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
//