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Protein

Heme oxygenase

Gene

hmuO

Organism
Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Allows the bacteria to use the host heme as an iron source. Involved in the oxidation of heme and subsequent release of iron from the heme moiety.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi20 – 201Iron (heme axial ligand)By similarity

GO - Molecular functioni

  1. heme oxygenase (decyclizing) activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. heme oxidation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.99.3. 1645.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase (EC:1.14.99.3)
Gene namesi
Name:hmuO
Ordered Locus Names:DIP1669
OrganismiCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Taxonomic identifieri257309 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000002198 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Heme oxygenasePRO_0000209703Add
BLAST

Interactioni

Protein-protein interaction databases

DIPiDIP-61184N.
STRINGi257309.DIP1669.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2417Combined sources
Helixi27 – 337Combined sources
Helixi39 – 6628Combined sources
Turni70 – 723Combined sources
Helixi75 – 773Combined sources
Helixi80 – 9112Combined sources
Beta strandi92 – 943Combined sources
Helixi96 – 994Combined sources
Helixi104 – 11916Combined sources
Helixi122 – 15130Combined sources
Helixi155 – 1573Combined sources
Helixi159 – 1624Combined sources
Helixi169 – 18214Combined sources
Helixi187 – 21226Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IW0X-ray1.40A/B/C1-215[»]
1IW1X-ray1.50A/B/C1-215[»]
1V8XX-ray1.85A/B/C1-215[»]
1WNVX-ray1.85A/B/C1-215[»]
1WNWX-ray1.70A/B/C1-215[»]
1WNXX-ray1.85A/B1-215[»]
1WZDX-ray1.35A/B1-215[»]
1WZFX-ray1.85A/B1-215[»]
1WZGX-ray1.75A/B1-215[»]
ProteinModelPortaliP71119.
SMRiP71119. Positions 2-213.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP71119.

Family & Domainsi

Sequence similaritiesi

Belongs to the heme oxygenase family.Curated

Phylogenomic databases

eggNOGiCOG5398.
HOGENOMiHOG000233221.
KOiK00510.
OMAiYAPLYFP.
OrthoDBiEOG69PQ2G.

Family and domain databases

Gene3Di1.20.910.10. 1 hit.
InterProiIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
PANTHERiPTHR10720. PTHR10720. 1 hit.
PfamiPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFiPIRSF000343. Haem_Oase. 1 hit.
PRINTSiPR00088. HAEMOXYGNASE.
SUPFAMiSSF48613. SSF48613. 1 hit.
PROSITEiPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P71119-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTATAGLAV ELKQSTAQAH EKAEHSTFMS DLLEGRLGVA EFTRLQEQAW
60 70 80 90 100
LFYTALEQAA DAVRASGFAE SLLDPALNRA EVLARDLDKL NDGSEWRSRI
110 120 130 140 150
TASPAVIDYV NRLEEIRDNV DGPALVAHHY VRYLGDLSGG QVIARMMQRH
160 170 180 190 200
YGVDPEALGF YHFEGIAKLK VYKDEYREKL NNLELSDEQR ENLLKEATDA
210
FVFNHQVFAD LGKGL
Length:215
Mass (Da):24,116
Last modified:November 28, 2003 - v2
Checksum:i60D9E8E2ED7ED456
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341E → K in AAC44832 (PubMed:9006041).Curated
Sequence conflicti60 – 601A → V in AAC44832 (PubMed:9006041).Curated
Sequence conflicti92 – 932DG → GS in AAC44832 (PubMed:9006041).Curated
Sequence conflicti192 – 1921N → H in AAC44832 (PubMed:9006041).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73860 Genomic DNA. Translation: AAC44832.1.
BX248358 Genomic DNA. Translation: CAE50198.1.
RefSeqiNP_940009.1. NC_002935.2.
WP_010935240.1. NC_002935.2.

Genome annotation databases

GeneIDi2648714.
KEGGicdi:DIP1669.
PATRICi21484548. VBICorDip47633_1650.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73860 Genomic DNA. Translation: AAC44832.1.
BX248358 Genomic DNA. Translation: CAE50198.1.
RefSeqiNP_940009.1. NC_002935.2.
WP_010935240.1. NC_002935.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IW0X-ray1.40A/B/C1-215[»]
1IW1X-ray1.50A/B/C1-215[»]
1V8XX-ray1.85A/B/C1-215[»]
1WNVX-ray1.85A/B/C1-215[»]
1WNWX-ray1.70A/B/C1-215[»]
1WNXX-ray1.85A/B1-215[»]
1WZDX-ray1.35A/B1-215[»]
1WZFX-ray1.85A/B1-215[»]
1WZGX-ray1.75A/B1-215[»]
ProteinModelPortaliP71119.
SMRiP71119. Positions 2-213.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61184N.
STRINGi257309.DIP1669.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2648714.
KEGGicdi:DIP1669.
PATRICi21484548. VBICorDip47633_1650.

Phylogenomic databases

eggNOGiCOG5398.
HOGENOMiHOG000233221.
KOiK00510.
OMAiYAPLYFP.
OrthoDBiEOG69PQ2G.

Enzyme and pathway databases

BRENDAi1.14.99.3. 1645.

Miscellaneous databases

EvolutionaryTraceiP71119.

Family and domain databases

Gene3Di1.20.910.10. 1 hit.
InterProiIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
PANTHERiPTHR10720. PTHR10720. 1 hit.
PfamiPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFiPIRSF000343. Haem_Oase. 1 hit.
PRINTSiPR00088. HAEMOXYGNASE.
SUPFAMiSSF48613. SSF48613. 1 hit.
PROSITEiPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin."
    Schmitt M.P.
    J. Bacteriol. 179:838-845(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C7.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700971 / NCTC 13129 / Biotype gravis.

Entry informationi

Entry nameiHMUO_CORDI
AccessioniPrimary (citable) accession number: P71119
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 28, 2003
Last modified: April 29, 2015
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.