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Database: UniProt
Entry: P00211
LinkDB: P00211
Original site: P00211 
ID   FER2_DESNO              Reviewed;          59 AA.
AC   P00211;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   20-DEC-2017, entry version 84.
DE   RecName: Full=Ferredoxin-2;
DE   AltName: Full=Ferredoxin II;
OS   Desulfomicrobium norvegicum (strain DSM 1741 / NCIMB 8310)
OS   (Desulfovibrio baculatus (strain Norway 4)) (Desulfovibrio
OS   desulfuricans (strain Norway 4)).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfomicrobiaceae; Desulfomicrobium.
OX   NCBI_TaxID=52561;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6403056; DOI=10.1016/S0300-9084(83)80027-3;
RA   Guerlesquin F.A., Bruschi M., Bovier-Lapierre G.E., Bonicel J.J.,
RA   Couchoud P.M.;
RT   "Primary structure of the two (4 Fe-4 S) clusters ferredoxin from
RT   Desulfovibrio desulfuricans (strain Norway 4).";
RL   Biochimie 65:43-47(1983).
RN   [2]
RP   STRUCTURE BY NMR.
RX   PubMed=8396440; DOI=10.1016/0005-2728(93)90165-C;
RA   Blanchard L., Payan F., Qian M., Haser R., Noailly M., Bruschi M.,
RA   Guerlesquin F.A.;
RT   "Intramolecular electron transfer in ferredoxin II from Desulfovibrio
RT   desulfuricans Norway.";
RL   Biochim. Biophys. Acta 1144:125-133(1993).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer
CC       electrons in a wide variety of metabolic reactions.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 2 [4Fe-4S] clusters.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
DR   PIR; A00213; FEDV2N.
DR   ProteinModelPortal; P00211; -.
DR   SMR; P00211; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   InterPro; IPR001080; 3Fe4S_ferredoxin.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   PRINTS; PR00352; 3FE4SFRDOXIN.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Periplasm; Repeat; Transport.
FT   CHAIN         1     59       Ferredoxin-2.
FT                                /FTId=PRO_0000159157.
FT   DOMAIN        3     32       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       33     59       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        12     12       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        15     15       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        18     18       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        22     22       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        42     42       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        45     45       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        48     48       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        52     52       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
SQ   SEQUENCE   59 AA;  6313 MW;  CB09AB6D4F856DDC CRC64;
     MGYSVIVDSD KCIGCGECVD VCPVEVYELQ NGKAVPVNEE ECLGCESCIE VCPQNAIVE
//
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