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Database: UniProt
Entry: H5UU55_9MICO
LinkDB: H5UU55_9MICO
Original site: H5UU55_9MICO 
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
//
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