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Database: UniProt
Entry: E6W257_DESIS
LinkDB: E6W257_DESIS
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ID   E6W257_DESIS            Unreviewed;       461 AA.
AC   E6W257;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE            EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN   OrderedLocusNames=Selin_0772 {ECO:0000313|EMBL:ADU65515.1};
OS   Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC   Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC   Desulfurispirillum.
OX   NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU65515.1, ECO:0000313|Proteomes:UP000002572};
RN   [1] {ECO:0000313|EMBL:ADU65515.1, ECO:0000313|Proteomes:UP000002572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC   {ECO:0000313|Proteomes:UP000002572};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA   Bini E., Woyke T.;
RT   "Complete sequence of Desulfurispirillum indicum S5.";
RL   Submitted (DEC-2010) 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; CP002432; ADU65515.1; -; Genomic_DNA.
DR   RefSeq; WP_013505403.1; NC_014836.1.
DR   AlphaFoldDB; E6W257; -.
DR   STRING; 653733.Selin_0772; -.
DR   KEGG; din:Selin_0772; -.
DR   eggNOG; COG1232; Bacteria.
DR   HOGENOM; CLU_009629_3_0_0; -.
DR   InParanoid; E6W257; -.
DR   OMA; WFDQWFG; -.
DR   OrthoDB; 9805195at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000002572; Chromosome.
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:UP000002572}.
FT   DOMAIN          12..452
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   461 AA;  50368 MW;  F656C8E7F3FDC956 CRC64;
     MTERIAIIGG GLSGLGTAYY LHQGAPDARI TVFEAAPRTG GKIQTSRGEF TCESGPNGFL
     DSRPEIVQLS HELGLTATLL PANANSARRF IYSSARLNEI HAHPLKFMAS PLLSPLGKLR
     LCLEHFAPKP RAEDETLEEF GCRKLGREAF ERLIDPMASG VYAGNPAHMS VRSCFPRIYQ
     MERQYGSLTR ALFAIKKEKK QQGETSSGPA GPAGLLTSFK GGLYEMIEAL QEQCGATIRT
     NCPVLNLTCS QDSQWEVWTS AGKETFDAVV CATPAWDSAD ILHSGFAELA GKLRAIQSSP
     ISVVALAYDT PSLSGVDTNG FGFLVPGREG RKLLGSLWSS SIFQHRAPAG TFLTQCMVGG
     ARQPELALLD DDALVQLVRD ELRITMGIAA EPIYRKIFRW DAGIPQYNMG HSQILSDIEE
     LRRHTPRLYF TGNSYRGISV NDCVVDARSI SELLLREGRT P
//
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