P71119 (HMUO_CORDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heme oxygenase
EC=1.14.99.3

Gene names

Name:	hmuO
Ordered Locus Names:	DIP1669

Organism

Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) [Complete proteome] [HAMAP]

Taxonomic identifier

257309 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › Corynebacterium diphtheriae

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.
Sequence similarities	Belongs to the heme oxygenase family.

Ontologies

Keywords
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	heme oxidation Inferred from electronic annotation. Source: InterPro
Molecular_function	heme oxygenase (decyclizing) activity Inferred from electronic annotation. Source: EC metal ion binding 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 – 215

215

Heme oxygenase

PRO_0000209703

Sites

Metal binding

20

1

Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict

34

1

E → K in AAC44832. Ref.1

Sequence conflict

60

1

A → V in AAC44832. Ref.1

Sequence conflict

92 – 93

2

DG → GS in AAC44832. Ref.1

Sequence conflict

192

1

N → H in AAC44832. Ref.1

Secondary structure

1

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215

Helix Strand Turn

Details...

Helix

8 – 15

8

Helix

17 – 24

8

Helix

27 – 33

7

Helix

39 – 66

28

Turn

70 – 72

3

Helix

75 – 77

3

Helix

80 – 91

12

Beta strand

92 – 94

3

Helix

96 – 99

4

Helix

104 – 119

16

Helix

122 – 151

30

Helix

155 – 157

3

Helix

159 – 161

3

Helix

169 – 181

13

Helix

187 – 212

26

Sequences

	Sequence		Length	Mass (Da)
	P71119 [UniParc]. Last modified November 28, 2003. Version 2. Checksum: 60D9E8E2ED7ED456	FASTA	215	24,116
	10 20 30 40 50 60 MTTATAGLAV ELKQSTAQAH EKAEHSTFMS DLLEGRLGVA EFTRLQEQAW LFYTALEQAA 70 80 90 100 110 120 DAVRASGFAE SLLDPALNRA EVLARDLDKL NDGSEWRSRI TASPAVIDYV NRLEEIRDNV 130 140 150 160 170 180 DGPALVAHHY VRYLGDLSGG QVIARMMQRH YGVDPEALGF YHFEGIAKLK VYKDEYREKL 190 200 210 NNLELSDEQR ENLLKEATDA FVFNHQVFAD LGKGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129." Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K., Moule S. , Quail M.A., Rabbinowitsch E., Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G., Parkhill J. Nucleic Acids Res. 31:6516-6523(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700971 / NCTC 13129 / Biotype gravis.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U73860 Genomic DNA. Translation: AAC44832.1.
BX248358 Genomic DNA. Translation: CAE50198.1.

RefSeq

NP_940009.1. NC_002935.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IW0	X-ray	1.40	A/B/C	1-215	[»]
1IW1	X-ray	1.50	A/B/C	1-215	[»]
1V8X	X-ray	1.85	A/B/C	1-215	[»]
1WNV	X-ray	1.85	A/B/C	1-215	[»]
1WNW	X-ray	1.70	A/B/C	1-215	[»]
1WNX	X-ray	1.85	A/B	1-215	[»]
1WZD	X-ray	1.35	A/B	1-215	[»]
1WZF	X-ray	1.85	A/B	1-215	[»]
1WZG	X-ray	1.75	A/B	1-215	[»]

ProteinModelPortal

P71119.

SMR

P71119. Positions 2-213.

ModBase

Search...

Protein-protein interaction databases

STRING

257309.DIP1669.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAE50198; CAE50198; DIP1669.

GeneID

2648714.

KEGG

cdi:DIP1669.

PATRIC

21484548. VBICorDip47633_1650.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG5398.

HOGENOM

HOG000233221.

KO

K00510.

OMA

GNFYFVY.

ProtClustDB

CLSK900077.

Family and domain databases

Gene3D

1.20.910.10. 1 hit.

InterPro

IPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]

PANTHER

PTHR10720. PTHR10720. 1 hit.

Pfam

PF01126. Heme_oxygenase. 1 hit.
[Graphical view]

PIRSF

PIRSF000343. Haem_Oase. 1 hit.

PRINTS

PR00088. HAEMOXYGNASE.

SUPFAM

SSF48613. Heme_oxygenase. 1 hit.

PROSITE

PS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P71119.

Entry information

Entry name

HMUO_CORDI

Accession

Primary (citable) accession number: P71119

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 28, 2003
Last modified:	May 1, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program