ID V6V4D9_CORUL Unreviewed; 212 AA.
AC V6V4D9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=heme oxygenase (biliverdin-producing) {ECO:0000256|ARBA:ARBA00012360};
DE EC=1.14.14.18 {ECO:0000256|ARBA:ARBA00012360};
GN ORFNames=D881_09170 {ECO:0000313|EMBL:ESU57941.1};
OS Corynebacterium ulcerans NCTC 12077.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1258583 {ECO:0000313|EMBL:ESU57941.1, ECO:0000313|Proteomes:UP000018265};
RN [1] {ECO:0000313|EMBL:ESU57941.1, ECO:0000313|Proteomes:UP000018265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 12077 {ECO:0000313|EMBL:ESU57941.1,
RC ECO:0000313|Proteomes:UP000018265};
RA Pethick F.E., Lainson A.F., Yaga R., Flockhart A., Walker C.A., Smith D.G.,
RA Donachie W., Fontaine M.C.;
RT "Draft genome sequence of the Corynebacterium ulcerans type strain, NCTC
RT 12077.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001701};
CC -!- SIMILARITY: Belongs to the heme oxygenase family.
CC {ECO:0000256|ARBA:ARBA00006134}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESU57941.1}.
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DR EMBL; AYUJ01000007; ESU57941.1; -; Genomic_DNA.
DR RefSeq; WP_023636034.1; NZ_AYUJ01000007.1.
DR AlphaFoldDB; V6V4D9; -.
DR PATRIC; fig|1258583.3.peg.1878; -.
DR OrthoDB; 5493802at2; -.
DR Proteomes; UP000018265; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000343-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000343-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000343-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT BINDING 13
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
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:0000256|PIRSR:PIRSR000343-2"
FT BINDING 130
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 177
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
SQ SEQUENCE 212 AA; 23957 MW; 6E09A4CBE113854D CRC64;
MTTATKGLAA ELKESTAKAH ADAEHSSFMS DLIEGRLDAE AFIRLQEQAW LFYTALEEAA
DVVRAEGFAT DLLDPKLNRA DILAEDIDNF HGNDQWRKDL IALPAVRDYV ARLNHIRDEA
HGPALVAHHY VRYLGDLSGG QVIARMMSRH YGVDEKSLKF YSFEGIDKLK VYKDNYRQHL
DDLHLSAEAV EQMLEEASAA FSYNQRVFAE LA
//
