(data stored in ACNUC7421 zone)

SWISSPROT: A1AZN4_PARDP

ID   A1AZN4_PARDP            Unreviewed;       161 AA.
AC   A1AZN4;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   RecName: Full=Bacterioferritin {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|RuleBase:RU000623};
DE            EC=1.16.3.1 {ECO:0000256|PIRNR:PIRNR002560};
GN   OrderedLocusNames=Pden_0616 {ECO:0000313|EMBL:ABL68728.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68728.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Iron-storage protein, whose ferroxidase center binds
CC       Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates
CC       in the subsequent Fe(3+) oxide mineral core formation within the
CC       central cavity of the protein complex.
CC       {ECO:0000256|PIRNR:PIRNR002560}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC         Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
CC         EC=1.16.3.1; Evidence={ECO:0000256|PIRNR:PIRNR002560};
CC   -!- SIMILARITY: Belongs to the bacterioferritin family.
CC       {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|RuleBase:RU000623}.
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; CP000489; ABL68728.1; -; Genomic_DNA.
DR   RefSeq; WP_011746961.1; NC_008686.1.
DR   STRING; 318586.Pden_0616; -.
DR   PRIDE; A1AZN4; -.
DR   EnsemblBacteria; ABL68728; ABL68728; Pden_0616.
DR   KEGG; pde:Pden_0616; -.
DR   eggNOG; ENOG4108UQY; Bacteria.
DR   eggNOG; COG2193; LUCA.
DR   HOGENOM; HOG000262383; -.
DR   KO; K03594; -.
DR   OMA; FLHAKMQ; -.
DR   BioCyc; PDEN318586:G1GW1-623-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
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   Pfam; PF00210; Ferritin; 1.
DR   PIRSF; PIRSF002560; Bacterioferritin; 1.
DR   PRINTS; PR00601; BACFERRITIN.
DR   SUPFAM; SSF47240; SSF47240; 1.
DR   TIGRFAMs; TIGR00754; bfr; 1.
DR   PROSITE; PS00549; BACTERIOFERRITIN; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AZN4.
DR   SWISS-2DPAGE; A1AZN4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Heme {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|RuleBase:RU000623};
KW   Iron {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|PIRSR:PIRSR002560-1,
KW   ECO:0000256|RuleBase:RU000623};
KW   Iron storage {ECO:0000256|PIRNR:PIRNR002560,
KW   ECO:0000256|RuleBase:RU000623};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR002560,
KW   ECO:0000256|PIRSR:PIRSR002560-1, ECO:0000256|RuleBase:RU000623};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361}.
FT   DOMAIN        1    145       Ferritin-like diiron.
FT                                {ECO:0000259|PROSITE:PS50905}.
FT   METAL        18     18       Iron 1. {ECO:0000256|PIRSR:PIRSR002560-
FT                                1}.
FT   METAL        50     50       Iron 3. {ECO:0000256|PIRSR:PIRSR002560-
FT                                1}.
FT   METAL        51     51       Iron 1. {ECO:0000256|PIRSR:PIRSR002560-
FT                                1}.
FT   METAL        51     51       Iron 2. {ECO:0000256|PIRSR:PIRSR002560-
FT                                1}.
FT   METAL        52     52       Iron (heme axial ligand); shared with
FT                                dimeric partner. {ECO:0000256|PIRSR:
FT                                PIRSR002560-1}.
FT   METAL        54     54       Iron 1. {ECO:0000256|PIRSR:PIRSR002560-
FT                                1}.
FT   METAL        94     94       Iron 2. {ECO:0000256|PIRSR:PIRSR002560-
FT                                1}.
FT   METAL       127    127       Iron 1. {ECO:0000256|PIRSR:PIRSR002560-
FT                                1}.
FT   METAL       127    127       Iron 2. {ECO:0000256|PIRSR:PIRSR002560-
FT                                1}.
FT   METAL       130    130       Iron 2. {ECO:0000256|PIRSR:PIRSR002560-
FT                                1}.
SQ   SEQUENCE   161 AA;  18459 MW;  3E33944646C99523 CRC64;
     MKGDAKVIEY LNAALRSELT AVSQYWLHYR LQEDWGYGKV ADKSRAESIE EMHHADRLIQ
     RIIFLEGHPN LQKLDPLRIG QNLKETLESD LAAEHDARTL YIEAREYCDK VGDYVSKNLF
     DALLTDEEGH IDFLETQLGL YEEIGAQNYG QLNAKSADEA E
//

If you have problems or comments...

PBIL Back to PBIL home page