FER_TRIVA
ID FER_TRIVA Reviewed; 100 AA.
AC P21149;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ferredoxin;
DE Flags: Precursor;
OS Trichomonas vaginalis.
OC Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC Trichomonas.
OX NCBI_TaxID=5722;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 9-100.
RC STRAIN=ATCC 30001 / NIH-C1;
RX PubMed=1696716; DOI=10.1073/pnas.87.16.6097;
RA Johnson P.J., D'Oliveira C.E., Gorrell T.E., Mueller M.;
RT "Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic
RT protist Trichomonas vaginalis.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6097-6101(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 9-100.
RX PubMed=12051855; DOI=10.1016/s0022-2836(02)00051-7;
RA Crossnoe C.R., Germanas J.P., LeMagueres P., Mustata G., Krause K.L.;
RT "The crystal structure of Trichomonas vaginalis ferredoxin provides insight
RT into metronidazole activation.";
RL J. Mol. Biol. 318:503-518(2002).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions. It links pyruvate:ferredoxin
CC oxidoreductase to hydrogenase.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- SUBCELLULAR LOCATION: Hydrogenosome.
CC -!- MISCELLANEOUS: The propeptide may play a role in the targeting of this
CC protein to the organelle.
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DR EMBL; M33717; AAA30324.1; -; Genomic_DNA.
DR PIR; A36003; A36003.
DR PDB; 1L5P; X-ray; 2.20 A; A/B/C=9-100.
DR PDBsum; 1L5P; -.
DR AlphaFoldDB; P21149; -.
DR SMR; P21149; -.
DR VEuPathDB; TrichDB:TVAG_003900; -.
DR EvolutionaryTrace; P21149; -.
DR GO; GO:0042566; C:hydrogenosome; IEA:UniProtKB-SubCell.
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; IPR012675; Beta-grasp_dom_sf.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Electron transport;
KW Hydrogenosome; Iron; Iron-sulfur; Metal-binding; Transport.
FT PROPEP 1..8
FT /evidence="ECO:0000269|PubMed:1696716"
FT /id="PRO_0000008841"
FT CHAIN 9..100
FT /note="Ferredoxin"
FT /id="PRO_0000008842"
FT DOMAIN 9..100
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 52
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 55
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 85
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:1L5P"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:1L5P"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:1L5P"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1L5P"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1L5P"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1L5P"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:1L5P"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1L5P"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1L5P"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1L5P"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1L5P"
SQ SEQUENCE 100 AA; 10675 MW; 66ADB3EDAD3F4773 CRC64;
MLSQVCRFGT ITAVKGGVKK QLKFEDDQTL FTVLTEAGLM SADDTCQGNK ACGKCICKHV
SGKVAAEDDE KEFLEDQPAN ARLACAITLS GENDGAVFEL