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Protein

Heme-degrading monooxygenase

Gene

isdG

Organism
Bacillus weihenstephanensis (strain KBAB4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring to the biliverdin in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron.UniRule annotation

Catalytic activityi

Protoheme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi6 – 61IronUniRule annotation
Sitei66 – 661Transition state stabilizerUniRule annotation
Metal bindingi76 – 761Iron (heme axial ligand)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciBWEI315730:GHRU-4488-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme-degrading monooxygenaseUniRule annotation (EC:1.14.99.3UniRule annotation)
Alternative name(s):
Heme oxygenaseUniRule annotation
Iron-regulated surface determinantUniRule annotation
Iron-responsive surface determinantUniRule annotation
Gene namesi
Name:isdGUniRule annotation
Ordered Locus Names:BcerKBAB4_4370
OrganismiBacillus weihenstephanensis (strain KBAB4)
Taxonomic identifieri315730 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002154 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 107107Heme-degrading monooxygenasePRO_1000140205Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi315730.BcerKBAB4_4370.

Structurei

3D structure databases

ProteinModelPortaliA9VJK2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 9493ABMUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.UniRule annotation
Contains 1 ABM domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG2329.
HOGENOMiHOG000008026.
KOiK07145.
OMAiISTRWKE.
OrthoDBiEOG6GTZMS.

Family and domain databases

HAMAPiMF_01272. Heme_degrading_monooxygenase.
InterProiIPR007138. ABM_dom.
IPR011008. Dimeric_a/b-barrel.
IPR023953. IsdG.
[Graphical view]
PfamiPF03992. ABM. 1 hit.
[Graphical view]
SUPFAMiSSF54909. SSF54909. 1 hit.
PROSITEiPS51725. ABM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A9VJK2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIIVTNTTKI TKGNGHKLIE RFNKVGKVET MSGFLGLEVL LTQNTVDYDE
60 70 80 90 100
VTISTRWNAK EDFQGWTKSS AFKDAHSHQG GMPDYILDNK IAYYDVKVVR

MPMAAAQ
Length:107
Mass (Da):12,056
Last modified:February 5, 2008 - v1
Checksum:iFE1EB4ACEBA205D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000903 Genomic DNA. Translation: ABY45529.1.
RefSeqiWP_002015426.1. NC_010184.1.
YP_001647157.1. NC_010184.1.

Genome annotation databases

EnsemblBacteriaiABY45529; ABY45529; BcerKBAB4_4370.
GeneIDi22938687.
KEGGibwe:BcerKBAB4_4370.
PATRICi19013412. VBIBacWei55973_5019.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000903 Genomic DNA. Translation: ABY45529.1.
RefSeqiWP_002015426.1. NC_010184.1.
YP_001647157.1. NC_010184.1.

3D structure databases

ProteinModelPortaliA9VJK2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi315730.BcerKBAB4_4370.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABY45529; ABY45529; BcerKBAB4_4370.
GeneIDi22938687.
KEGGibwe:BcerKBAB4_4370.
PATRICi19013412. VBIBacWei55973_5019.

Phylogenomic databases

eggNOGiCOG2329.
HOGENOMiHOG000008026.
KOiK07145.
OMAiISTRWKE.
OrthoDBiEOG6GTZMS.

Enzyme and pathway databases

BioCyciBWEI315730:GHRU-4488-MONOMER.

Family and domain databases

HAMAPiMF_01272. Heme_degrading_monooxygenase.
InterProiIPR007138. ABM_dom.
IPR011008. Dimeric_a/b-barrel.
IPR023953. IsdG.
[Graphical view]
PfamiPF03992. ABM. 1 hit.
[Graphical view]
SUPFAMiSSF54909. SSF54909. 1 hit.
PROSITEiPS51725. ABM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KBAB4.

Entry informationi

Entry nameiHDOX_BACWK
AccessioniPrimary (citable) accession number: A9VJK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: June 24, 2015
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.