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Heme oxygenase (staphylobilin-producing) 2 (EC 1.14.99.48) (Heme-degrading monooxygenase 2) (Iron-regulated surface determinant 2) (Iron-responsive surface determinant 2)

 HDOX2_STAAN             Reviewed;         108 AA.
Q7A827;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
07-JUN-2017, entry version 91.
RecName: Full=Heme oxygenase (staphylobilin-producing) 2 {ECO:0000255|HAMAP-Rule:MF_01272};
EC=1.14.99.48 {ECO:0000255|HAMAP-Rule:MF_01272, ECO:0000269|PubMed:20180905};
AltName: Full=Heme-degrading monooxygenase 2 {ECO:0000255|HAMAP-Rule:MF_01272};
AltName: Full=Iron-regulated surface determinant 2 {ECO:0000255|HAMAP-Rule:MF_01272};
AltName: Full=Iron-responsive surface determinant 2 {ECO:0000255|HAMAP-Rule:MF_01272};
Name=isdI; OrderedLocusNames=SA0160;
Staphylococcus aureus (strain N315).
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=158879;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=N315;
PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
Ogasawara N., Hayashi H., Hiramatsu K.;
"Whole genome sequencing of meticillin-resistant Staphylococcus
aureus.";
Lancet 357:1225-1240(2001).
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=N315;
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
"Shotgun proteomic analysis of total and membrane protein extracts of
S. aureus strain N315.";
Submitted (OCT-2007) to UniProtKB.
[3]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-108 IN COMPLEX WITH HEME,
FUNCTION, AND SUBUNIT.
PubMed=18713745; DOI=10.1074/jbc.M709486200;
Lee W.C., Reniere M.L., Skaar E.P., Murphy M.E.;
"Ruffling of metalloporphyrins bound to IsdG and IsdI, two heme-
degrading enzymes in Staphylococcus aureus.";
J. Biol. Chem. 283:30957-30963(2008).
[4]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-108 IN COMPLEX WITH HEME,
FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
PubMed=20180905; DOI=10.1111/j.1365-2958.2010.07076.x;
Reniere M.L., Ukpabi G.N., Harry S.R., Stec D.F., Krull R.,
Wright D.W., Bachmann B.O., Murphy M.E., Skaar E.P.;
"The IsdG-family of haem oxygenases degrades haem to a novel
chromophore.";
Mol. Microbiol. 75:1529-1538(2010).
[5]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-108 IN COMPLEX WITH HEME,
AND SUBUNIT.
Takayama S.J., Ukpabi G.N., Murphy M.E.P., Mauk A.G.;
"Heme ruffling enables the catalytic activity of the heme degrading
enzyme IsdI.";
Submitted (JAN-2011) to the PDB data bank.
[6]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-108 OF MUTANT THR-66 IN
COMPLEX WITH HEME, MUTAGENESIS OF TRP-66, AND SUBUNIT.
PubMed=22891243; DOI=10.1074/jbc.M112.393249;
Ukpabi G., Takayama S.J., Mauk A.G., Murphy M.E.;
"Inactivation of the heme degrading enzyme IsdI by an active site
substitution that diminishes heme ruffling.";
J. Biol. Chem. 287:34179-34188(2012).
-!- FUNCTION: Allows bacterial pathogens to use the host heme as an
iron source. Catalyzes the oxidative degradation of the heme
macrocyclic porphyrin ring to the oxo-bilirubin chromophore
staphylobilin (a mixture of the linear tetrapyrroles 5-oxo-delta-
bilirubin and 15-oxo-beta-bilirubin) in the presence of a suitable
electron donor such as ascorbate or NADPH--cytochrome P450
reductase, with subsequent release of free iron.
{ECO:0000255|HAMAP-Rule:MF_01272, ECO:0000269|PubMed:18713745,
ECO:0000269|PubMed:20180905}.
-!- CATALYTIC ACTIVITY: Protoheme + 5 reduced acceptor + 4 O(2) = 5-
oxo-delta-bilirubin + Fe(2+) + formaldehyde + 5 acceptor + 4
H(2)O. {ECO:0000255|HAMAP-Rule:MF_01272,
ECO:0000269|PubMed:20180905}.
-!- CATALYTIC ACTIVITY: Protoheme + 5 reduced acceptor + 4 O(2) = 15-
oxo-beta-bilirubin + Fe(2+) + formaldehyde + 5 acceptor + 4 H(2)O.
