HEMTB_METCA
ID HEMTB_METCA Reviewed; 131 AA.
AC Q60AX2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Bacteriohemerythrin;
DE AltName: Full=McHr;
GN OrderedLocusNames=MCA0715;
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
RN [2]
RP FUNCTION, SUBUNIT, IRON-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15885093; DOI=10.1111/j.1742-4658.2005.04663.x;
RA Karlsen O.A., Ramsevik L., Bruseth L.J., Larsen O., Brenner A.,
RA Berven F.S., Jensen H.B., Lillehaug J.R.;
RT "Characterization of a prokaryotic haemerythrin from the methanotrophic
RT bacterium Methylococcus capsulatus (Bath).";
RL FEBS J. 272:2428-2440(2005).
RN [3]
RP SUBUNIT.
RX PubMed=18397812; DOI=10.1016/j.jinorgbio.2008.02.008;
RA Kao W.C., Wang V.C., Huang Y.C., Yu S.S., Chang T.C., Chan S.I.;
RT "Isolation, purification and characterization of hemerythrin from
RT Methylococcus capsulatus (Bath).";
RL J. Inorg. Biochem. 102:1607-1614(2008).
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:0000269|PubMed:15885093}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15885093,
CC ECO:0000269|PubMed:18397812}.
CC -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000305}.
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DR EMBL; AE017282; AAU93139.1; -; Genomic_DNA.
DR RefSeq; WP_010960053.1; NC_002977.6.
DR PDB; 4XPW; X-ray; 1.17 A; A=1-131.
DR PDB; 4XPX; X-ray; 1.03 A; A=2-131.
DR PDB; 4XPY; X-ray; 1.13 A; A=1-131.
DR PDB; 4XQ1; X-ray; 1.40 A; A=1-131.
DR PDBsum; 4XPW; -.
DR PDBsum; 4XPX; -.
DR PDBsum; 4XPY; -.
DR PDBsum; 4XQ1; -.
DR AlphaFoldDB; Q60AX2; -.
DR SMR; Q60AX2; -.
DR STRING; 243233.MCA0715; -.
DR EnsemblBacteria; AAU93139; AAU93139; MCA0715.
DR KEGG; mca:MCA0715; -.
DR eggNOG; COG2703; Bacteria.
DR HOGENOM; CLU_086902_3_1_6; -.
DR OMA; MLWKDKY; -.
DR OrthoDB; 1991725at2; -.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR CDD; cd12107; Hemerythrin; 1.
DR Gene3D; 1.20.120.50; -; 1.
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 1: Evidence at protein level;
KW 3D-structure; Iron; Metal-binding; Oxygen transport; Reference proteome;
KW Transport.
FT CHAIN 1..131
FT /note="Bacteriohemerythrin"
FT /id="PRO_0000343361"
FT BINDING 22
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 77
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 81
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 117
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:4XPX"
FT HELIX 16..35
FT /evidence="ECO:0007829|PDB:4XPX"
FT HELIX 41..68
FT /evidence="ECO:0007829|PDB:4XPX"
FT HELIX 74..96
FT /evidence="ECO:0007829|PDB:4XPX"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:4XPX"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:4XPX"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:4XPX"
SQ SEQUENCE 131 AA; 14715 MW; 3ED34BBE2F3C178E CRC64;
MALMTWTAAE FGTNVGFADD QHKTIFDMVN KLHDTAATGN RSEIGKQLDA LIDYVVMHFK
SEETEMQKKG YADFAAHKAE HDKLVGVCAD LQKKFHAGEA EVNQDTTRFV RDWLVNHIPK
VDKLYGPCLS A
