HDOX2_STAAM
ID HDOX2_STAAM Reviewed; 108 AA.
AC Q99X56;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Heme oxygenase (staphylobilin-producing) 2 {ECO:0000255|HAMAP-Rule:MF_01272};
DE EC=1.14.99.48 {ECO:0000255|HAMAP-Rule:MF_01272};
DE AltName: Full=Heme-degrading monooxygenase 2 {ECO:0000255|HAMAP-Rule:MF_01272};
DE AltName: Full=Iron-regulated surface determinant 2 {ECO:0000255|HAMAP-Rule:MF_01272};
DE AltName: Full=Iron-responsive surface determinant 2 {ECO:0000255|HAMAP-Rule:MF_01272};
GN Name=isdI; OrderedLocusNames=SAV0165;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=15520015; DOI=10.1074/jbc.m409526200;
RA Wu R., Skaar E.P., Zhang R., Joachimiak G., Gornicki P., Schneewind O.,
RA Joachimiak A.;
RT "Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with
RT structural similarity to monooxygenases.";
RL J. Biol. Chem. 280:2840-2846(2005).
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 oxo-bilirubin chromophore staphylobilin (a
CC mixture of the linear tetrapyrroles 5-oxo-delta-bilirubin and 15-oxo-
CC beta-bilirubin) in the presence of a suitable electron donor such as
CC ascorbate or NADPH--cytochrome P450 reductase, with subsequent release
CC of free iron. {ECO:0000255|HAMAP-Rule:MF_01272,
CC ECO:0000269|PubMed:15520015}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5 AH2 + 2 H(+) + heme b + 4 O2 = 5 A + delta-staphylobilin +
CC Fe(2+) + formaldehyde + 4 H2O; Xref=Rhea:RHEA:37039,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:60344, ChEBI:CHEBI:74361;
CC EC=1.14.99.48; Evidence={ECO:0000255|HAMAP-Rule:MF_01272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5 AH2 + 2 H(+) + heme b + 4 O2 = 5 A + beta-staphylobilin +
CC Fe(2+) + formaldehyde + 4 H2O; Xref=Rhea:RHEA:37363,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:60344, ChEBI:CHEBI:74362;
CC EC=1.14.99.48; Evidence={ECO:0000255|HAMAP-Rule:MF_01272};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01272,
CC ECO:0000269|PubMed:15520015}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01272}.
CC -!- MISCELLANEOUS: IsdI seems to carry out oxygenation of the heme without
CC the assistance of any of the prosthetic groups or cofactors normally
CC associated with activation of molecular oxygen.
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; BA000017; BAB56327.1; -; Genomic_DNA.
DR RefSeq; WP_000480603.1; NC_002758.2.
DR PDB; 1SQE; X-ray; 1.50 A; A/B=1-108.
DR PDBsum; 1SQE; -.
DR AlphaFoldDB; Q99X56; -.
DR SMR; Q99X56; -.
DR PaxDb; Q99X56; -.
DR EnsemblBacteria; BAB56327; BAB56327; SAV0165.
DR KEGG; sav:SAV0165; -.
DR HOGENOM; CLU_141544_2_1_9; -.
DR OMA; FRESHSH; -.
DR PhylomeDB; Q99X56; -.
DR BioCyc; SAUR158878:SAV_RS00970-MON; -.
DR BRENDA; 1.14.99.48; 3352.
DR EvolutionaryTrace; Q99X56; -.
DR Proteomes; UP000002481; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase;
KW Oxidoreductase.
FT CHAIN 1..108
FT /note="Heme oxygenase (staphylobilin-producing) 2"
FT /id="PRO_0000270088"
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 21..28
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1SQE"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1SQE"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:1SQE"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1SQE"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:1SQE"
FT STRAND 46..58
FT /evidence="ECO:0007829|PDB:1SQE"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:1SQE"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:1SQE"
FT STRAND 91..107
FT /evidence="ECO:0007829|PDB:1SQE"
SQ SEQUENCE 108 AA; 12791 MW; 8AF2718571451004 CRC64;
MFMAENRLQL QKGSAEETIE RFYNRQGIET IEGFQQMFVT KTLNTEDTDE VKILTIWESE
DSFNNWLNSD VFKEAHKNVR LKSDDDGQQS PILSNKVFKY DIGYHYQK
