ID U4KRN5_9MOLU Unreviewed; 55 AA.
AC U4KRN5;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU365098};
GN ORFNames=BN85308770 {ECO:0000313|EMBL:CCV65898.1};
OS Paracholeplasma brassicae.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Paracholeplasma.
OX NCBI_TaxID=61635 {ECO:0000313|EMBL:CCV65898.1, ECO:0000313|Proteomes:UP000032737};
RN [1] {ECO:0000313|EMBL:CCV65898.1, ECO:0000313|Proteomes:UP000032737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0502 {ECO:0000313|Proteomes:UP000032737};
RX PubMed=24158107; DOI=10.1159/000354322;
RA Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R.,
RA Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.;
RT "Analysis of the Complete Genomes of Acholeplasma brassicae , A. palmae and
RT A. laidlawii and Their Comparison to the Obligate Parasites from '
RT Candidatus Phytoplasma'.";
RL J. Mol. Microbiol. Biotechnol. 24:19-36(2013).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC {ECO:0000256|RuleBase:RU365098}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU365098};
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DR EMBL; FO681348; CCV65898.1; -; Genomic_DNA.
DR RefSeq; WP_030004760.1; NC_022549.1.
DR AlphaFoldDB; U4KRN5; -.
DR STRING; 61635.BN85308770; -.
DR KEGG; abra:BN85308770; -.
DR HOGENOM; CLU_139698_11_4_14; -.
DR OrthoDB; 9803319at2; -.
DR Proteomes; UP000032737; Chromosome Acholeplasma brassicae.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.20; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR000813; 7Fe_ferredoxin.
DR Pfam; PF00037; Fer4; 2.
DR PRINTS; PR00354; 7FE8SFRDOXIN.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|RuleBase:RU365098};
KW Electron transport {ECO:0000256|RuleBase:RU365098};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365098};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU365098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365098};
KW Reference proteome {ECO:0000313|Proteomes:UP000032737};
KW Transport {ECO:0000256|RuleBase:RU365098}.
FT DOMAIN 1..25
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 28..55
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 55 AA; 5870 MW; 93EDEEC7885A52E3 CRC64;
MPRWINDTCI ACGSCQAECP VDCISEGDIY VIDESICIDC GACQEVCPVG AIAER
//
