ID   A0A385YX82_9BACL        Unreviewed;       474 AA.
AC   A0A385YX82;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE            EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN   ORFNames=D3873_09870 {ECO:0000313|EMBL:AYC30163.1};
OS   Paenisporosarcina cavernae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae;
OC   Paenisporosarcina.
OX   NCBI_TaxID=2320858 {ECO:0000313|EMBL:AYC30163.1, ECO:0000313|Proteomes:UP000265725};
RN   [1] {ECO:0000313|Proteomes:UP000265725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K2R23-3 {ECO:0000313|Proteomes:UP000265725};
RA   Zhu H.;
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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; CP032418; AYC30163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A385YX82; -.
DR   KEGG; paek:D3873_09870; -.
DR   OrthoDB; 9805195at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000265725; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU364052};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265725};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..460
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   474 AA;  52290 MW;  1E73F8B88298323D CRC64;
     MSQQKKKIII IGGGITGLSA AFYMQKEARE KGYPLEITLI ESSPRLGGKI QTLRKDGFIV
     ERGPDSFLAR KVSFGQLAED LGIEDQLVKN ATGQAYVLVG EELHPIPAGS VMGIPTEISP
     FVTSGLFSWS GKVRAAGDFV LPKSNIQGDQ SLGHFFRRRF GNEVVENLIE PLLSGIYAGD
     LDRLSLQATF PQFEKVEQEH RSLILGTKRT TPKSPTKAKK EGIFRTFRDG LETIVESLEQ
     ALTDVQLYKG VRAERLQQVG EQVEITLNTG STLQADGIIL TTPHGVTKSL LEEHGIMEEF
     EEMPSTSVAT VAMAFKEDQV QISKDGTGFV VSRNSDYSIT ACTWTHKKWP TTTPEGHVLM
     RGYVGRAGDE AIVDLSDKEI EKVVLDDLRK TTKIDGDPLF TVVTRWKEAM PQYVVGHQDR
     VQRVKADLAT KLPHVKLAGS SYEGLGLPDC VDQGKAMTRE LLDELFLKEV VVAK
//