ID G0L3D5_ZOBGA Unreviewed; 170 AA.
AC G0L3D5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
DE EC=1.16.3.2 {ECO:0000256|RuleBase:RU361145};
GN Name=ftnA {ECO:0000313|EMBL:CAZ95372.1};
GN OrderedLocusNames=zobellia_1316 {ECO:0000313|EMBL:CAZ95372.1};
OS Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS NCIMB 13871 / Dsij).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zobellia.
OX NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ95372.1, ECO:0000313|Proteomes:UP000008898};
RN [1] {ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RG Genoscope - CEA;
RT "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAZ95372.1, ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RX PubMed=22513138; DOI=10.1111/j.1462-2920.2012.02751.x;
RA Thomas F., Barbeyron T., Tonon T., Genicot S., Czjzek M., Michel G.;
RT "Characterization of the first alginolytic operons in a marine bacterium:
RT from their emergence in marine Flavobacteriia to their independent
RT transfers to marine Proteobacteria and human gut Bacteroides.";
RL Environ. Microbiol. 14:2379-2394(2012).
CC -!- FUNCTION: Iron-storage protein. {ECO:0000256|RuleBase:RU361145}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide;
CC Xref=Rhea:RHEA:11972, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:78619; EC=1.16.3.2;
CC Evidence={ECO:0000256|RuleBase:RU361145};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU361145}.
CC -!- SIMILARITY: Belongs to the ferritin family. Prokaryotic subfamily.
CC {ECO:0000256|RuleBase:RU361145}.
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DR EMBL; FP476056; CAZ95372.1; -; Genomic_DNA.
DR RefSeq; WP_013992681.1; NZ_JAUOSS010000004.1.
DR AlphaFoldDB; G0L3D5; -.
DR STRING; 63186.ZOBELLIA_1316; -.
DR KEGG; zga:ZOBELLIA_1316; -.
DR PATRIC; fig|63186.3.peg.1301; -.
DR HOGENOM; CLU_065681_1_0_10; -.
DR OrthoDB; 9801481at2; -.
DR Proteomes; UP000008898; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR CDD; cd01055; Nonheme_Ferritin; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR001519; Ferritin.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009040; Ferritin-like_diiron.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR InterPro; IPR041719; Ferritin_prok.
DR PANTHER; PTHR11431; FERRITIN; 1.
DR PANTHER; PTHR11431:SF75; FERRITIN; 1.
DR Pfam; PF00210; Ferritin; 1.
DR SUPFAM; SSF47240; Ferritin-like; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU361145};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361145};
KW Iron storage {ECO:0000256|ARBA:ARBA00022434,
KW ECO:0000256|RuleBase:RU361145};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361145};
KW Oxidoreductase {ECO:0000313|EMBL:CAZ95372.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008898}.
FT DOMAIN 9..154
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000259|PROSITE:PS50905"
SQ SEQUENCE 170 AA; 19382 MW; BFFFC38CFCF49067 CRC64;
MKDIARQQMS IKVESMDMLN AQIQMEGKAS ASYLAMASWC DQRGYTGSAD FMYQQAAEER
EHMMKIFKFV NDCGGNAISP EVTNINHDFS SLEEVFETAL TQEIEVSKSI NRIVATARKN
SDFGVENFMQ WFITEQLEEE KSIRDILDLF ELMGRDGIAL KLIDERINAA
//
