NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pgen.0030231; PubMed=18159947 [NCBI, ExPASy, EBI, Israel, Japan]
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.;
"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus.";
PLoS Genet. 3:2515-2528(2007).

Comments

CATALYTIC ACTIVITY: Coproporphyrinogen-III + O₂ + 2 H⁺ = protoporphyrinogen-IX + 2 CO₂ + 2 H₂O.
PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen III (O2 route): step 1/1 .
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

CP000551; ABM71072.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001010179.1; -.

3D structure databases

ModBase

A2BTG1.

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

A2BTG1.

Genome annotation databases

GeneID

4718523; -.

GenomeReviews

CP000551_GR; A9601_17891.

KEGG

pmb:A9601_17891; -.

CMR

A2BTG1; A9601_17891.

Other

ProtoNet

A2BTG1.

UniRef

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

Keywords

Complete proteome; Cytoplasm; Oxidoreductase; Porphyrin biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 342`	`342`		`Coproporphyrinogen III oxidase, aerobic.`	`PRO_1000019480`

Sequence information

Length: 342 AA [This is the length of the unprocessed precursor]

Molecular weight: 39554 Da [This is the MW of the unprocessed precursor]

CRC64: 77782845E1E26A8B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLKEPPKNSR EKTKNLLLTL QDKICSGLEN VDGKGKFTEE SWLRDEGGGG RSRVLKNGSI 

        70         80         90        100        110        120 
FEQAGVNFSE VQGKELPQSI ISQRPEAKGH EWFATGTSMV LHPKNPYIPT VHLNYRYFEA 

       130        140        150        160        170        180 
GPVWWFGGGA DLTPFYPYLS DVRNFHNEHK KACEKVDQDL HKVFKPWCDE YFFLKHRNES 

       190        200        210        220        230        240 
RGIGGIFYDY QDGSGNIYRG NNKNGEASKA SQNVGRSNLN WDNLFSLAEN CGQAFLPSYL 

       250        260        270        280        290        300 
PIIEKRASQK YSPKEREFQL YRRGRYVEFN LVWDRGTIFG LQTNGRTESI LMSLPPLARW 

       310        320        330        340 
EYGYKAKNGS REEFLTSIFT KPQDWFNDKE LEKFCMENNI FD

A2BTG1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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