ID M9M5C6_PSEA3 Unreviewed; 1128 AA.
AC M9M5C6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Protoporphyrinogen oxidase {ECO:0000313|EMBL:GAC75730.1};
GN ORFNames=PANT_18d00038 {ECO:0000313|EMBL:GAC75730.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC75730.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
CC -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC to form protoporphyrin-IX. {ECO:0000256|ARBA:ARBA00002600}.
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:0000256|ARBA:ARBA00000672};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320;
CC Evidence={ECO:0000256|ARBA:ARBA00000778};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005073}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the NDUFAF7 family.
CC {ECO:0000256|ARBA:ARBA00005891}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Protoporphyrinogen oxidase subfamily.
CC {ECO:0000256|ARBA:ARBA00010551}.
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DR EMBL; DF196784; GAC75730.1; -; Genomic_DNA.
DR AlphaFoldDB; M9M5C6; -.
DR STRING; 1151754.M9M5C6; -.
DR OrthoDB; 166586at2759; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000011976; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.12710; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR003788; NDUFAF7.
DR InterPro; IPR038375; NDUFAF7_sf.
DR InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00562; proto_IX_ox; 1.
DR PANTHER; PTHR12049:SF7; PROTEIN ARGININE METHYLTRANSFERASE NDUFAF7, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12049; UNCHARACTERIZED; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF02636; Methyltransf_28; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000011976};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 44..576
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 950..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1128 AA; 121758 MW; 40438323291CF06F CRC64;
MATGLRGASQ AAIAPPRRSL ATSSALLAAA ASDKKRIAVL GGGIAGLTSA YRLAQQLPQD
RYDVVLLEQQ SRLGGWIQSE RISLPSDAST SPSPTALVEM GPRSIRPAGY SGLVMLQLVQ
SLGLLERLLR VPKTAPSAQN RFLYFPDKLA KLPSSIPSLL SALFKLPFLR AIVPSIMREP
LVPSRFLRPR SESQAEKKRL QQRELLDDES VDSFVSRRFG KGVAENLVSA VIHGIYAGDT
RKLSVRAVMP FLWEAERVHG SVLRSMLPAK RNKRHRPLPE PEAAAKAAKE DRLKHVEQQL
GKELVDSFKG ISVYSFPEGV QEIVAALEQR LAALPNFQLR KGDSVRGINI DESGKLRITT
ASGESIEADR VISSVPSSKL ADILPSAELP HLKHNPAANV AVVNVVISPS AAAEAGRALV
PVQGFGYLIP RTTPGNDDGI LGVVFDSDAV PDQDAAEPSR RPVKLTVMMG GAHWAGLEQL
PDADEVKARA VRALSRQLGI DAQLLRDASK VTIKPTMQRE CIPWYLVGHP VRMAQLHKAL
AGNAHLASRL TLVGASYTGV SLNDCVAYAT EAVEHIVAAE LHGDDQTVTG LASFAIPPPA
APAAASAVRR VAQRGTAGLP SQGLVGPASS PTMQFGRALH TRRAFSTCRP LHEQGYPAAP
APTTVVGEKA NKSLREILLD SVRASGPMTV STYMRTCLLD PMQGYYASAN SPATEREVLG
SRGDFITSPE ISQVFGELLA IFYLARWQAV GSPASTRLVE LGPGKGTLLA DMLRTFASFR
PFMATLKRIQ LVETSAGLME LQLSAIRDAL AAAGKRVVDA EEEVGEDGVV VEWFPSVDMV
PIVAEEFSIV TAHEFFDALP THIFEKHVDG KFREVLVGIK PKSSITVLRP GQEMEVPKEE
LGFVLSPTPT PWAQMLVQNN PRFAALQPGQ RVEVSPESWA VARRVGELVA GRPASPPRNP
AATEEQDQQY DEAEQQRLAA NSAGGVGLII DYGGDQAYGA SFRAFKQHAL VDVFQSPGAV
DLTVNVDFLH LKSALHTTNA RYAGPIDQAD LLVGMGLQMR VDRLLQGKDD SARKRIIDAA
NRLIDETGMG VQYKALAVAA AHIPPADPRT QVRDKKQDPD MYPFEFEQ
//
