C2DV19 (C2DV19_ECOLX) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Coproporphyrinogen-III oxidase, aerobic HAMAP MF_00333
Short name=Coprogen oxidase HAMAP MF_00333
Short name=Coproporphyrinogenase HAMAP MF_00333
EC=1.3.3.3 HAMAP MF_00333

Gene names

Name:	hemF HAMAP MF_00333 EMBL EEJ46297.1
ORF Names:	HMPREF0358_4073 EMBL EEJ46297.1

Organism

Escherichia coli 83972 EMBL EEJ46297.1

Taxonomic identifier

525281 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	299 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 SAAS SAAS018375
Catalytic activity	Coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O. HAMAP MF_00333 SAAS SAAS018375
Cofactor	Manganese By similarity. HAMAP MF_00333
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1. HAMAP MF_00333 SAAS SAAS018375
Subunit structure	Homodimer By similarity. HAMAP MF_00333 SAAS SAAS018375
Subcellular location	Cytoplasm By similarity HAMAP MF_00333.
Sequence similarities	Belongs to the aerobic coproporphyrinogen-III oxidase family. HAMAP MF_00333

Ontologies

Keywords
Biological process	Porphyrin biosynthesis HAMAP MF_00333 SAAS SAAS018375
Cellular component	Cytoplasm HAMAP MF_00333
Ligand	Manganese HAMAP MF_00333
Molecular function	Oxidoreductase HAMAP MF_00333 SAAS SAAS018375 EMBL EEJ46297.1
Gene Ontology (GO)
Biological process	porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	coproporphyrinogen oxidase activity Inferred from electronic annotation. Source: HAMAP protein homodimerization activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Region	48 – 57	10	Important for dimerization By similarity HAMAP MF_00333
	Region	108 – 110	3	Substrate binding By similarity HAMAP MF_00333
	Region	240 – 275	36	Important for dimerization By similarity HAMAP MF_00333
	Region	258 – 263	6	Substrate binding By similarity HAMAP MF_00333
Sites
	Active site	106	1	Proton donor By similarity HAMAP MF_00333
	Binding site	92	1	Substrate By similarity HAMAP MF_00333
	Site	175	1	Important for dimerization By similarity HAMAP MF_00333

Sequences

	Sequence		Length	Mass (Da)
	C2DV19 [UniParc]. Last modified June 16, 2009. Version 1. Checksum: DC689C92CD71AE9B	FASTA	299	34,304
	10 20 30 40 50 60 MKPDAHQVKQ FLLNLQDTIC QQLSAVDGAE FVEDSWQREA GGGGRSRVLR NGGVFEQAGV 70 80 90 100 110 120 NFSHVHGEAM PASATAHRPE LAGRSFEAMG VSLVVHPHNP YVPTSHANVR FFIAEKPGAE 130 140 150 160 170 180 PVWWFGGGFD LTPFYGFEED AIHWHRTARD LCLPFGEDVY PRYKKWCDEY FYLKHRNEQR 190 200 210 220 230 240 GIGGLFFDDL NTPDFDHCFA FMQAVGKGYT DAYLPIVERR KAMAYGERER NFQLYRRGRY 250 260 270 280 290 VEFNLVWDRG TLFGLQTGGR TESILMSMPP LVRWEYDYQP KDGSPEAALS EFIKVRDWV

References

[1]

Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y. , Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., Worley K., Gibbs R. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: 83972 EMBL EEJ46297.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	ACGN01000122 Genomic DNA. Translation: EEJ46297.1.
3D structure databases
ProteinModelPortal	C2DV19.
SMR	C2DV19. Positions 8-299.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
PATRIC	31225668. VBIEscCol21464_4224.
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.
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

C2DV19_ECOLX

Accession

Primary (citable) accession number: C2DV19

Entry history

Integrated into UniProtKB/TrEMBL:	June 16, 2009
Last sequence update:	June 16, 2009
Last modified:	December 14, 2011
This is version 17 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)