HEMTB_AQUAE
ID HEMTB_AQUAE Reviewed; 131 AA.
AC O67614;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Bacteriohemerythrin {ECO:0000255|HAMAP-Rule:MF_00556};
GN OrderedLocusNames=aq_1719;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Oxygen-binding protein. May be involved in a storage
CC mechanism or for delivery to oxygen-requiring enzymes. The oxygen-
CC binding site contains two iron atoms. {ECO:0000255|HAMAP-
CC Rule:MF_00556}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00556}.
CC -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000255|HAMAP-
CC Rule:MF_00556}.
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DR EMBL; AE000657; AAC07584.1; -; Genomic_DNA.
DR PIR; D70448; D70448.
DR RefSeq; NP_214180.1; NC_000918.1.
DR RefSeq; WP_010881117.1; NC_000918.1.
DR AlphaFoldDB; O67614; -.
DR SMR; O67614; -.
DR STRING; 224324.aq_1719; -.
DR EnsemblBacteria; AAC07584; AAC07584; aq_1719.
DR KEGG; aae:aq_1719; -.
DR PATRIC; fig|224324.8.peg.1322; -.
DR eggNOG; COG2703; Bacteria.
DR HOGENOM; CLU_086902_1_3_0; -.
DR InParanoid; O67614; -.
DR OMA; MDTVTAM; -.
DR OrthoDB; 1991725at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-UniRule.
DR CDD; cd12107; Hemerythrin; 1.
DR Gene3D; 1.20.120.50; -; 1.
DR HAMAP; MF_00556; Hemerythrin; 1.
DR InterPro; IPR023504; Bacteriohemerythrin-like.
DR InterPro; IPR016131; Haemerythrin_Fe_BS.
DR InterPro; IPR012312; Hemerythrin-like.
DR InterPro; IPR035938; Hemerythrin-like_sf.
DR InterPro; IPR012827; Hemerythrin_metal-bd.
DR Pfam; PF01814; Hemerythrin; 1.
DR SUPFAM; SSF47188; SSF47188; 1.
DR TIGRFAMs; TIGR02481; hemeryth_dom; 1.
DR PROSITE; PS00550; HEMERYTHRINS; 1.
PE 3: Inferred from homology;
KW Iron; Metal-binding; Oxygen transport; Reference proteome; Transport.
FT CHAIN 1..131
FT /note="Bacteriohemerythrin"
FT /id="PRO_0000191845"
FT BINDING 20
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 23
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 56
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 75
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 117
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
SQ SEQUENCE 131 AA; 15964 MW; 1494DD8CDFAB235C CRC64;
MLIRPNKVQK VGNLFMDTVH EEEIRLLNQL YDTLMKKDVE KADQLMDELL VDLEDHFTTE
EELMREFEFF AYPMHKAEHD TMRKRFKEVY DKWKKEKNPE EVVRFLKEEF VPWLKSHVAR
WDSTTAQQLG D