NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8809776 [NCBI, ExPASy, EBI, Israel, Japan]
de Gier J.W., Schepper M., Reijnders W.N.M., van Dyck S.J., Slotboom D.J., Warne A., Saraste M., Krab K., Finel M., Stouthamer A.H., van Spanning R.J.M., der Oost J.;
"Structural and functional analysis of aa3-type and cbb3-type cytochrome c oxidases of Paracoccus denitrificans reveals significant differences in proton-pump design.";
Mol. Microbiol. 20:1247-1260(1996).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.;
"Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Anaerobic transformation of coproporphyrinogen-III into protoporphyrinogen-IX (By similarity).
CATALYTIC ACTIVITY: Coproporphyrinogen-III + 2 S-adenosyl-L-methionine = protoporphyrinogen-IX + 2 CO₂ + 2 L-methionine + 2 5'-deoxyadenosine.
COFACTOR: Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen III (AdoMet route): step 1/1 .
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the anaerobic 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

U34353; AAC44513.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000489; ABL69948.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S77599; S77599.

RefSeq

YP_915644.1; -.

3D structure databases

ModBase

Q51676.

Ontologies

GO:0051989;	Molecular function: coproporphyrinogen dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR006638; Elp3/MiaB/NifB.
IPR004558; HemN.
IPR010723; HemN_C.
IPR007197; Radical_SAM.
Graphical view of domain structure.

Pfam

PF06969; HemN_C; 1.
PF04055; Radical_SAM; 1.
Pfam graphical view of domain structure.

SMART

SM00729; Elp3; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00538; hemN; 1.

BLOCKS

Q51676.

Genome annotation databases

GeneID

4581035; -.

GenomeReviews

CP000489_GR; Pden_1851.

KEGG

pde:Pden_1851; -.

CMR

Q51676; Pden_1851.

Other

ProtoNet

Q51676.

UniRef

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

Keywords

4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Porphyrin biosynthesis; S-adenosyl-L-methionine.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 451`	`451`	`Oxygen-independent coproporphyrinogen III oxidase.`	`PRO_0000109945`
`REGION`	`112 113`	`2`	`S-adenosyl-L-methionine 2 binding (By similarity).`
`METAL`	`60 60`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`METAL`	`64 64`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`METAL`	`67 67`		`Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity).`
`BINDING`	`54 54`		`S-adenosyl-L-methionine 1 (By similarity).`
`BINDING`	`66 66`		`S-adenosyl-L-methionine 2; via carbonyl oxygen (By similarity).`
`BINDING`	`111 111`		`S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`144 144`		`S-adenosyl-L-methionine 1 (By similarity).`
`BINDING`	`171 171`		`S-adenosyl-L-methionine 2 (By similarity).`
`BINDING`	`183 183`		`S-adenosyl-L-methionine 2 (By similarity).`
`BINDING`	`208 208`		`S-adenosyl-L-methionine 2 (By similarity).`

Sequence information

Length: 451 AA [This is the length of the unprocessed precursor]

Molecular weight: 49848 Da [This is the MW of the unprocessed precursor]

CRC64: D424AA04E4B4519A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEQQSQLERL GLFDARVPRY TSYPTAPHFT PAVGEPVFRD WIAAIPAGAA ISLYMHVPFC 

        70         80         90        100        110        120 
RRLCWFCACR TQGTQSDEPV RAYAKALLAE LDMLKSALAP GVRLSRLHWG GGTPTLMPAE 

       130        140        150        160        170        180 
MMRLVAGAVL DAFPLAEGAE FSVEIDPNEI DEARMDALAE AGLNRASIGV QDFDPEIQKI 

       190        200        210        220        230        240 
IGREQSFEVT KRAVDMIRDR GIASLNADIL YGLPHQDPHR IAESVQKLLA LSPDRVALYG 

       250        260        270        280        290        300 
YAHVPWMAKR QVMIPSEALP DPHGRLRLFE TARELFLADG YDEIGIDHFA RPGDGLARAQ 

       310        320        330        340        350        360 
KAGLLRRNFQ GYTDDRAEVL VGLGASSISR FPQGYAQNAP ATGAHLARIR DGRFSTTRGH 

       370        380        390        400        410        420 
AFSAEDRWRS RMIEALMCDF EIRAEEFIRD HGFDAESLSR ILTPVAAHFG DMVDADASGL 

       430        440        450 
RITPRGRPLT RMIARMFDGY DMAASGHSAA I

Q51676 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