HDOX2_STAAN
ID HDOX2_STAAN Reviewed; 108 AA.
AC Q7A827;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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, ECO:0000269|PubMed:20180905};
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=SA0160;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-108 IN COMPLEX WITH HEME,
RP FUNCTION, AND SUBUNIT.
RX PubMed=18713745; DOI=10.1074/jbc.m709486200;
RA Lee W.C., Reniere M.L., Skaar E.P., Murphy M.E.;
RT "Ruffling of metalloporphyrins bound to IsdG and IsdI, two heme-degrading
RT enzymes in Staphylococcus aureus.";
RL J. Biol. Chem. 283:30957-30963(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-108 IN COMPLEX WITH HEME,
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=20180905; DOI=10.1111/j.1365-2958.2010.07076.x;
RA Reniere M.L., Ukpabi G.N., Harry S.R., Stec D.F., Krull R., Wright D.W.,
RA Bachmann B.O., Murphy M.E., Skaar E.P.;
RT "The IsdG-family of haem oxygenases degrades haem to a novel chromophore.";
RL Mol. Microbiol. 75:1529-1538(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-108 IN COMPLEX WITH HEME, AND
RP SUBUNIT.
RA Takayama S.J., Ukpabi G.N., Murphy M.E.P., Mauk A.G.;
RT "Heme ruffling enables the catalytic activity of the heme degrading enzyme
RT IsdI.";
RL Submitted (JAN-2011) to the PDB data bank.
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-108 OF MUTANT THR-66 IN COMPLEX
RP WITH HEME, MUTAGENESIS OF TRP-66, AND SUBUNIT.
RX PubMed=22891243; DOI=10.1074/jbc.m112.393249;
RA Ukpabi G., Takayama S.J., Mauk A.G., Murphy M.E.;
RT "Inactivation of the heme degrading enzyme IsdI by an active site
RT substitution that diminishes heme ruffling.";
RL J. Biol. Chem. 287:34179-34188(2012).
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:18713745, ECO:0000269|PubMed:20180905}.
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 ECO:0000269|PubMed:20180905};
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 ECO:0000269|PubMed:20180905};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01272,
CC ECO:0000269|PubMed:18713745, ECO:0000269|PubMed:20180905,
CC ECO:0000269|PubMed:22891243, ECO:0000269|Ref.5}.
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; BA000018; BAB41380.1; -; Genomic_DNA.
DR PIR; A89778; A89778.
DR RefSeq; WP_000480603.1; NC_002745.2.
DR PDB; 2ZDP; X-ray; 1.50 A; A/B=1-108.
DR PDB; 3LGM; X-ray; 1.88 A; A/B=1-108.
DR PDB; 3LGN; X-ray; 1.50 A; A/B=1-108.
DR PDB; 3QGP; X-ray; 1.80 A; A/B=1-108.
DR PDB; 4FNH; X-ray; 1.90 A; A/B=1-108.
DR PDB; 4FNI; X-ray; 1.80 A; A/B=1-108.
DR PDBsum; 2ZDP; -.
DR PDBsum; 3LGM; -.
DR PDBsum; 3LGN; -.
DR PDBsum; 3QGP; -.
DR PDBsum; 4FNH; -.
DR PDBsum; 4FNI; -.
DR AlphaFoldDB; Q7A827; -.
DR SMR; Q7A827; -.
DR EnsemblBacteria; BAB41380; BAB41380; BAB41380.
DR KEGG; sau:SA0160; -.
DR HOGENOM; CLU_141544_2_1_9; -.
DR OMA; FRESHSH; -.
DR BioCyc; MetaCyc:MON-20095; -.
DR BRENDA; 1.14.99.48; 3352.
DR EvolutionaryTrace; Q7A827; -.
DR Proteomes; UP000000751; 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_0000270092"
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 BINDING 21..28
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 SITE 66
FT /note="Transition state stabilizer"
FT MUTAGEN 66
FT /note="W->A: Inactive."
FT /evidence="ECO:0000269|PubMed:22891243"
FT MUTAGEN 66
FT /note="W->F: Heme degradation activity is approximately
FT half that of the wild-type enzyme."
FT /evidence="ECO:0000269|PubMed:22891243"
FT MUTAGEN 66
FT /note="W->L: Inactive."
FT /evidence="ECO:0000269|PubMed:22891243"
FT MUTAGEN 66
FT /note="W->Y: Heme degradation activity is approximately
FT half that of the wild-type enzyme. Heme binds to this
FT enzyme with less heme ruffling than observed for wild-
FT type."
FT /evidence="ECO:0000269|PubMed:22891243"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:2ZDP"
FT HELIX 15..20
FT /evidence="ECO:0007829|PDB:2ZDP"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:4FNH"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:2ZDP"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:2ZDP"
FT STRAND 47..58
FT /evidence="ECO:0007829|PDB:2ZDP"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:2ZDP"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:2ZDP"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:2ZDP"
FT STRAND 92..107
FT /evidence="ECO:0007829|PDB:2ZDP"
SQ SEQUENCE 108 AA; 12791 MW; 8AF2718571451004 CRC64;
MFMAENRLQL QKGSAEETIE RFYNRQGIET IEGFQQMFVT KTLNTEDTDE VKILTIWESE
DSFNNWLNSD VFKEAHKNVR LKSDDDGQQS PILSNKVFKY DIGYHYQK
