HDOX_LISMO
ID HDOX_LISMO Reviewed; 121 AA.
AC Q92EH3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
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}; OrderedLocusNames=lmo0484;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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 [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; Evidence={ECO:0000255|HAMAP-
CC 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; AL591975; CAC98563.1; -; Genomic_DNA.
DR PIR; AE1135; AE1135.
DR PIR; AG1493; AG1493.
DR RefSeq; NP_464012.1; NC_003210.1.
DR RefSeq; WP_003721271.1; NZ_CP023861.1.
DR AlphaFoldDB; Q92EH3; -.
DR SMR; Q92EH3; -.
DR STRING; 169963.lmo0484; -.
DR PaxDb; Q92EH3; -.
DR EnsemblBacteria; CAC98563; CAC98563; CAC98563.
DR GeneID; 61169521; -.
DR GeneID; 66485482; -.
DR GeneID; 985220; -.
DR KEGG; lmo:lmo0484; -.
DR PATRIC; fig|169963.11.peg.503; -.
DR eggNOG; COG2329; Bacteria.
DR HOGENOM; CLU_141544_2_0_9; -.
DR OMA; FRESHSH; -.
DR PhylomeDB; Q92EH3; -.
DR BioCyc; LMON169963:LMO0484-MON; -.
DR Proteomes; UP000000817; 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 HAMAP; MF_01272; Heme_degrading_monooxygenase; 1.
DR InterPro; IPR007138; ABM_dom.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR023953; IsdG.
DR Pfam; PF03992; ABM; 1.
DR SUPFAM; SSF54909; SSF54909; 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..121
FT /note="Heme-degrading monooxygenase"
FT /id="PRO_0000270078"
FT DOMAIN 2..101
FT /note="ABM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
FT REGION 76..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 6
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
FT BINDING 84
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 74
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
SQ SEQUENCE 121 AA; 13785 MW; 95674EA508DA2D49 CRC64;
MIIVTNTIKV EKGAAEHVIR QFTGANGDGH PTKDIAEVEG FLGFELWHSK PEDKDYEEVV
VTSKWESEEA QRNWVKSDSF KKAHGRTKDT REQREDRKGI VGNAIARFEV VHVQNPVIVE
K
