A9M6L4 (HEM6_BRUC2) 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:	BCAN_A1586

Organism

Brucella canis (strain ATCC 23365 / NCTC 10854) [Complete proteome] [HAMAP]

Taxonomic identifier

483179 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

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_1000119789
Regions
	Region	72 – 81	10	Important for dimerization By similarity
	Region	132 – 134	3	Substrate binding By similarity
	Region	268 – 303	36	Important for dimerization By similarity
	Region	286 – 291	6	Substrate binding By similarity
Sites
	Active site	130	1	Proton donor By similarity
	Binding site	116	1	Substrate By similarity
	Site	199	1	Important for dimerization By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9M6L4 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 65C4C1B754D13CE0	FASTA	303	35,111
	10 20 30 40 50 60 MKREDIPAII PADIEEKKKA AQSWFEELRD RICASYEQLE DELQGPLSDR EPGRFVRTPW 70 80 90 100 110 120 QKDDGNGGGV MSIMHGRVFE KVGVHVSTVH GEFSPEFRKQ IPGAEEDPRY WASGISLIAH 130 140 150 160 170 180 PQNPNVPAVH MNTRMIVTTR QWFAGGADLT PVLDRRRTQE DPDTLAFHKA FRFICEKHKD 190 200 210 220 230 240 IVDYQRLKEW CDEYFFLPHR DEPRGIGGIF YDWLHSPEEK GGWDSDFAFT RDVGRGFSVV 250 260 270 280 290 300 YPHLVRQNFN KDWTEADRDE QLIRRGRYVE FNLLYDRGTI FGLKTGGNMN AILSSMPPVV KWP

References

[1]

"Brucella canis ATCC 23365 whole genome shotgun sequencing project." Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M., Snyder E.E. , Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., Munk C., Brettin T.S. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 23365 / NCTC 10854.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000872 Genomic DNA. Translation: ABX62610.1.
RefSeq	YP_001593381.1. NC_010103.1.
3D structure databases
ProteinModelPortal	A9M6L4.
ModBase	Search...
Protein-protein interaction databases
STRING	A9M6L4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5785224.
GenomeReviews	Gene locus BCAN_A1586 in contig CP000872_GR.
KEGG	bcs:BCAN_A1586.
PATRIC	17831864. VBIBruCan25663_1582.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG631180.
OMA	VKAYLLD.
ProtClustDB	PRK05330.
Enzyme and pathway databases
BioCyc	BCAN483179:BCAN_A1586-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_BRUC2

Accession

Primary (citable) accession number: A9M6L4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program