Reviewed, UniProtKB/Swiss-Prot P71119 (HMUO_CORDI)

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 [Complete proteome] [HAMAP]

Taxonomic identifier

1717 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	heme oxygenase (decyclizing) activity Inferred from electronic annotation. Source: EC iron 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 – 24

17

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 – 162

4

Helix

169 – 182

14

Helix

187 – 212

26

Sequences

	Sequence		Length	Mass (Da)
	P71119-1 [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: 9006041] [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: 14602910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700971 / NCTC 13129 / Biotype gravis.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

RefSeq

NP_940009.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Genome annotation databases

GeneID

2648714.

GenomeReviews

Gene locus DIP1669 in contig BX248353_GR.

KEGG

cdi:DIP1669.

NMPDR

fig|257309.1.peg.1600.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P71119.

OMA

P71119. GDISKCP.

Enzyme and pathway databases

BioCyc

CDIP257309:DIP1669-MON.

BRENDA

1.14.99.3. 20483.

Family and domain databases

InterPro

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

Gene3D

G3DSA:1.20.910.10. Haem_Oase-like_multi-hlx. 1 hit.

PANTHER

PTHR10720. Haem_Oase. 1 hit.

Pfam

PF01126. Heme_oxygenase. 1 hit.
[Graphical view]

PIRSF

PIRSF000343. Haem_Oase. 1 hit.

PRINTS

PR00088. HAEMOXYGNASE.

PROSITE

PS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	June 16, 2009
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)