ID   HDOX_SHOC1              Reviewed;         107 AA.
AC   Q5WCF2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 99.
DE   RecName: Full=Heme-degrading monooxygenase {ECO:0000255|HAMAP-Rule:MF_01272};
DE            EC=1.14.14.18 {ECO:0000255|HAMAP-Rule:MF_01272};
DE   AltName: Full=Heme oxygenase {ECO:0000255|HAMAP-Rule:MF_01272};
DE   AltName: Full=Iron-regulated surface determinant {ECO:0000255|HAMAP-Rule:MF_01272};
DE   AltName: Full=Iron-responsive surface determinant {ECO:0000255|HAMAP-Rule:MF_01272};
GN   Name=isdG {ECO:0000255|HAMAP-Rule:MF_01272};
GN   OrderedLocusNames=ABC3425;
OS   Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Allows bacterial pathogens to use the host heme as an iron
CC       source. Catalyzes the oxidative degradation of the heme macrocyclic
CC       porphyrin ring to the biliverdin in the presence of a suitable electron
CC       donor such as ascorbate or NADPH--cytochrome P450 reductase, with
CC       subsequent release of free iron. {ECO:0000255|HAMAP-Rule:MF_01272}.
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:0000255|HAMAP-Rule:MF_01272};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01272}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01272}.
CC   -!- SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase
CC       family. Heme-degrading monooxygenase IsdG subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01272}.
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DR   EMBL; AP006627; BAD65958.1; -; Genomic_DNA.
DR   RefSeq; WP_011248264.1; NC_006582.1.
DR   AlphaFoldDB; Q5WCF2; -.
DR   SMR; Q5WCF2; -.
DR   STRING; 66692.ABC3425; -.
DR   KEGG; bcl:ABC3425; -.
DR   eggNOG; COG2329; Bacteria.
DR   HOGENOM; CLU_141544_2_1_9; -.
DR   OrthoDB; 384737at2; -.
DR   Proteomes; UP000001168; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042167; P:heme catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0033212; P:iron import into cell; IEA:InterPro.
DR   Gene3D; 3.30.70.100; -; 1.
DR   HAMAP; MF_01272; Heme_degrading_monooxygenase; 1.
DR   InterPro; IPR007138; ABM_dom.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR023953; IsdG.
DR   PANTHER; PTHR34474:SF4; HEME OXYGENASE (STAPHYLOBILIN-PRODUCING) 1; 1.
DR   PANTHER; PTHR34474; SIGNAL TRANSDUCTION PROTEIN TRAP; 1.
DR   Pfam; PF03992; ABM; 1.
DR   SUPFAM; SSF54909; Dimeric alpha+beta barrel; 1.
DR   PROSITE; PS51725; ABM; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..107
FT                   /note="Heme-degrading monooxygenase"
FT                   /id="PRO_0000270074"
FT   DOMAIN          2..93
FT                   /note="ABM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
FT   BINDING         6
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
FT   BINDING         76
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
FT   SITE            66
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
SQ   SEQUENCE   107 AA;  12302 MW;  31ED9218A7A4B6D8 CRC64;
     MVIVANKTLI RKGEGHKLVK RFDKIGKIEM QKGFLGLEVL VNAKEKEVDE VTISTRWETK
     ADFHAWTKSE AFREAHSGRN ARPDYILGNE IEFYDVEVVR MPIAQAQ
//