Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P51175 (PPOX_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protoporphyrinogen oxidase

Short name=PPO
EC=1.3.3.4
Gene names
Name:Ppox
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. Ref.1

Catalytic activity

Protoporphyrinogen-IX + 3 O2 = protoporphyrin-IX + 3 H2O2. Ref.1

Cofactor

Binds 1 FAD per subunit By similarity.

Enzyme regulation

Inhibited by acifluorfen. Ref.1

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.

Subunit structure

Monomer. Homodimer By similarity.

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side Ref.4.

Induction

During erythroid differentiation. Ref.1 Ref.2

Sequence similarities

Belongs to the protoporphyrinogen oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 477477Protoporphyrinogen oxidase
PRO_0000135272

Regions

Nucleotide binding9 – 146FAD By similarity
Nucleotide binding34 – 352FAD By similarity
Nucleotide binding57 – 604FAD By similarity
Nucleotide binding454 – 4563FAD By similarity

Sites

Binding site421FAD; via amide nitrogen By similarity
Binding site2571FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site4491FAD; via amide nitrogen By similarity

Experimental info

Sequence conflict641A → T Ref.2
Sequence conflict661A → P Ref.2
Sequence conflict1081L → S in BAA08126. Ref.2
Sequence conflict1761R → Q in AAH02047. Ref.3
Sequence conflict4271W → C in BAA08126. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P51175 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 8CFB48120728DE6F

FASTA47750,871
        10         20         30         40         50         60 
MGRTVIVLGG GISGLAASYH LIRGPSPPKV ILVEGSKRLG GWIRSIRGSD GAIFELGPRG 

        70         80         90        100        110        120 
IRPAGALGAR TLLLVSELGL ESEVLPVRGD HPAAQNRFLY VGGTLHPLPS GLRGLLRPSP 

       130        140        150        160        170        180 
PFSKPLFWAG LRELLKPRGK EPDETVHSFA QRRLGPEVAS LAMDSLCRGV FAGNSRELSI 

       190        200        210        220        230        240 
RSCFPSLFQA EQTHRSILLG LLLGAGQSPQ PDSSLIRQAR AERWSQWSLR GGLEVLPQAL 

       250        260        270        280        290        300 
HNHLASKGVT VLSGQPVCGL SLQPEGRWKV SLGDSSLEAD HIISAIPASE LSKLLPAEAA 

       310        320        330        340        350        360 
PLARILSTIK AVSVAVVNLQ YRGACLPVQG FGHLVPSSED PTVLGIVYDS VAFPEQDGNP 

       370        380        390        400        410        420 
PSLRVTVMLG GYWLQKLKAA GHQLSPELFQ QQAQEAAATQ LGLKEPPSHC LVHLHKNCIP 

       430        440        450        460        470 
QYTIGHWQKL DSAMQFLTAQ RLPLTLAGAS YEGVAVNDCI ESGRQAAVAV LGTESNS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequence, and expression of mouse protoporphyrinogen oxidase."
Dailey T.A., Dailey H.A., Meissner P., Prasad A.R.
Arch. Biochem. Biophys. 324:379-384(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
[2]"Induction of terminal enzymes for heme biosynthesis during differentiation of mouse erythroleukemia cells."
Taketani S., Yoshinaga T., Furukawa T., Kohno H., Tokunaga R., Nishimura K., Inokuchi H.
Eur. J. Biochem. 230:760-765(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
Tissue: Erythroleukemia.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
[4]"Organization of the terminal two enzymes of the heme biosynthetic pathway. Orientation of protoporphyrinogen oxidase and evidence for a membrane complex."
Ferreira G.C., Andrew T.L., Karr S.W., Dailey H.A.
J. Biol. Chem. 263:3835-3839(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U25114 mRNA. Translation: AAA96003.1.
D45185 mRNA. Translation: BAA08126.1.
BC002047 mRNA. Translation: AAH02047.1.
CCDSCCDS15487.1.
PIRS65684.
S68367.
RefSeqNP_032937.1. NM_008911.2.
XP_006496770.1. XM_006496707.1.
UniGeneMm.266888.

3D structure databases

ProteinModelPortalP51175.
SMRP51175. Positions 2-474.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP51175.

Proteomic databases

MaxQBP51175.
PaxDbP51175.
PRIDEP51175.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000073120; ENSMUSP00000072863; ENSMUSG00000062729.
GeneID19044.
KEGGmmu:19044.
UCSCuc007dns.1. mouse.

Organism-specific databases

CTD5498.
MGIMGI:104968. Ppox.

Phylogenomic databases

eggNOGCOG1232.
GeneTreeENSGT00390000008744.
HOGENOMHOG000269479.
HOVERGENHBG001709.
InParanoidP51175.
KOK00231.
OMAWIRSIRG.
OrthoDBEOG7DJSMB.
PhylomeDBP51175.
TreeFamTF323479.

Enzyme and pathway databases

UniPathwayUPA00251; UER00324.

Gene expression databases

ArrayExpressP51175.
BgeeP51175.
CleanExMM_PPOX.
GenevestigatorP51175.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.660.20. 1 hit.
InterProIPR002937. Amino_oxidase.
IPR016040. NAD(P)-bd_dom.
IPR004572. Protoporphyrinogen_oxidase.
IPR027418. Protoporphyrinogen_oxidase_C.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00562. proto_IX_ox. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPPOX. mouse.
NextBio295501.
PROP51175.
SOURCESearch...

Entry information

Entry namePPOX_MOUSE
AccessionPrimary (citable) accession number: P51175
Secondary accession number(s): P97344, Q99M34
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot