Reviewed, UniProtKB/Swiss-Prot Q81L50 (ISDG_BACAN)

Names and origin

Protein names

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

Gene names

Name:	isdG
Ordered Locus Names:	BA_4782, GBAA_4782, BAS4437

Organism

Bacillus anthracis [Complete proteome] [HAMAP]

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	107 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. Is also necessary to protect B.anthracis from heme-mediated toxicity that might be encountered upon exposure to oxidative radicals. Ref.4
Catalytic activity	Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O. Ref.4
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Induction	Up-regulated under iron-starved conditions Probable.
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	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 – 107	107	Heme-degrading monooxygenase isdG HAMAP MF_01272		PRO_0000270070
Sites
	Metal binding	6	1	Iron Potential
	Metal binding	76	1	Iron (heme axial ligand) Potential
	Site	66	1	Transition state stabilizer Potential

Sequences

	Sequence		Length	Mass (Da)
	Q81L50-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: ACB308A337A92DFB	FASTA	107	12,004
	10 20 30 40 50 60 MIIVTNTAKI TKGNGHKLID RFNKVGQVET MPGFLGLEVL LTQNTVDYDE VTISTRWNAK 70 80 90 100 EDFQGWTKSP AFKAAHSHQG GMPDYILDNK ISYYDVKVVR MPMAAAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.
[3]	"Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[4]	"Bacillus anthracis IsdG, a heme-degrading monooxygenase." Skaar E.P., Gaspar A.H., Schneewind O. J. Bacteriol. 188:1071-1080(2006) [PubMed: 16428411] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016879 Genomic DNA. Translation: AAP28473.1. AE017225 Genomic DNA. Translation: AAT56735.1. AE017334 Genomic DNA. Translation: AAT33903.1.
RefSeq	NP_846987.1. YP_021428.1. YP_030684.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1083895. 2815699. 2851618.
GenomeReviews	Gene locus BA_4782 in contig AE016879_GR. Gene locus BAS4437 in contig AE017225_GR. Gene locus GBAA4782 in contig AE017334_GR.
KEGG	ban:BA4782. bar:GBAA4782. bat:BAS4437.
TIGR	BA_4782. GBAA_4782.
Phylogenomic databases
HOGENOM	Q81L50.
OMA	Q81L50. DAHSHQG.
Enzyme and pathway databases
BioCyc	BANT260799:BAS4437-MON. BANT261594:GBAA4782-MON.
BRENDA	1.14.99.3. 267517.
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

ISDG_BACAN

Accession

Primary (citable) accession number: Q81L50
Secondary accession number(s): Q6HSK4, Q6KLU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	June 1, 2003
Last modified:	June 16, 2009
This is version 47 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)