ID C9YVV7_STRSW Unreviewed; 494 AA.
AC C9YVV7;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|ARBA:ARBA00019046, ECO:0000256|RuleBase:RU364052};
DE EC=1.3.3.15 {ECO:0000256|ARBA:ARBA00012402, ECO:0000256|RuleBase:RU364052};
GN OrderedLocusNames=SCAB_20811 {ECO:0000313|EMBL:CBG69196.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG69196.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG69196.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG69196.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis.
CC Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin
CC III. {ECO:0000256|ARBA:ARBA00002185, ECO:0000256|RuleBase:RU364052}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2;
CC Xref=Rhea:RHEA:43436, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57309, ChEBI:CHEBI:131725; EC=1.3.3.15;
CC Evidence={ECO:0000256|ARBA:ARBA00001755};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43437;
CC Evidence={ECO:0000256|ARBA:ARBA00001755};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU364052};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004744,
CC ECO:0000256|RuleBase:RU364052}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364052}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Coproporphyrinogen III oxidase subfamily.
CC {ECO:0000256|ARBA:ARBA00008310, ECO:0000256|RuleBase:RU364052}.
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DR EMBL; FN554889; CBG69196.1; -; Genomic_DNA.
DR RefSeq; WP_012999918.1; NC_013929.1.
DR AlphaFoldDB; C9YVV7; -.
DR STRING; 680198.SCAB_20811; -.
DR GeneID; 24306911; -.
DR KEGG; scb:SCAB_20811; -.
DR eggNOG; COG1232; Bacteria.
DR HOGENOM; CLU_009629_3_1_11; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000001444; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.3110.10; protoporphyrinogen ix oxidase, domain 3; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_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 SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU364052};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU364052};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU364052};
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133,
KW ECO:0000256|RuleBase:RU364052};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364052};
KW Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT DOMAIN 22..470
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 494 AA; 51052 MW; 1C6429D71C8BC395 CRC64;
MSGSGTDAGR GAGHVVVIGA GIAGLAAAHR LVDRGARVTV LEAADRVGGK LLPGEIAGAR
VDLGAESMLA RRPEAVALAR EVGLADRLRP PATATASLWT RGALRPMPKG HVMGVPGTAS
ALAGVLSDEG LARIERDADL PRTEVGDDVA VGEYVAARLG REVVDRLVEP LLGGVYAGDA
YRISMRSAVP QLFQAALTHT SLTEAVRGIQ ERAAAAGQTG PVFMGIEGGI GRLPLAVAES
VRARGAEIRT RTSVTGLRRE APGGWRVVTG GTGGGEERVL RADAVVLAVP APVAAALLRA
EAPGAAAELA GVEYASMALV TLAYRRAGLT LPEGSGFLVP PVDGRTIKAS TFSSRKWGWL
AEENPDLLIL RTSVGRYGET AILDHDDAHL VDVSRTDLRE ATGLTAAPVE TRVTRWDDGL
PQYPVGHHAR VTRVREYLSK LPGLAVCGAA YDGVGIPACV ASATAAVDEI HGDLRALRDL
TADPVQSLHG GAGE
//
