ID H5UU55_9MICO Unreviewed; 472 AA.
AC H5UU55;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
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 ORFNames=MOPEL_099_00630 {ECO:0000313|EMBL:GAB49263.1};
OS Mobilicoccus pelagius NBRC 104925.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Mobilicoccus.
OX NCBI_TaxID=1089455 {ECO:0000313|EMBL:GAB49263.1, ECO:0000313|Proteomes:UP000004367};
RN [1] {ECO:0000313|EMBL:GAB49263.1, ECO:0000313|Proteomes:UP000004367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 104925 {ECO:0000313|EMBL:GAB49263.1,
RC ECO:0000313|Proteomes:UP000004367};
RA Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Mobilicoccus pelagius NBRC 104925.";
RL Submitted (FEB-2012) 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|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}.
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:GAB49263.1}.
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DR EMBL; BAFE01000076; GAB49263.1; -; Genomic_DNA.
DR AlphaFoldDB; H5UU55; -.
DR STRING; 1089455.MOPEL_099_00630; -.
DR eggNOG; COG1232; Bacteria.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000004367; 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|RuleBase:RU364052};
KW Reference proteome {ECO:0000313|Proteomes:UP000004367}.
FT DOMAIN 8..458
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 472 AA; 49094 MW; AF5D3F0C75C40543 CRC64;
MAVIGGGVSG LRAARRLAEA GADVTVLEAS PRIGGQVHTV EVAGVPVDTG AEAMHLGAPG
VTDLLDSLGL TDDMVTARPG ASWIVTPRGL RRLPAGVGPA GPTRLRPVLR SGVMTVPGLV
RAGLEPIVAQ RVGGIDLSPG EDRSVGDFVG SRFGGQVVDR FVDPLLGSLH AGDVRTLSLR
ATTPSLVPAA TAGRSLVRKR RPARTGAAPT MSFVSWREGL DRVVTALASG LDVHTDTPVE
VVERLTPGEG RERGGYRVVV GGSDPRTLDV DGLVLATPGD VTARLLAEVS PEASAPLTLT
DRASVATIVL AYPRHVVEAL PAFRGTGVLV PSRVGSLLKA ATFLSTKWPQ LDHPEWYFCR
LSAGRAGDDR LASFDDDELL ARVRGDLRTI IGLDVAPRHA LVQRWPHAMP QLTVGHPDRV
ATARAALPAG VTIAGSSYDG VGIASCLTSA TRAADTLLDH LGLTATQGDR PV
//