IRO_ACIFR
ID IRO_ACIFR Reviewed; 90 AA.
AC P50500;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Iron oxidase;
DE EC=1.16.3.-;
DE AltName: Full=Fe(II) oxidase;
DE Flags: Precursor;
GN Name=iro;
OS Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=920;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 38-62.
RC STRAIN=Fe1;
RX PubMed=1317860; DOI=10.1016/s0021-9258(19)49902-x;
RA Kusano T., Takeshima T., Sugawara K., Inoue C., Shiratori T., Yano T.,
RA Fukumori Y., Yamanaka T.;
RT "Molecular cloning of the gene encoding Thiobacillus ferrooxidans Fe(II)
RT oxidase. High homology of the gene product with HiPIP.";
RL J. Biol. Chem. 267:11242-11247(1992).
CC -!- FUNCTION: Catalyzes the oxidation of Fe(2+) to Fe(3+) coupled to
CC cytochrome c552 reduction.
CC -!- SUBUNIT: Homomultimer.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|PROSITE-ProRule:PRU00705}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the high-potential iron-sulfur protein (HiPIP)
CC family. {ECO:0000255|PROSITE-ProRule:PRU00705}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X57324; CAA40594.1; -; Genomic_DNA.
DR PIR; S23259; S23259.
DR RefSeq; WP_064219818.1; NZ_LVXZ01000181.1.
DR AlphaFoldDB; P50500; -.
DR SMR; P50500; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR Gene3D; 4.10.490.10; -; 1.
DR InterPro; IPR000170; High_potential_FeS_prot.
DR InterPro; IPR036369; HIPIP_sf.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR SUPFAM; SSF57652; SSF57652; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS51373; HIPIP; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Periplasm; Signal; Transport.
FT SIGNAL 1..37
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:1317860"
FT CHAIN 38..90
FT /note="Iron oxidase"
FT /id="PRO_0000013440"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
FT BINDING 82
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
SQ SEQUENCE 90 AA; 9410 MW; 75E9AA0688E44ADA CRC64;
MSEKDKMITR RDALRNIAVV VGSVATTTMM GVGVADAGSM PKAAVQYQDT PKGKDHCSVC
AQFIAPHSCK VVAGNISPNG WCVAFVPKSA