{ECO:0000255|HAMAP-Rule:MF_01272, ECO:0000269|PubMed:20180905}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01272,
ECO:0000269|PubMed:18713745, ECO:0000269|PubMed:20180905,
ECO:0000269|PubMed:22891243, ECO:0000269|Ref.5}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01272}.
-!- SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase
family. Heme-degrading monooxygenase IsdG subfamily.
{ECO:0000255|HAMAP-Rule:MF_01272}.
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EMBL; BA000018; BAB41380.1; -; Genomic_DNA.
PIR; A89778; A89778.
RefSeq; WP_000480603.1; NC_002745.2.
PDB; 2ZDP; X-ray; 1.50 A; A/B=1-108.
PDB; 3LGM; X-ray; 1.88 A; A/B=1-108.
PDB; 3LGN; X-ray; 1.50 A; A/B=1-108.
PDB; 3QGP; X-ray; 1.80 A; A/B=1-108.
PDB; 4FNH; X-ray; 1.90 A; A/B=1-108.
PDB; 4FNI; X-ray; 1.80 A; A/B=1-108.
PDBsum; 2ZDP; -.
PDBsum; 3LGM; -.
PDBsum; 3LGN; -.
PDBsum; 3QGP; -.
PDBsum; 4FNH; -.
PDBsum; 4FNI; -.
ProteinModelPortal; Q7A827; -.
SMR; Q7A827; -.
EnsemblBacteria; BAB41380; BAB41380; BAB41380.
GeneID; 31212972; -.
KEGG; sau:SA0160; -.
HOGENOM; HOG000008026; -.
KO; K07145; -.
OMA; FRESHSH; -.
BRENDA; 1.14.99.48; 3352.
EvolutionaryTrace; Q7A827; -.
Proteomes; UP000000751; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0033212; P:iron assimilation; IEA:InterPro.
HAMAP; MF_01272; Heme_degrading_monooxygenase; 1.
InterPro; IPR007138; ABM_dom.
InterPro; IPR011008; Dimeric_a/b-barrel.
InterPro; IPR023953; IsdG.
Pfam; PF03992; ABM; 1.
SUPFAM; SSF54909; SSF54909; 1.
PROSITE; PS51725; ABM; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Heme; Iron; Metal-binding;
Monooxygenase; Oxidoreductase.
CHAIN 1 108 Heme oxygenase (staphylobilin-producing)
2.
/FTId=PRO_0000270092.
DOMAIN 2 93 ABM. {ECO:0000255|HAMAP-Rule:MF_01272}.
REGION 21 28 Heme binding.
METAL 6 6 Iron.
METAL 76 76 Iron (heme axial ligand).
SITE 66 66 Transition state stabilizer.
MUTAGEN 66 66 W->A: Inactive.
{ECO:0000269|PubMed:22891243}.
MUTAGEN 66 66 W->F: Heme degradation activity is
approximately half that of the wild-type
enzyme. {ECO:0000269|PubMed:22891243}.
MUTAGEN 66 66 W->L: Inactive.
{ECO:0000269|PubMed:22891243}.
MUTAGEN 66 66 W->Y: Heme degradation activity is
approximately half that of the wild-type
enzyme. Heme binds to this enzyme with
less heme ruffling than observed for
wild-type. {ECO:0000269|PubMed:22891243}.
STRAND 2 10 {ECO:0000244|PDB:2ZDP}.
HELIX 15 20 {ECO:0000244|PDB:2ZDP}.
HELIX 21 23 {ECO:0000244|PDB:4FNH}.
HELIX 28 30 {ECO:0000244|PDB:2ZDP}.
STRAND 34 42 {ECO:0000244|PDB:2ZDP}.
STRAND 47 58 {ECO:0000244|PDB:2ZDP}.
HELIX 60 67 {ECO:0000244|PDB:2ZDP}.
HELIX 70 75 {ECO:0000244|PDB:2ZDP}.
TURN 76 78 {ECO:0000244|PDB:2ZDP}.
STRAND 92 107 {ECO:0000244|PDB:2ZDP}.
SEQUENCE 108 AA; 12791 MW; 8AF2718571451004 CRC64;
MFMAENRLQL QKGSAEETIE RFYNRQGIET IEGFQQMFVT KTLNTEDTDE VKILTIWESE
DSFNNWLNSD VFKEAHKNVR LKSDDDGQQS PILSNKVFKY DIGYHYQK


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