Reviewed, UniProtKB/Swiss-Prot Q99X56 (ISDI_STAAM)

Names and origin

Protein names

Recommended name:
    Heme-degrading monooxygenase isdI
    EC=1.14.99.3
Alternative name(s):
    Iron-regulated surface determinant isdI
    Iron-responsive surface determinant isdI
    Heme oxygenase

Gene names

Name:	isdI
Ordered Locus Names:	SAV0165

Organism

Staphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]

Taxonomic identifier

158878 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	108 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron. Ref.2
Catalytic activity	Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O. HAMAP MF_01272
Subunit structure	Homodimer. Ref.2
Subcellular location	Cytoplasm By similarity.
Miscellaneous	IsdI seems to carry out oxygenation of the heme without the assistance of any of the prosthetic groups or cofactors normally associated with activation of molecular oxygen. HAMAP MF_01272
Sequence similarities	Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase isdG subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	antibiotic biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	heme binding Inferred from electronic annotation. Source: HAMAP heme oxygenase (decyclizing) activity Inferred from electronic annotation. Source: EC monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 108

108

Heme-degrading monooxygenase isdI HAMAP MF_01272

PRO_0000270088

Sites

Metal binding

6

1

Iron Potential

Metal binding

76

1

Iron (heme axial ligand) Potential

Site

66

1

Transition state stabilizer Potential

Secondary structure

1

.

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.

.

.

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.

.

.

108

Helix Strand Turn

Details...

Beta strand

2 – 10

9

Helix

15 – 18

4

Helix

19 – 23

5

Helix

28 – 30

3

Beta strand

34 – 42

9

Beta strand

46 – 58

13

Helix

60 – 67

8

Helix

70 – 74

5

Beta strand

91 – 107

17

Sequences

	Sequence		Length	Mass (Da)
	Q99X56-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 8AF2718571451004	FASTA	108	12,791
	10 20 30 40 50 60 MFMAENRLQL QKGSAEETIE RFYNRQGIET IEGFQQMFVT KTLNTEDTDE VKILTIWESE 70 80 90 100 DSFNNWLNSD VFKEAHKNVR LKSDDDGQQS PILSNKVFKY DIGYHYQK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." 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. Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases." Wu R., Skaar E.P., Zhang R., Joachimiak G., Gornicki P., Schneewind O., Joachimiak A. J. Biol. Chem. 280:2840-2846(2005) [PubMed: 15520015] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), FUNCTION, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

BA000017 Genomic DNA. Translation: BAB56327.1.

RefSeq

NP_370689.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SQE	X-ray	1.50	A/B	1-108	[»]

ModBase

Search...

Genome annotation databases

GeneID

1120124.

GenomeReviews

Gene locus SAV0165 in contig BA000017_GR.

KEGG

sav:SAV0165.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q99X56.

OMA

Q99X56. DAHSHQG.

Enzyme and pathway databases

BioCyc

SAUR158878:SAV0165-MON.

Family and domain databases

HAMAP

MF_01272.
[Tree]

InterPro

IPR007138. Antibiotic_mOase.
[Graphical view]

Pfam

PF03992. ABM. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ISDI_STAAM

Accession

Primary (citable) accession number: Q99X56

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)