ID B7HR92_BACC7 Unreviewed; 466 AA.
AC B7HR92;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN Name=hemY2 {ECO:0000313|EMBL:ACJ80130.1};
GN OrderedLocusNames=BCAH187_A2517 {ECO:0000313|EMBL:ACJ80130.1};
OS Bacillus cereus (strain AH187).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534 {ECO:0000313|EMBL:ACJ80130.1, ECO:0000313|Proteomes:UP000002214};
RN [1] {ECO:0000313|EMBL:ACJ80130.1, ECO:0000313|Proteomes:UP000002214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187 {ECO:0000313|EMBL:ACJ80130.1,
RC ECO:0000313|Proteomes:UP000002214};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
RL Submitted (OCT-2008) 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; CP001177; ACJ80130.1; -; Genomic_DNA.
DR AlphaFoldDB; B7HR92; -.
DR KEGG; bcr:BCAH187_A2517; -.
DR HOGENOM; CLU_009629_3_0_9; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000002214; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364052}.
FT DOMAIN 31..458
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 466 AA; 52197 MW; 34EE405CA270F9B0 CRC64;
MKTVVVIGGG ITGLSTMFYL EKLKKDYNID LNLILVEKEE YLGGKIHSVE EKDFIMESGA
DSIVARNEHV MPLIKDLNLE EEMVYNETGI SYIYSDNILH PIPSDTIFGI PMSARSLFSS
TLVSTKGKIV ALKDFITKNK EFTKDTSLAV FLESFLGKEL VERQIAPVLS GVYSGKLNEL
TMASTLPYLL DYKNKYGSII KGFEENKKQF QSAGNKKFVS FKGGLSTIID RLEEVLTETV
VKKGVVTTAV SKQGNRYEVS FANHESIQAD YVVLATPHDI AESLLQSNEL NEQFHTFKNS
SLISIYLGFD ILDEQLPADG TGFIVTENSD LHCDACTWTS RKWKHTSGNQ KLLVRMFYKS
TNPVYETIKN YNEEKLVRVA LYDIEKSLGI KGEPEVVEVT KWKDLMPKYH LEHNQAVQTL
QEKMTDLYPN VYLAGASYYG VGIGACIGNG KNTANKIIAT LNEPTN
//
