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Database: UniProt
Entry: A0A1I3Y321_9PROT
LinkDB: A0A1I3Y321_9PROT
Original site: A0A1I3Y321_9PROT 
ID   A0A1I3Y321_9PROT        Unreviewed;       115 AA.
AC   A0A1I3Y321;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=ferroxidase {ECO:0000256|ARBA:ARBA00013107};
DE            EC=1.16.3.1 {ECO:0000256|ARBA:ARBA00013107};
DE   Flags: Fragment;
GN   ORFNames=SAMN05216302_10031 {ECO:0000313|EMBL:SFK26228.1};
OS   Nitrosomonas aestuarii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=52441 {ECO:0000313|EMBL:SFK26228.1, ECO:0000313|Proteomes:UP000199533};
RN   [1] {ECO:0000313|Proteomes:UP000199533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm69 {ECO:0000313|Proteomes:UP000199533};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Iron-storage protein, whose ferroxidase center binds Fe(2+)
CC       ions, oxidizes them by dioxygen to Fe(3+), and participates in the
CC       subsequent Fe(3+) oxide mineral core formation within the central
CC       cavity of the protein complex. {ECO:0000256|ARBA:ARBA00037326}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
CC   -!- SUBUNIT: Oligomer of 24 subunits, arranged as 12 dimers, that are
CC       packed together to form an approximately spherical molecule with a
CC       central cavity, in which large amounts of iron can be deposited.
CC       {ECO:0000256|ARBA:ARBA00011713}.
CC   -!- SIMILARITY: Belongs to the bacterioferritin family.
CC       {ECO:0000256|ARBA:ARBA00008093}.
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DR   EMBL; FOSP01000003; SFK26228.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3Y321; -.
DR   STRING; 52441.SAMN05216302_10031; -.
DR   OrthoDB; 9800505at2; -.
DR   Proteomes; UP000199533; Unassembled WGS sequence.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:InterPro.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   CDD; cd00907; Bacterioferritin; 1.
DR   Gene3D; 1.20.1260.10; -; 1.
DR   InterPro; IPR002024; Bacterioferritin.
DR   InterPro; IPR012347; Ferritin-like.
DR   InterPro; IPR009040; Ferritin-like_diiron.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR008331; Ferritin_DPS_dom.
DR   PANTHER; PTHR30295; BACTERIOFERRITIN; 1.
DR   PANTHER; PTHR30295:SF9; BACTERIOFERRITIN; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   PIRSF; PIRSF002560; Bacterioferritin; 1.
DR   PRINTS; PR00601; BACFERRITIN.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617};
KW   Iron {ECO:0000256|PIRSR:PIRSR002560-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR002560-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199533}.
FT   DOMAIN          1..106
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000259|PROSITE:PS50905"
FT   BINDING         6
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT   BINDING         10
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT   BINDING         11
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT   BINDING         11
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT   BINDING         14
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT   BINDING         54
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT   BINDING         88
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT   BINDING         88
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT   BINDING         91
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:SFK26228.1"
SQ   SEQUENCE   115 AA;  13326 MW;  029E8C9A847DE9E1 CRC64;
     YERIDHEMDD EKQHADLLIK RILLLEGVPA VSNRSPLRIG KDVPAMLRND LELERSVITA
     LRNAIAVCEQ EQDYQTREIL EGLLSETEED HAYWLEKQLG LIEKVGLQNY LQSQI
//
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