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Database: UniProt
Entry: E3EH62_PAEPS
LinkDB: E3EH62_PAEPS
Original site: E3EH62_PAEPS 
ID   E3EH62_PAEPS            Unreviewed;       481 AA.
AC   E3EH62;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE            EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN   Name=hemY1 {ECO:0000313|EMBL:ADO55853.1};
GN   ORFNames=PPSC2_08875 {ECO:0000313|EMBL:ADO55853.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO55853.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO55853.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO55853.1,
RC   ECO:0000313|Proteomes:UP000006868};
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT   growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT   activity.";
RL   J. Bacteriol. 193:311-312(2011).
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; CP002213; ADO55853.1; -; Genomic_DNA.
DR   RefSeq; WP_013370471.1; NC_014622.2.
DR   AlphaFoldDB; E3EH62; -.
DR   STRING; 1406.LK13_21340; -.
DR   KEGG; ppm:PPSC2_08875; -.
DR   PATRIC; fig|886882.15.peg.1871; -.
DR   eggNOG; COG1232; Bacteria.
DR   HOGENOM; CLU_009629_3_0_9; -.
DR   OMA; WFDQWFG; -.
DR   OrthoDB; 9805195at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000006868; 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:UP000006868}.
FT   DOMAIN          15..465
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   481 AA;  52937 MW;  C5BD4259861757DE CRC64;
     MEQKLRNIVI VGGGLTGLST AFYTRKMYKE AGYTPRITLV EKASALGGKI ETLHKDGFVI
     EKGPDSFLAR KTAMIDLAKE LEMDHELVST NPEAKKTYIL HEGQLHPMPP GLVLGIPTEL
     KPFLRSGLIS LGGKMRAMMD FVIPPRREPG DEALGDFIER RLGKEVLENV TEPLLAGIYA
     ANMKTLSLQA TFPQFAEVEQ QYGSLIHGMR TGRKPAETHT GTKKSAFLTF RQGLQSLVHA
     LLNDLYDCDL RTGIAVTEFT KTTETKGSPY CVMLDNGETL EADDIFVTTP NFAAAPLLRD
     HVNVSALEAV NYVSVANVVM AFDKTDIENI FDGSGFLVPR KEGRSVTACT WTSAKWLHTS
     PDDKVLLRCY VGRAGAEETV DLPDNELIAV VRKDLKEMMG VTATPLFTEI TRLRNSMPQY
     PVGHPQAIAN LREELRSAMP GVYVLGAGYD AIGLPDCIRQ AKEWASKAVH TAQREAVKVQ
     V
//
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