Q8NX62 (ISDG_STAAW) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heme-degrading monooxygenase isdG
EC=1.14.99.3

Alternative name(s):
Heme oxygenase
Iron-regulated surface determinant isdG
Iron-responsive surface determinant isdG

Gene names

Name:	isdG
Ordered Locus Names:	MW1018

Organism

Staphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]

Taxonomic identifier

196620 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	107 AA.
Sequence status	Complete.
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 HAMAP MF_01272.
Miscellaneous	IsdG 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	iron assimilation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	heme oxygenase (decyclizing) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 107

107

Heme-degrading monooxygenase isdG HAMAP MF_01272

PRO_0000270089

Sites

Metal binding

7

1

Iron Potential

Metal binding

77

1

Iron (heme axial ligand) Potential

Site

67

1

Transition state stabilizer Potential

Experimental info

Mutagenesis

7

1

N → A: Loss of activity. Ref.2

Mutagenesis

17

1

K → A: No effect. Ref.2

Mutagenesis

23

1

F → A: No effect. Ref.2

Mutagenesis

38

1

M → A: Slight loss of activity. Changes in heme binding. Ref.2

Mutagenesis

67

1

W → A: Loss of activity. Ref.2

Mutagenesis

70

1

S → A: No effect. Ref.2

Mutagenesis

77

1

H → A: Loss of activity. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

107

Helix Strand Turn

Details...

Beta strand

3 – 12

10

Helix

16 – 21

6

Helix

29 – 31

3

Beta strand

35 – 45

11

Beta strand

47 – 60

14

Helix

61 – 68

8

Helix

71 – 79

9

Beta strand

91 – 106

16

Sequences

	Sequence		Length	Mass (Da)
	Q8NX62 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: DB13A134D5EC4FF0	FASTA	107	12,546
	10 20 30 40 50 60 MKFMAENRLT LTKGTAKDII ERFYTRHGIE TLEGFDGMFV TQTLEQEDFD EVKILTVWKS 70 80 90 100 KQAFTDWLKS DVFKAAHKHV RSKNEDESSP IINNKVITYD IGYSYMK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome and virulence determinants of high virulence community-acquired MRSA." Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K. Lancet 359:1819-1827(2002) [PubMed: 12044378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MW2.
[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 (1.9 ANGSTROMS), FUNCTION, SUBUNIT, MUTAGENESIS OF ASN-7; LYS-17; PHE-23; MET-38; TRP-67; SER-70 AND HIS-77.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000033 Genomic DNA. Translation: BAB94883.1.

RefSeq

NP_645835.1. NC_003923.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XBW	X-ray	1.90	A/B/C/D	1-107	[»]

ProteinModelPortal

Q8NX62.

ModBase

Search...

Protein-protein interaction databases

STRING

Q8NX62.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBSTAT00000026617; EBSTAP00000025656; EBSTAG00000026616.

GeneID

1003130.

GenomeReviews

Gene locus MW1018 in contig BA000033_GR.

KEGG

sam:MW1018.

PATRIC

19568616. VBIStaAur44266_1067.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG2329.

GeneTree

EBGT00050000024362.

HOGENOM

HBG616589.

OMA

GEGERIM.

ProtClustDB

PRK13312.

Enzyme and pathway databases

BioCyc

SAUR196620:MW1018-MONOMER.

Family and domain databases

HAMAP

MF_01272. IsdG.
[Tree]

InterPro

IPR007138. Antibiotic_mOase.
IPR011008. Dimeric_a/b-barrel.
IPR023953. Heme-degrad_mOase.
[Graphical view]

KO

K00510.

Pfam

PF03992. ABM. 1 hit.
[Graphical view]

SUPFAM

SSF54909. Dimer_A_B_barrel. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ISDG_STAAW

Accession

Primary (citable) accession number: Q8NX62

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program