOI=10.1093/oxfordjournals.jbchem.a132078;
RA Hase T., Wakabayashi S., Matsubara H., Kerscher L., Oesterhelt D.,
RA Rao K.K., Hall D.O.;
RT "Complete amino acid sequence of Halobacterium halobium ferredoxin
RT containing an Nepsilon-acetyllysine residue.";
RL J. Biochem. 83:1657-1670(1978).
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 ---------------------------------------------------------------------------
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; X68103; CAA48224.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG20406.1; -; Genomic_DNA.
DR PIR; B84380; B84380.
DR PIR; S35235; FEHS.
DR RefSeq; WP_010903707.1; NC_002607.1.
DR PDB; 1E0Z; NMR; -; A=2-129.
DR PDB; 1E10; NMR; -; A=2-129.
DR PDBsum; 1E0Z; -.
DR PDBsum; 1E10; -.
DR AlphaFoldDB; P00216; -.
DR BMRB; P00216; -.
DR SMR; P00216; -.
DR STRING; 64091.VNG_2293G; -.
DR iPTMnet; P00216; -.
DR PaxDb; P00216; -.
DR EnsemblBacteria; AAG20406; AAG20406; VNG_2293G.
DR GeneID; 5953323; -.
DR GeneID; 62887568; -.
DR KEGG; hal:VNG_2293G; -.
DR PATRIC; fig|64091.14.peg.1769; -.
DR HOGENOM; CLU_1773154_0_0_2; -.
DR InParanoid; P00216; -.
DR OMA; IEMDMQQ; -.
DR OrthoDB; 100430at2157; -.
DR PhylomeDB; P00216; -.
DR EvolutionaryTrace; P00216; -.
DR Proteomes; UP000000554; Chromosome.
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; Acetylation; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:670159"
FT CHAIN 2..129
FT /note="Ferredoxin"
FT /id="PRO_0000189387"
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 BINDING 69
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 72
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 103
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:670159"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1E0Z"
FT HELIX 9..15
FT /evidence="ECO:0007829|PDB:1E0Z"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:1E0Z"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:1E0Z"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1E0Z"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1E0Z"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:1E0Z"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1E0Z"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1E0Z"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1E0Z"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1E10"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:1E0Z"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1E0Z"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:1E0Z"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1E10"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:1E0Z"
SQ SEQUENCE 129 AA; 14418 MW; 787BA486807ADCA7 CRC64;
MPTVEYLNYE TLDDQGWDMD DDDLFEKAAD AGLDGEDYGT MEVAEGEYIL EAAEAQGYDW
PFSCRAGACA NCASIVKEGE IDMDMQQILS DEEVEEKDVR LTCIGSPAAD EVKIVYNAKH
LDYLQNRVI
