ID B8M1L1_TALSN Unreviewed; 1151 AA.
AC B8M1L1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Protoporphyrinogen oxidase {ECO:0000256|ARBA:ARBA00044160};
DE EC=1.3.3.4 {ECO:0000256|ARBA:ARBA00012867};
GN ORFNames=TSTA_093440 {ECO:0000313|EMBL:EED22098.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED22098.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005073}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Protoporphyrinogen oxidase subfamily.
CC {ECO:0000256|ARBA:ARBA00010551}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EQ962653; EED22098.1; -; Genomic_DNA.
DR RefSeq; XP_002479061.1; XM_002479016.1.
DR AlphaFoldDB; B8M1L1; -.
DR STRING; 441959.B8M1L1; -.
DR GeneID; 8102588; -.
DR VEuPathDB; FungiDB:TSTA_093440; -.
DR eggNOG; KOG1276; Eukaryota.
DR eggNOG; KOG3702; Eukaryota.
DR HOGENOM; CLU_287420_0_0_1; -.
DR InParanoid; B8M1L1; -.
DR OMA; HSHANEM; -.
DR OrthoDB; 65450at2759; -.
DR PhylomeDB; B8M1L1; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 4.10.1000.30; -; 1.
DR Gene3D; 4.10.1000.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.340.40; Nuclear abundant poly(A) RNA-bind protein 2, N-terminal domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR043094; Nab2/ZC3H14_N_sf.
DR InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR NCBIfam; TIGR00562; proto_IX_ox; 1.
DR PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR PANTHER; PTHR42923:SF3; PROTOPORPHYRINOGEN OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF14608; zf-CCCH_2; 4.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 593..1104
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 105..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1151 AA; 127208 MW; C6ECA56F8F8E1480 CRC64;
MPATVAPGTP LAEALANVVQ PKLVEMGWSS DSGEDSALTE YVILMLVNGK TQDQIAEELS
NDLLNLGEGD TQAVDFSRWL FEQVEVLNNN INGLSSIPDA APAAAQSIPA SNEQNAFGAQ
DQQDATMGEA SGPSDNIPTG PRAMRENNNR GRGRLLNQIN KNLERGPDAM LHRVRGPNNS
GRINTHGRDF QKNQRGQFGP GRGGRGRPGF GQMQGQGAGN MMQMTPENQM QLMALLEEQA
RMMSQLMPGF MPPAVNPNFQ NQHQQHQQGR SLFERVERPN QRQGGDFQSR ASQNGIAAKQ
GDDGDMDTAE DQTAVDGQAS TDSVCRFNLR CTRKDCPFAH QSPAAPEGAP VDVTDTCPFG
AACKNKKCTG RHPSPAVKAS HQAEEVCRFF PHCTNPHCHF KHPSMPLCRN GADCTTEGCK
FTHLTTPCKF NPCMNRTCPY KHVEGQKGSF PDKVWIAGQE KPHVSERKFV DDENGEEELI
KPDAAQAEQF RVHTSTTDGC FNSAVDQLTN SHHLTTQLLL KQHCRKGCLY DHIFNRCMNR
FPAAAMRRYC LAHAIRPSPP TLLRSPTTSR FIKHRFFHHE TKPYNVAVIG GGLTGLTAAW
KLLQDPKCQK ITLYEKSPQV GGWLQSERIE VGGGKYVVFE HGPRTIRVAD PAVMPMLDLL
FGLDLTEQLV LISKGSPASL NRYIYYPDHL VRVPGPKPEG GTLGTIWEAI TTLFTEPLFK
GTVMGIVKEP AVEVRSDLRK DESVGDFISR RFNPTMADNI VSAVHHGIYA GDIYKLSADA
IIGIPRLLEA KHESVIIGVV DNSQQKRKIL PADYLLAMSS VVGQRPLGHF DRLRKLVRPA
SVFTIRDGMA EIARAFERVF KEHSEKIQVV TDARISDIKR EKDHNITISL NAGNETTSQT
FNRVISTAPP TEMANLIAAG SENDSQKPIE SISRLRAHNY AVNVMVVNLF YNEPNLIPYR
GFGYLIPRNI PFEQNPERGL GVIFSSETSE HQDTAVGTKL TVMMGGHWWD GWAESDFPDP
EKATLMARSL LKRHLGIDAT PVVTRARLQR NAIPQYTVNH LSKMQGLSDA VREDFDRRLT
LAGNWYGMHG VGVNDCVIQG YLAATWGVDS IEGATKFSSG MPPDLMEHQA GGIPTSSMRY
LMQQAHKIKA N
//
