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Database: UniProt
Entry: G7W4G4_PAETH
LinkDB: G7W4G4_PAETH
Original site: G7W4G4_PAETH 
ID   G7W4G4_PAETH            Unreviewed;       481 AA.
AC   G7W4G4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE            EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN   OrderedLocusNames=HPL003_16875 {ECO:0000313|EMBL:AET60121.1};
OS   Paenibacillus terrae (strain HPL-003).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=985665 {ECO:0000313|EMBL:AET60121.1, ECO:0000313|Proteomes:UP000005876};
RN   [1] {ECO:0000313|Proteomes:UP000005876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPL-003 {ECO:0000313|Proteomes:UP000005876};
RA   Shin S.H., Kim S., Kim J.Y.;
RT   "Complete sequence of Paenibacillus terrae HPL-003.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HPL-003;
RA   Shin S.H., Kim S., Kim J.Y.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AET60121.1, ECO:0000313|Proteomes:UP000005876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPL-003 {ECO:0000313|EMBL:AET60121.1,
RC   ECO:0000313|Proteomes:UP000005876};
RX   PubMed=22328761; DOI=10.1128/JB.06668-11;
RA   Shin S.H., Kim S., Kim J.Y., Song H.Y., Cho S.J., Kim D.R., Lee K.I.,
RA   Lim H.K., Park N.J., Hwang I.T., Yang K.S.;
RT   "Genome Sequence of Paenibacillus terrae HPL-003, a Xylanase-Producing
RT   Bacterium Isolated from Soil Found in Forest Residue.";
RL   J. Bacteriol. 194:1266-1266(2012).
CC   -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis.
CC       Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin
CC       III. {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|RuleBase:RU364052};
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|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|RuleBase:RU364052}.
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DR   EMBL; CP003107; AET60121.1; -; Genomic_DNA.
DR   RefSeq; WP_014280834.1; NC_016641.1.
DR   AlphaFoldDB; G7W4G4; -.
DR   STRING; 985665.HPL003_16875; -.
DR   KEGG; pta:HPL003_16875; -.
DR   eggNOG; COG1232; Bacteria.
DR   HOGENOM; CLU_009629_3_0_9; -.
DR   OMA; WFDQWFG; -.
DR   OrthoDB; 9805195at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000005876; 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|RuleBase:RU364052}.
FT   DOMAIN          15..465
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   481 AA;  52870 MW;  3ECB323D2BB21F6C CRC64;
     MEQKLRNIVI VGGGLTGLST AFYTRKMYKE AGYTPRITLV EKAPVLGGKI ETLHKDGFVI
     EKGPDSFLAR KTAMIDLAKE LELDHELVST NPEAKKTYIL HEGQLHPMPP GLVLGIPTEL
     KPFLRSGLIS LGGKLRAMMD FVIQPRRVSG DEALGDFIER RLGKEVLENI TEPLLAGIYA
     ANMKTLSLQA TFPQFAEVEQ QYGSLIHGMM TGRKPAETHT GTKKSVFLTF RQGLQSLVHA
     LLDDLRDCDL RRGVAVTEFT KTADGEGSVY HVVLDNGETL EADDLFITTP NFAAAPLLRG
     HVNVAALEAV NYVSVANVVM AFNKKDIENV FDGSGFLVPR KEGRSVTACT WTSAKWLHTS
     PDDKVLLRCY VGRAGAEETV ELPDDELTAL VRKDLQDMMG ITATPLFTEI TRLRHSMPQY
     PVGHPQAIAD LREELRTTMP GVYVLGAGYD AIGLPDCIRQ AKEWASVAVQ AAEREAVEVQ
     V
//
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