HMUO_CORDI
ID HMUO_CORDI Reviewed; 215 AA.
AC P71119;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Heme oxygenase;
DE EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
GN Name=hmuO; OrderedLocusNames=DIP1669;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C7;
RX PubMed=9006041; DOI=10.1128/jb.179.3.838-845.1997;
RA Schmitt M.P.;
RT "Utilization of host iron sources by Corynebacterium diphtheriae:
RT identification of a gene whose product is homologous to eukaryotic heme
RT oxygenases and is required for acquisition of iron from heme and
RT hemoglobin.";
RL J. Bacteriol. 179:838-845(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
CC -!- FUNCTION: Allows the bacteria to use the host heme as an iron source.
CC Involved in the oxidation of heme and subsequent release of iron from
CC the heme moiety.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] =
CC biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:60344; EC=1.14.14.18;
CC Evidence={ECO:0000250|UniProtKB:O48782};
CC -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
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DR EMBL; U73860; AAC44832.1; -; Genomic_DNA.
DR EMBL; BX248358; CAE50198.1; -; Genomic_DNA.
DR RefSeq; WP_010935240.1; NC_002935.2.
DR PDB; 1IW0; X-ray; 1.40 A; A/B/C=1-215.
DR PDB; 1IW1; X-ray; 1.50 A; A/B/C=1-215.
DR PDB; 1V8X; X-ray; 1.85 A; A/B/C=1-215.
DR PDB; 1WNV; X-ray; 1.85 A; A/B/C=1-215.
DR PDB; 1WNW; X-ray; 1.70 A; A/B/C=1-215.
DR PDB; 1WNX; X-ray; 1.85 A; A/B=1-215.
DR PDB; 1WZD; X-ray; 1.35 A; A/B=1-215.
DR PDB; 1WZF; X-ray; 1.85 A; A/B=1-215.
DR PDB; 1WZG; X-ray; 1.75 A; A/B=1-215.
DR PDBsum; 1IW0; -.
DR PDBsum; 1IW1; -.
DR PDBsum; 1V8X; -.
DR PDBsum; 1WNV; -.
DR PDBsum; 1WNW; -.
DR PDBsum; 1WNX; -.
DR PDBsum; 1WZD; -.
DR PDBsum; 1WZF; -.
DR PDBsum; 1WZG; -.
DR AlphaFoldDB; P71119; -.
DR BMRB; P71119; -.
DR SMR; P71119; -.
DR DIP; DIP-61184N; -.
DR STRING; 257309.DIP1669; -.
DR DrugBank; DB02772; Sucrose.
DR EnsemblBacteria; CAE50198; CAE50198; DIP1669.
DR KEGG; cdi:DIP1669; -.
DR HOGENOM; CLU_057050_2_0_11; -.
DR OMA; KKSHTMA; -.
DR OrthoDB; 1371367at2; -.
DR BioCyc; MetaCyc:MON-20096; -.
DR BRENDA; 1.14.14.18; 1645.
DR EvolutionaryTrace; P71119; -.
DR Proteomes; UP000002198; Chromosome.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006788; P:heme oxidation; IEA:InterPro.
DR CDD; cd19165; HemeO; 1.
DR Gene3D; 1.20.910.10; -; 1.
DR InterPro; IPR002051; Haem_Oase.
DR InterPro; IPR016053; Haem_Oase-like.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR018207; Haem_oxygenase_CS.
DR PANTHER; PTHR10720; PTHR10720; 1.
DR Pfam; PF01126; Heme_oxygenase; 1.
DR PIRSF; PIRSF000343; Haem_Oase; 1.
DR PRINTS; PR00088; HAEMOXYGNASE.
DR SUPFAM; SSF48613; SSF48613; 1.
DR PROSITE; PS00593; HEME_OXYGENASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..215
FT /note="Heme oxygenase"
FT /id="PRO_0000209703"
FT BINDING 20
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CONFLICT 34
FT /note="E -> K (in Ref. 1; AAC44832)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="A -> V (in Ref. 1; AAC44832)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..93
FT /note="DG -> GS (in Ref. 1; AAC44832)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="N -> H (in Ref. 1; AAC44832)"
FT /evidence="ECO:0000305"
FT HELIX 8..24
FT /evidence="ECO:0007829|PDB:1IW0"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:1IW0"
FT HELIX 39..66
FT /evidence="ECO:0007829|PDB:1IW0"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1IW0"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1IW0"
FT HELIX 80..91
FT /evidence="ECO:0007829|PDB:1IW0"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1IW0"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:1IW0"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:1IW0"
FT HELIX 122..151
FT /evidence="ECO:0007829|PDB:1IW0"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1IW0"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:1IW0"
FT HELIX 169..182
FT /evidence="ECO:0007829|PDB:1IW0"
FT HELIX 187..212
FT /evidence="ECO:0007829|PDB:1IW0"
SQ SEQUENCE 215 AA; 24116 MW; 60D9E8E2ED7ED456 CRC64;
MTTATAGLAV ELKQSTAQAH EKAEHSTFMS DLLEGRLGVA EFTRLQEQAW LFYTALEQAA
DAVRASGFAE SLLDPALNRA EVLARDLDKL NDGSEWRSRI TASPAVIDYV NRLEEIRDNV
DGPALVAHHY VRYLGDLSGG QVIARMMQRH YGVDPEALGF YHFEGIAKLK VYKDEYREKL
NNLELSDEQR ENLLKEATDA FVFNHQVFAD LGKGL
