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 (By similarity).
CATALYTIC ACTIVITY: Heme + 3 AH₂ + 3 O₂ = biliverdin + Fe²⁺ + CO + 3 A + 3 H₂O.
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase isdG subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000730; ABX29088.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001574967.1; -.

3D structure databases

ModBase

A8Z1R5.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from HAMAP).
GO:0004392;	Molecular function: heme oxygenase (decyclizing) activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from HAMAP).
GO:0004497;	Molecular function: monooxygenase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0017000;	Biological process: antibiotic biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01272; -; 1.
PBIL [Tree]

InterPro

IPR007138; Antibiotic_mOase.
Graphical view of domain structure.

Pfam

PF03992; ABM; 1.
Pfam graphical view of domain structure.

ProtoNet

A8Z1R5.

Genome annotation databases

GeneID

5776534; -.

GenomeReviews

CP000730_GR; USA300HOU_1069.

KEGG

sax:USA300HOU_1069; -.

CMR

A8Z1R5; USA300HOU_1069.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 107`	`107`	`Heme-degrading monooxygenase isdG.`	`PRO_1000085844`
`METAL`	`7 7`		`Iron (Potential).`
`METAL`	`77 77`		`Iron (heme axial ligand) (Potential).`
`SITE`	`67 67`	`1`	`Transition state stabilizer (Potential).`

Sequence information

Length: 107 AA [This is the length of the unprocessed precursor]

Molecular weight: 12546 Da [This is the MW of the unprocessed precursor]

CRC64: DB13A134D5EC4FF0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKFMAENRLT LTKGTAKDII ERFYTRHGIE TLEGFDGMFV TQTLEQEDFD EVKILTVWKS 

        70         80         90        100 
KQAFTDWLKS DVFKAAHKHV RSKNEDESSP IINNKVITYD IGYSYMK

A8Z1R5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools