FER_GOTA9
ID FER_GOTA9 Reviewed; 56 AA.
AC P00198; K0AXP4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=4Fe-4S ferredoxin FdxA {ECO:0000312|EMBL:AFS77196.1};
DE AltName: Full=Ferredoxin {ECO:0000303|PubMed:5799135};
GN Name=fdxA {ECO:0000312|EMBL:AFS77196.1};
GN OrderedLocusNames=Curi_c01160 {ECO:0000312|EMBL:AFS77196.1};
OS Gottschalkia acidurici (strain ATCC 7906 / DSM 604 / BCRC 14475 / CIP
OS 104303 / KCTC 5404 / NCIMB 10678 / 9a) (Clostridium acidurici).
OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Gottschalkiaceae;
OC Gottschalkia.
OX NCBI_TaxID=1128398;
RN [1] {ECO:0000312|EMBL:AFS77196.1, ECO:0000312|Proteomes:UP000006094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7906 / DSM 604 / BCRC 14475 / CIP 104303 / KCTC 5404 / NCIMB
RC 10678 / 9a {ECO:0000305};
RX PubMed=23240052; DOI=10.1371/journal.pone.0051662;
RA Hartwich K., Poehlein A., Daniel R.;
RT "The purine-utilizing bacterium Clostridium acidurici 9a: a genome-guided
RT metabolic reconsideration.";
RL PLoS ONE 7:E51662-E51662(2012).
RN [2]
RP PROTEIN SEQUENCE OF 2-56.
RX PubMed=5799135; DOI=10.1021/bi00834a035;
RA Rall S.C., Bolinger R.E., Cole R.D.;
RT "The amino acid sequence of ferredoxin from Clostridium acidi-urici.";
RL Biochemistry 8:2486-2496(1969).
RN [3]
RP SEQUENCE REVISION TO 16; 22; 26 AND 29.
RC STRAIN=ATCC 7906 / DSM 604 / BCRC 14475 / CIP 104303 / KCTC 5404 / NCIMB
RC 10678 / 9a {ECO:0000305};
RX PubMed=8373379; DOI=10.1042/bj2940622;
RA Meyer J., Moulis J.-M., Scherrer N., Gagnon J., Ulrich J.;
RT "Sequences of clostridial ferredoxins: determination of the Clostridium
RT sticklandii sequence and correction of the Clostridium acidurici
RT sequence.";
RL Biochem. J. 294:622-623(1993).
RN [4] {ECO:0007744|PDB:1FDN}
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 2-56 IN COMPLEX WITH IRON-SULFUR
RP (4FE-4S).
RX PubMed=7966291; DOI=10.1016/0022-2836(94)90041-8;
RA Duee E.D., Fanchon E., Vicat J., Sieker L.C., Meyer J., Moulis J.-M.;
RT "Refined crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium
RT acidurici at 1.84-A resolution.";
RL J. Mol. Biol. 243:683-695(1994).
RN [5] {ECO:0007744|PDB:2FDN}
RP X-RAY CRYSTALLOGRAPHY (0.94 ANGSTROMS) OF 2-56 IN COMPLEX WITH IRON-SULFUR
RP (4FE-4S).
RX PubMed=9405040; DOI=10.1021/bi972155y;
RA Dauter Z., Wilson K.S., Sieker L.C., Meyer J., Moulis J.-M.;
RT "Atomic resolution (0.94 A) structure of Clostridium acidurici ferredoxin.
RT Detailed geometry of [4Fe-4S] clusters in a protein.";
RL Biochemistry 36:16065-16073(1997).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC {ECO:0000250|UniProtKB:P50727}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000269|PubMed:7966291,
CC ECO:0000269|PubMed:9405040};
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DR EMBL; CP003326; AFS77196.1; -; Genomic_DNA.
DR PIR; S36790; FECLCU.
DR RefSeq; WP_014966333.1; NC_018664.1.
DR PDB; 1FCA; X-ray; 1.80 A; A=2-56.
DR PDB; 1FDN; X-ray; 1.84 A; A=2-56.
DR PDB; 2FDN; X-ray; 0.94 A; A=2-56.
DR PDBsum; 1FCA; -.
DR PDBsum; 1FDN; -.
DR PDBsum; 2FDN; -.
DR AlphaFoldDB; P00198; -.
DR PCDDB; P00198; -.
DR SMR; P00198; -.
DR STRING; 1128398.Curi_c01160; -.
DR EnsemblBacteria; AFS77196; AFS77196; Curi_c01160.
DR KEGG; cad:Curi_c01160; -.
DR PATRIC; fig|1128398.3.peg.115; -.
DR eggNOG; COG2768; Bacteria.
DR HOGENOM; CLU_139698_11_4_9; -.
DR OMA; PAECIVQ; -.
DR OrthoDB; 1873445at2; -.
DR EvolutionaryTrace; P00198; -.
DR Proteomes; UP000006094; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR000813; 7Fe_ferredoxin.
DR Pfam; PF12838; Fer4_7; 1.
DR PRINTS; PR00354; 7FE8SFRDOXIN.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5799135"
FT CHAIN 2..56
FT /note="4Fe-4S ferredoxin FdxA"
FT /evidence="ECO:0000269|PubMed:5799135"
FT /id="PRO_0000159109"
FT DOMAIN 1..28
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 29..56
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 9
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711,
FT ECO:0000269|PubMed:7966291, ECO:0000269|PubMed:9405040,
FT ECO:0007744|PDB:1FDN, ECO:0007744|PDB:2FDN"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711,
FT ECO:0000269|PubMed:7966291, ECO:0000269|PubMed:9405040,
FT ECO:0007744|PDB:1FDN, ECO:0007744|PDB:2FDN"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711,
FT ECO:0000269|PubMed:7966291, ECO:0000269|PubMed:9405040,
FT ECO:0007744|PDB:1FDN, ECO:0007744|PDB:2FDN"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711,
FT ECO:0000269|PubMed:7966291, ECO:0000269|PubMed:9405040,
FT ECO:0007744|PDB:1FDN, ECO:0007744|PDB:2FDN"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711,
FT ECO:0000269|PubMed:7966291, ECO:0000269|PubMed:9405040,
FT ECO:0007744|PDB:1FDN, ECO:0007744|PDB:2FDN"
FT BINDING 41
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711,
FT ECO:0000269|PubMed:7966291, ECO:0000269|PubMed:9405040,
FT ECO:0007744|PDB:1FDN, ECO:0007744|PDB:2FDN"
FT BINDING 44
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711,
FT ECO:0000269|PubMed:7966291, ECO:0000269|PubMed:9405040,
FT ECO:0007744|PDB:1FDN, ECO:0007744|PDB:2FDN"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711,
FT ECO:0000269|PubMed:7966291, ECO:0000269|PubMed:9405040,
FT ECO:0007744|PDB:1FDN, ECO:0007744|PDB:2FDN"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2FDN"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:2FDN"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1FDN"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2FDN"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:2FDN"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:2FDN"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2FDN"
SQ SEQUENCE 56 AA; 5670 MW; AD388C7B4A1E979F CRC64;
MAYVINEACI SCGACEPECP VNAISSGDDR YVIDADTCID CGACAGVCPV DAPVQA
