A9ITM7 (HEM6_BORPD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coproporphyrinogen-III oxidase, aerobic
Short name=Coprogen oxidase
Short name=Coproporphyrinogenase
EC=1.3.3.3

Gene names

Name:	hemF
Ordered Locus Names:	Bpet3101

Organism

Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]

Taxonomic identifier

340100 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III By similarity. HAMAP MF_00333
Catalytic activity	Coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O. HAMAP MF_00333
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1. HAMAP MF_00333
Subunit structure	Homodimer By similarity. HAMAP MF_00333
Subcellular location	Cytoplasm By similarity HAMAP MF_00333.
Sequence similarities	Belongs to the aerobic coproporphyrinogen-III oxidase family.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Cellular component	Cytoplasm
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	coproporphyrinogen oxidase activity Inferred from electronic annotation. Source: EC protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 303	303	Coproporphyrinogen-III oxidase, aerobic HAMAP MF_00333		PRO_1000119785
Regions
	Region	49 – 58	10	Important for dimerization By similarity
	Region	109 – 111	3	Substrate binding By similarity
	Region	244 – 279	36	Important for dimerization By similarity
	Region	262 – 267	6	Substrate binding By similarity
Sites
	Active site	107	1	Proton donor By similarity
	Binding site	93	1	Substrate By similarity
	Site	179	1	Important for dimerization By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9ITM7 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: CAC05BD308AAD95F	FASTA	303	34,082
	10 20 30 40 50 60 MSAVPVSDVH AYLTGLQDNI VQALEQAGGE SFRTDTWQRP EGGGGVSRLI EGGQLLERAG 70 80 90 100 110 120 VLFSHVHGTR LPPSASAHRP ELAGRSWQAM GVSLVLHPRN PYVPTTHMNV RMFVAAARPG 130 140 150 160 170 180 HDENDVFWFG GGLDLTPYYA FEDDARHFHQ VCRAALDPHG AAYYPQYKRW CDEYFYLKHR 190 200 210 220 230 240 QEMRGVGGVF FDDLNEPGFD ASFALLRSVG DAFLPAYLPI VQRRRDTPYT QAQRDFQAYR 250 260 270 280 290 300 RGRYVEFNLV FDRGTLFGLQ SGGRTESILL SMPPMAQWRY DWQPAAGSPE AALAGFLQPR DWA

References

[1]

"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae." Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R. BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-461 / DSM 12804 / CCUG 43448.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM902716 Genomic DNA. Translation: CAP43443.1.
RefSeq	YP_001631711.1. NC_010170.1.
3D structure databases
ProteinModelPortal	A9ITM7.
ModBase	Search...
Protein-protein interaction databases
STRING	A9ITM7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5816943.
GenomeReviews	Gene locus Bpet3101 in contig AM902716_GR.
KEGG	bpt:Bpet3101.
PATRIC	21167745. VBIBorPet31633_3126.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG631180.
OMA	VKAYLLD.
ProtClustDB	PRK05330.
Enzyme and pathway databases
BioCyc	BPET94624:BPET3101-MONOMER.
Family and domain databases
HAMAP	MF_00333. Coprogen_oxidas. [Tree]
InterPro	IPR001260. Coprogen_oxidase_aer. IPR018375. Coprogen_oxidase_CS. [Graphical view]
Gene3D	G3DSA:3.40.1500.10. Coprogen_oxidas. 1 hit.
KO	K00228.
PANTHER	PTHR10755. Coprogen_oxidas. 1 hit.
Pfam	PF01218. Coprogen_oxidas. 1 hit. [Graphical view]
PIRSF	PIRSF000166. Coproporphyri_ox. 1 hit.
PRINTS	PR00073. COPRGNOXDASE.
SUPFAM	SSF102886. Coprogen_oxidas. 1 hit.
PROSITE	PS01021. COPROGEN_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM6_BORPD

Accession

Primary (citable) accession number: A9ITM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program