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P56602 (PPOX_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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.2

Catalytic activity

Protoporphyrinogen-IX + 3 O2 = protoporphyrin-IX + 3 H2O2. Ref.2

Cofactor

Binds 1 FAD per subunit By similarity.

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 By similarity. Mitochondrion. Note: Bound to the mitochondrial inner membrane with its active site facing the cytosolic side By similarity. Ref.2

Tissue specificity

Detected in liver (at protein level). Ref.2

Sequence similarities

Belongs to the protoporphyrinogen oxidase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 477477Protoporphyrinogen oxidase
PRO_0000135269

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

Sequences

Sequence LengthMass (Da)Tools
P56602 [UniParc].

Last modified February 19, 2014. Version 2.
Checksum: E2A4581893001BEB

FASTA47750,612
        10         20         30         40         50         60 
MGRTVVVLGG GISGLAASYY LSRAPCPPKV VLVEGSERLG GWIRSVRGPD GAIFELGPRG 

        70         80         90        100        110        120 
IRPAGALGAR TLLLVSELGL DSEVLPVRGD HPAAQNRFLY VGGALHALPS GIRGLLRPSP 

       130        140        150        160        170        180 
PFSKPLFWAG LRDLTTPRGK DPDETVHSFA QRRLGPEVAS LAMDSLCRGV FAGNSRELSI 

       190        200        210        220        230        240 
RSCFPSLFQA EQTHRSILLG LLLGAGRGPQ LDSALIRQAQ AERWSQWSLR GGLETLPQAL 

       250        260        270        280        290        300 
HAHLTSRGVS VLQGQPVCGL SLQAEGRWKV SLEDSSLEAD HIISAIPASV LSKLLPAEAT 

       310        320        330        340        350        360 
PLARALSTIT AVSVAVVNLQ YRGARLPVQG FGHLVPSSED PVILGIVYDS VAFPEQDGSL 

       370        380        390        400        410        420 
PGLRLTVMLG GSWLQTLEAR GCVLSQELLQ QEAEKAAATQ LGLNEPPSHC LVHLHKNSIP 

       430        440        450        460        470 
QYTLGHWQKL ESAAQFLAAQ KLPLTLAGAS YEGVAVNDCI ESGRQAAARV LGTEPNS 

« Hide

References

« Hide 'large scale' references
[1]"A whole-genome assembly of the domestic cow, Bos taurus."
Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.
Genome Biol. 10:R42.01-R42.10(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hereford.
[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: PROTEIN SEQUENCE OF 2-14 AND 164-178, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DAAA02006959 Genomic DNA. No translation available.
PIRS65629.
RefSeqNP_001179355.1. NM_001192426.1.
XP_005203553.1. XM_005203496.1.
XP_005203554.1. XM_005203497.1.
UniGeneBt.4335.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000053328.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000061124; ENSBTAP00000053328; ENSBTAG00000021894.
GeneID515770.
KEGGbta:515770.

Organism-specific databases

CTD5498.

Phylogenomic databases

eggNOGCOG1232.
GeneTreeENSGT00390000008744.
OMAPNGFLDS.
OrthoDBEOG7DJSMB.

Enzyme and pathway databases

UniPathwayUPA00251; UER00324.

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

NextBio20871996.

Entry information

Entry namePPOX_BOVIN
AccessionPrimary (citable) accession number: P56602
Secondary accession number(s): E1BPX0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 19, 2014
Last modified: April 16, 2014
This is version 65 of the entry and version 2 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