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 27-MAR-2024, entry version 138. 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; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; 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 CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA- CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, CC ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18; CC Evidence={ECO:0000250|UniProtKB:O48782}; CC -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 KEGG; cdi:DIP1669; -. DR HOGENOM; CLU_057050_2_0_11; -. DR BioCyc; MetaCyc:MONOMER-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; Heme oxygenase-like; 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; HEME OXYGENASE; 1. DR PANTHER; PTHR10720:SF0; HEME OXYGENASE; 1. DR Pfam; PF01126; Heme_oxygenase; 1. DR PIRSF; PIRSF000343; Haem_Oase; 1. DR PRINTS; PR00088; HAEMOXYGNASE. DR SUPFAM; SSF48613; Heme oxygenase-like; 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 //