HEMTB_CLOAB
ID HEMTB_CLOAB Reviewed; 129 AA.
AC Q97MX1;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Bacteriohemerythrin {ECO:0000255|HAMAP-Rule:MF_00556};
GN OrderedLocusNames=CA_C0069;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK78055.1; -; Genomic_DNA.
DR PIR; D96908; D96908.
DR RefSeq; NP_346715.1; NC_003030.1.
DR RefSeq; WP_010963397.1; NC_003030.1.
DR AlphaFoldDB; Q97MX1; -.
DR SMR; Q97MX1; -.
DR STRING; 272562.CA_C0069; -.
DR EnsemblBacteria; AAK78055; AAK78055; CA_C0069.
DR GeneID; 44996551; -.
DR KEGG; cac:CA_C0069; -.
DR PATRIC; fig|272562.8.peg.250; -.
DR eggNOG; COG2703; Bacteria.
DR HOGENOM; CLU_086902_2_0_9; -.
DR OMA; FKYADEA; -.
DR OrthoDB; 1991725at2; -.
DR Proteomes; UP000000814; 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..129
FT /note="Bacteriohemerythrin"
FT /id="PRO_0000191847"
FT BINDING 19
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 78
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 82
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 119
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
SQ SEQUENCE 129 AA; 15924 MW; F265B9EC0A69E6F3 CRC64;
MFVWKDEFEL GIDKIDNEHR KLFEIANKGY ELLKNEFYVD KYDKIMDIIV ELKEYAEFHF
SEEEDYLASI GYKKLFTHKL EHDSFIKKVE SFNIKEIDYD QDKYIQEMLD FVVTWIKEHI
LEKDREYID
