(data stored in SCRATCH zone)

SWISSPROT: Q2IMD9_ANADE

ID   Q2IMD9_ANADE            Unreviewed;       158 AA.
AC   Q2IMD9;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 96.
DE   RecName: Full=Bacterioferritin {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|RuleBase:RU000623};
DE            EC=1.16.3.1 {ECO:0000256|PIRNR:PIRNR002560};
GN   OrderedLocusNames=Adeh_0191 {ECO:0000313|EMBL:ABC79968.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79968.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|EMBL:ABC79968.1, ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|EMBL:ABC79968.1,
RC   ECO:0000313|Proteomes:UP000001935};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-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}.
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DR   EMBL; CP000251; ABC79968.1; -; Genomic_DNA.
DR   RefSeq; WP_011419251.1; NC_007760.1.
DR   STRING; 290397.Adeh_0191; -.
DR   EnsemblBacteria; ABC79968; ABC79968; Adeh_0191.
DR   KEGG; ade:Adeh_0191; -.
DR   eggNOG; ENOG4108UQY; Bacteria.
DR   eggNOG; COG2193; LUCA.
DR   HOGENOM; HOG000262383; -.
DR   KO; K03594; -.
DR   OMA; FLHAKMQ; -.
DR   BioCyc; ADEH290397:G1G5W-197-MONOMER; -.
DR   Proteomes; UP000001935; Chromosome.
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; Q2IMD9.
DR   SWISS-2DPAGE; Q2IMD9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
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:UP000001935}.
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        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   158 AA;  17812 MW;  AD391205ECC4DD5A CRC64;
     MKGDAKVLDV LNEVLTNELT AINQYFLHAR VCENWGYDRL YAKFRAESID EMKDADHLIE
     RILYLDGMPN VQKLAKINIG ESVPEILAAD LDLEKHAIGV LNRGIETCRN AGDNGSADLL
     EDILEGEEEH ANWLETQLTA IDQIGVQNYL TEQLKKDS
//

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