FER_ACIAM
ID FER_ACIAM Reviewed; 103 AA.
AC P49949;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Zinc-containing ferredoxin;
DE AltName: Full=Seven-iron ferredoxin;
GN Name=zfx;
OS Acidianus ambivalens (Desulfurolobus ambivalens).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=2283;
RN [1]
RP PROTEIN SEQUENCE, AND METHYLATION AT LYS-29 AND LYS-101.
RA Gomes C.M., Faria A., Carita J.C., Mendes J., Regalla M., Chicau P.,
RA Huber H., Stetter K.O., Teixeira M.;
RT "Di-cluster, seven iron ferredoxins from hyperthermophilic Sulfolobales.";
RL J. Biol. Inorg. Chem. 3:499-507(1998).
RN [2]
RP PROTEIN SEQUENCE OF 1-50.
RC STRAIN=Lei 10 / DSM 3772 / JCM 9191;
RX PubMed=7851403; DOI=10.1111/j.1432-1033.1995.tb20392.x;
RA Teixeira M., Batista R., Campos A.P., Gomes C., Mendes J., Pacheco I.,
RA Anemuller S., Hagen W.R.;
RT "A seven-iron ferredoxin from the thermoacidophilic archaeon Desulfurolobus
RT ambivalens.";
RL Eur. J. Biochem. 227:322-327(1995).
RN [3]
RP STRUCTURE BY NMR.
RC STRAIN=Lei 10 / DSM 3772 / JCM 9191;
RX PubMed=8617291; DOI=10.1111/j.1432-1033.1996.00092.x;
RA Bentrop D., Bertini I., Lucinat C., Mendes J., Piccioli M., Teixeira M.;
RT "Paramagnetic NMR analysis of the seven-iron ferredoxin from the
RT hyperthermoacidophilic archaeon Desulfurolobus ambivalens reveals
RT structural similarity to other dicluster ferredoxins.";
RL Eur. J. Biochem. 236:92-99(1996).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions. The 3Fe-4S cluster is reduced
CC by a flavoprotein with NADH oxidase activity from the same organism.
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Note=Binds 1 [3Fe-4S] cluster.;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion.;
CC -!- PTM: Lys-29 was found to be 95% monomethylated and Lys-101 was found to
CC be 10% monomethylated.
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DR PDB; 2VKR; X-ray; 2.01 A; A/B/C/D/E/F/G=1-103.
DR PDBsum; 2VKR; -.
DR AlphaFoldDB; P49949; -.
DR SMR; P49949; -.
DR EvolutionaryTrace; P49949; -.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009157; Fd_Zn-bd.
DR Pfam; PF13237; Fer4_10; 1.
DR PIRSF; PIRSF000068; Zn_Fdx_Sulfol; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 3Fe-4S; 4Fe-4S; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Metal-binding; Methylation; Repeat;
KW Transport; Zinc.
FT CHAIN 1..103
FT /note="Zinc-containing ferredoxin"
FT /id="PRO_0000159173"
FT DOMAIN 37..65
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 74..103
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT REGION 1..36
FT /note="N-terminal extension"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT MOD_RES 29
FT /note="N6-methyllysine; partial"
FT /evidence="ECO:0000269|Ref.1"
FT MOD_RES 101
FT /note="N6-methyllysine; partial"
FT /evidence="ECO:0000269|Ref.1"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:2VKR"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:2VKR"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:2VKR"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2VKR"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2VKR"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2VKR"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:2VKR"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2VKR"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:2VKR"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2VKR"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:2VKR"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2VKR"
SQ SEQUENCE 103 AA; 11004 MW; F2504DB8AAC2DD17 CRC64;
GIDPNYRTSR QVVGEHQGHK VYGPVDPPKV LGIHGTIVGV DFDLCIADGS CITACPVNVF
QWYDTPGHPA SEKKADPINE QACIFCMACV NVCPVAAIDV KPP
