NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.01726-06; PubMed=17293413 [NCBI, ExPASy, EBI, Israel, Japan]
Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
"The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes.";
J. Bacteriol. 189:3228-3236(2007).

Comments

CATALYTIC ACTIVITY: Coproporphyrinogen-III + O₂ + 2 H⁺ = protoporphyrinogen-IX + 2 CO₂ + 2 H₂O.
COFACTOR: Manganese (By similarity).
PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen III (O2 route): step 1/1 .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the aerobic coproporphyrinogen III oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000468; ABJ01840.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_853554.1; -.

3D structure databases

ModBase

A1ADV0.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004109;	Molecular function: coproporphyrinogen oxidase activity (inferred from electronic annotation from HAMAP).
GO:0006779;	Biological process: porphyrin biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00333; -; 1.
PBIL [Tree]

InterPro

IPR001260; Coprogen_oxidas.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.1500.10; Coprogen_oxidas; 1.

PANTHER

PTHR10755; Coprogen_oxidas; 1.

Pfam

PF01218; Coprogen_oxidas; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000166; Coproporphyri_ox; 1.

PRINTS

PR00073; COPRGNOXDASE.

PROSITE

PS01021; COPROGEN_OXIDASE; 1.

BLOCKS

A1ADV0.

Genome annotation databases

GeneID

4495748; -.

GenomeReviews

CP000468_GR; Ecok1_23460.

KEGG

ecv:APECO1_4112; -.

CMR

A1ADV0; Ecok1_23460.

Other

ProtoNet

A1ADV0.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Manganese; Oxidoreductase; Porphyrin biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 299`	`299`		`Coproporphyrinogen III oxidase, aerobic.`	`PRO_1000019468`

Sequence information

Length: 299 AA [This is the length of the unprocessed precursor]

Molecular weight: 34304 Da [This is the MW of the unprocessed precursor]

CRC64: DC689C92CD71AE9B [This is a checksum on the sequence]

        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

A1ADV0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools