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Database: UniProt
Entry: E0I5X3_9BACL
LinkDB: E0I5X3_9BACL
Original site: E0I5X3_9BACL 
ID   E0I5X3_9BACL            Unreviewed;       467 AA.
AC   E0I5X3;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE            EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN   ORFNames=PaecuDRAFT_1045 {ECO:0000313|EMBL:EFM12365.1};
OS   Paenibacillus curdlanolyticus YK9.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM12365.1, ECO:0000313|Proteomes:UP000005387};
RN   [1] {ECO:0000313|EMBL:EFM12365.1, ECO:0000313|Proteomes:UP000005387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YK9 {ECO:0000313|EMBL:EFM12365.1,
RC   ECO:0000313|Proteomes:UP000005387};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA   Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT   "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL   Submitted (JUL-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; AEDD01000002; EFM12365.1; -; Genomic_DNA.
DR   RefSeq; WP_006037060.1; NZ_AEDD01000002.1.
DR   AlphaFoldDB; E0I5X3; -.
DR   STRING; 717606.PaecuDRAFT_1045; -.
DR   eggNOG; COG1232; Bacteria.
DR   OrthoDB; 9805195at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000005387; 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   ECO:0000313|EMBL:EFM12365.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005387}.
FT   DOMAIN          11..458
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   467 AA;  51237 MW;  010831798425D91E CRC64;
     MKTIAIIGGG ITGLSTAYYL QKQINERKLD ATIVLIEASE QLGGKIATLP AGPFMMETGA
     DSIVARKSNM TPLLDELGLQ DEIVYNATGR SYIHVDGELK LIPEEAVFGI PLSLESLAGS
     TLLSAEGKVD ALRDFYTPNT TFTKDDSIGD FLSFFLGKEL VEKQISPVLS GVYSGELHEL
     TLASTLPYLL DYKNEHGSII QGLAANRAKF KGKGDKKFYS FANGLSALID RMEERIPSVD
     IRKGTKAERI EKAEGSSYSI RLMNGETIQA DSIVLGTLHP VAQSLLQSPM LDEEFDQMRN
     SSLTSVYIAF DIADDELPLD GTGFIAAENS SLICNACTWT SRKWTHTSKT SQLLVRLFYK
     STKPAFEKLR NGSEQELLKT ALSDVKAAMG IVAEPLHYVV TKWDDTMPNY HIRHHAIVRA
     LETKMAEQFP RIRLAGCSYY GVGIPDCVAN GEQIAVDLAE WLAGESE
//
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