ID   HEMTB_METJA             Reviewed;         147 AA.
AC   Q58157;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Bacteriohemerythrin {ECO:0000255|HAMAP-Rule:MF_00556};
GN   OrderedLocusNames=MJ0747;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB98740.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L77117; AAB98740.1; ALT_INIT; Genomic_DNA.
DR   PIR; C64393; C64393.
DR   RefSeq; WP_064496610.1; NC_000909.1.
DR   AlphaFoldDB; Q58157; -.
DR   SMR; Q58157; -.
DR   STRING; 243232.MJ_0747; -.
DR   EnsemblBacteria; AAB98740; AAB98740; MJ_0747.
DR   GeneID; 1451624; -.
DR   KEGG; mja:MJ_0747; -.
DR   eggNOG; arCOG06577; Archaea.
DR   HOGENOM; CLU_086902_2_2_2; -.
DR   InParanoid; Q58157; -.
DR   OMA; AKHFKHE; -.
DR   PhylomeDB; Q58157; -.
DR   Proteomes; UP000000805; 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..147
FT                   /note="Bacteriohemerythrin"
FT                   /id="PRO_0000191844"
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         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         64
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT   BINDING         64
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         83
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT   BINDING         120
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT   BINDING         125
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT   BINDING         125
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
SQ   SEQUENCE   147 AA;  17478 MW;  A7B85A8542C17670 CRC64;
     MKKEIIKWSK DFETGIKAFD DEHKILVKTL NDIYNLLNEG KRDEAKELLK RRVVNYAAKH
     FKHEEEVMEK YGYPDLERHR KTHEIFVKTV IEKLLPKIEE GSENDFRSAL SFLVGWLTMH
     IAKPDKKYGE WFKEKGIVIE DEAVKID