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
//