PPOX_BOVIN
ID PPOX_BOVIN Reviewed; 477 AA.
AC P56602; E1BPX0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protoporphyrinogen oxidase;
DE Short=PPO;
DE EC=1.3.3.4;
GN Name=PPOX;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP PROTEIN SEQUENCE OF 2-14 AND 164-178, FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=7607249; DOI=10.1111/j.1432-1033.1995.0760h.x;
RA Taketani S., Yoshinaga T., Furukawa T., Kohno H., Tokunaga R.,
RA Nishimura K., Inokuchi H.;
RT "Induction of terminal enzymes for heme biosynthesis during differentiation
RT of mouse erythroleukemia cells.";
RL Eur. J. Biochem. 230:760-765(1995).
CC -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC to form protoporphyrin-IX. {ECO:0000269|PubMed:7607249}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX;
CC Xref=Rhea:RHEA:25576, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:57307; EC=1.3.3.4;
CC Evidence={ECO:0000269|PubMed:7607249};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC -!- SUBUNIT: Monomer. Homodimer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Intermembrane side
CC {ECO:0000250}. Mitochondrion {ECO:0000269|PubMed:7607249}. Note=Bound
CC to the mitochondrial inner membrane with its active site facing the
CC cytosolic side. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:7607249}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Protoporphyrinogen oxidase subfamily. {ECO:0000305}.
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DR EMBL; DAAA02006959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S65629; S65629.
DR RefSeq; NP_001179355.1; NM_001192426.1.
DR RefSeq; XP_005203553.1; XM_005203496.2.
DR RefSeq; XP_005203554.1; XM_005203497.3.
DR AlphaFoldDB; P56602; -.
DR SMR; P56602; -.
DR STRING; 9913.ENSBTAP00000053328; -.
DR PaxDb; P56602; -.
DR PRIDE; P56602; -.
DR Ensembl; ENSBTAT00000061124; ENSBTAP00000053328; ENSBTAG00000021894.
DR GeneID; 515770; -.
DR KEGG; bta:515770; -.
DR CTD; 5498; -.
DR VEuPathDB; HostDB:ENSBTAG00000021894; -.
DR VGNC; VGNC:33219; PPOX.
DR eggNOG; KOG1276; Eukaryota.
DR GeneTree; ENSGT00390000008744; -.
DR HOGENOM; CLU_009629_2_1_1; -.
DR OMA; WFDQWFG; -.
DR OrthoDB; 1578484at2759; -.
DR TreeFam; TF323479; -.
DR Reactome; R-BTA-189451; Heme biosynthesis.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000021894; Expressed in retina and 105 other tissues.
DR GO; GO:0031304; C:intrinsic component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IBA:GO_Central.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00562; proto_IX_ox; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Heme biosynthesis; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..477
FT /note="Protoporphyrinogen oxidase"
FT /id="PRO_0000135269"
FT BINDING 9..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 34..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 57..60
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 454..456
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 477 AA; 50612 MW; E2A4581893001BEB CRC64;
MGRTVVVLGG GISGLAASYY LSRAPCPPKV VLVEGSERLG GWIRSVRGPD GAIFELGPRG
IRPAGALGAR TLLLVSELGL DSEVLPVRGD HPAAQNRFLY VGGALHALPS GIRGLLRPSP
PFSKPLFWAG LRDLTTPRGK DPDETVHSFA QRRLGPEVAS LAMDSLCRGV FAGNSRELSI
RSCFPSLFQA EQTHRSILLG LLLGAGRGPQ LDSALIRQAQ AERWSQWSLR GGLETLPQAL
HAHLTSRGVS VLQGQPVCGL SLQAEGRWKV SLEDSSLEAD HIISAIPASV LSKLLPAEAT
PLARALSTIT AVSVAVVNLQ YRGARLPVQG FGHLVPSSED PVILGIVYDS VAFPEQDGSL
PGLRLTVMLG GSWLQTLEAR GCVLSQELLQ QEAEKAAATQ LGLNEPPSHC LVHLHKNSIP
QYTLGHWQKL ESAAQFLAAQ KLPLTLAGAS YEGVAVNDCI ESGRQAAARV LGTEPNS
