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Database: UniProt
Entry: A0A1R1EZ60_9BACL
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ID   A0A1R1EZ60_9BACL        Unreviewed;       464 AA.
AC   A0A1R1EZ60;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE            EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN   ORFNames=BK138_00035 {ECO:0000313|EMBL:OMF57062.1};
OS   Paenibacillus rhizosphaerae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=297318 {ECO:0000313|EMBL:OMF57062.1, ECO:0000313|Proteomes:UP000187172};
RN   [1] {ECO:0000313|EMBL:OMF57062.1, ECO:0000313|Proteomes:UP000187172}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R5-0378 {ECO:0000313|EMBL:OMF57062.1,
RC   ECO:0000313|Proteomes:UP000187172};
RA   Beno S.M.;
RT   "Paenibacillus species isolates.";
RL   Submitted (NOV-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OMF57062.1}.
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DR   EMBL; MRTP01000001; OMF57062.1; -; Genomic_DNA.
DR   RefSeq; WP_076164379.1; NZ_MRTP01000001.1.
DR   AlphaFoldDB; A0A1R1EZ60; -.
DR   STRING; 297318.BK138_00035; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000187172; Unassembled WGS sequence.
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:UP000187172}.
FT   DOMAIN          11..460
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   464 AA;  50896 MW;  5A771F433D0D9734 CRC64;
     MKTVVIIGGG ITGLSAAYYL RRTLNQYSGQ TEPANIILVE AEQTLGGKMR TVYDGGFTME
     SGADSIVTRK TNVAPLIQEL NLADQVVYNA TGISYIYTDG RLKQIPKDAV FGIPTSIESL
     ATTELVSAEG KVEALKDLYT PNEHFTKNDS VGAFLEAFLG KEFVEKQIAP VLSGVYSGKL
     SDLTIASTLP YLIDYKNEYG SLIKGLSENR AKFQSGGQKK FMSFQNGVSA LIDALEQQLT
     GTEIVKGVRA ESVAKDGSRY AVTLADGRVI DADYVVLGTM HYAAQQLLAD PVLDQEFNQL
     KNSSMISVYV GFDLPDAELP ADGTGFITAD GSDITCNACT WTSRKWEHTS RERKLLVRLF
     YKSSNPRYDE LVQLSEGELL NVALEDIRKS LGITGDPVTH EVTKWHNVMP NYHIKHHSIV
     KDLEQKMAER FPNIYLAGCS YYGVGIPDCI ANGEQTAYKI AAQL
//
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