NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Serotype A1 / PH101;
DOI=10.1016/0378-1119(96)00340-X; PubMed=8921897 [NCBI, ExPASy, EBI, Israel, Japan]
Highlander S.K., Garza O.;
"The restriction-modification system of Pasteurella haemolytica is a member of a new family of type I enzymes.";
Gene 178:89-96(1996).

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

U46781; AAC44662.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

P95506.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051989;	Molecular function: coproporphyrinogen dehydrogenase activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006779;	Biological process: porphyrin biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

ProtoNet

P95506.

Other

UniRef

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

Keywords

4Fe-4S; 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 >146`	`>146`	`Oxygen-independent coproporphyrinogen III oxidase.`	`PRO_0000109946`
`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).`
`NON_TER`	`146 146`

Sequence information

Length: 146 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 17351 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: F7C6AEFC4F2301EF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSEIIWDLAL IQKYNHSGPR YTSYPTALEF NENYTNEDFI RAAARYPERP LSLYVHIPFC 

        70         80         90        100        110        120 
HKLCYFCGCN KVITRHRHKV EIYLDYLERE IKTRAPLFQN RLVTQIHWGR GTPTYLDEDQ 

       130        140 
SARLMQMLRA NFDVSDDAEI SIEMDP

P95506 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