HEMTB_PSEAB
ID HEMTB_PSEAB Reviewed; 153 AA.
AC Q02KG3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Bacteriohemerythrin {ECO:0000255|HAMAP-Rule:MF_00556};
GN OrderedLocusNames=PA14_42860;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ10858.1; -; Genomic_DNA.
DR RefSeq; WP_003087637.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02KG3; -.
DR SMR; Q02KG3; -.
DR PRIDE; Q02KG3; -.
DR EnsemblBacteria; ABJ10858; ABJ10858; PA14_42860.
DR KEGG; pau:PA14_42860; -.
DR HOGENOM; CLU_086902_2_1_6; -.
DR OMA; AKHFKHE; -.
DR BioCyc; PAER208963:G1G74-3593-MON; -.
DR Proteomes; UP000000653; 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; Transport.
FT CHAIN 1..153
FT /note="Bacteriohemerythrin"
FT /id="PRO_1000017981"
FT BINDING 21
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 76
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 80
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 115
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="1"
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"
SQ SEQUENCE 153 AA; 17853 MW; 48A4913944398F40 CRC64;
MAHLVWQDDL NTGIQVIDNQ HKRIVEMINH LHDAQQGKEH AAIAEVIEEL VDYTLSHFAF
EETLMEDAGY QFSRAHKKIH ELFIRRVSEY RVRFQAGEDV GDELKGLLSR WLFNHIRNDD
AGYVDAVRHS MSELVKDKSE GGWLSRSMKR FFG