Reviewed, UniProtKB/Swiss-Prot P95506 (HEMN_PASHA)

Names and origin

Protein names

Recommended name:
    Oxygen-independent coproporphyrinogen-III oxidase
      Short name=Coproporphyrinogenase
      Short name=Coprogen oxidase
    EC=1.3.99.22

Gene names

Name:

hemN

Organism

Pasteurella haemolytica (Mannheimia haemolytica)

Taxonomic identifier

75985 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Mannheimia

Protein attributes

Sequence length	146 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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 structure	Monomer.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the anaerobic coproporphyrinogen-III oxidase family.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Cellular component	Cytoplasm
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW porphyrin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW coproporphyrinogen dehydrogenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›146	›146	Oxygen-independent coproporphyrinogen-III oxidase		PRO_0000109946
Sites
	Metal binding	60	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	64	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	67	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Experimental info
	Non-terminal residue	146	1

Sequences

	Sequence		Length	Mass (Da)
	P95506-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: F7C6AEFC4F2301EF	FASTA	146	17,351
	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

References

[1]	"The restriction-modification system of Pasteurella haemolytica is a member of a new family of type I enzymes." Highlander S.K., Garza O. Gene 178:89-96(1996) [PubMed: 8921897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Serotype A1 / PH101.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U46781 Genomic DNA. Translation: AAC44662.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.3.99.22. 267636.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

HEMN_PASHA

Accession

Primary (citable) accession number: P95506

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	May 1, 1997
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)