ID A0A1V3FXL8_9BACI Unreviewed; 472 AA. AC A0A1V3FXL8; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 13-SEP-2023, entry version 21. DE RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052}; DE EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052}; GN ORFNames=BO219_00755 {ECO:0000313|EMBL:OOE06346.1}; OS Anoxybacillus karvacharensis. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus. OX NCBI_TaxID=1919277 {ECO:0000313|EMBL:OOE06346.1, ECO:0000313|Proteomes:UP000188458}; RN [1] {ECO:0000313|EMBL:OOE06346.1, ECO:0000313|Proteomes:UP000188458} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=103 {ECO:0000313|EMBL:OOE06346.1, RC ECO:0000313|Proteomes:UP000188458}; RA Hovhannisyan P., Panosyan H., Birkeland N.-K.; RT "Draft genome sequence of Anoxybacillus sp. strain 103 isolated from the RT Qarvajar hot spring in Nagorno-Karabach."; RL Submitted (NOV-2016) 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OOE06346.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MQAD01000001; OOE06346.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1V3FXL8; -. DR EnsemblBacteria; OOE06346; OOE06346; BO219_00755. DR UniPathway; UPA00252; -. DR Proteomes; UP000188458; 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|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU364052}. FT DOMAIN 12..460 FT /note="Amine oxidase" FT /evidence="ECO:0000259|Pfam:PF01593" SQ SEQUENCE 472 AA; 52663 MW; F3EFE74872B24248 CRC64; MKKKVVIIGG GMTGLAAAYY LQKEAREKQL PISCELIEAS HRLGGKVQTV YRDGFVIERG PDSFLARKMS ASRLIHEVGL EKELVHNTAG QSYILVNRTL HPIPSGAVMG IPTKLAPFVV TRLFSPFGKL RAAADFVLPP LKTKGDVSLG QFFRRRLGNE VVDRLIEPLL SGIYAGDIDQ LSLMATFPQY FHLEQKHGSL VLGMKRSMPK QKTKQKSDKG IFQTLKTGLA SLVDAIEQRL EKGTVHKGVR VERIEKVEER YVLTLSNGEK KEADSVVVAV PHQSLPSLFP NETMFSSFET MPSTSVATVA LAFPKEAVAK DMNGTGFVVS RDSDYTITAC TWTHKKWPHT TPEGYVLLRC YVGRPGDEAI VDQTDEDIVQ VVMDDLNKVM NITMNPMFSI VTRWKQSMPQ YTVGHRERME RVKQHMQQHL PGIFLAGSSY EGLGLPDCID QGEEAVKKVL HYLAYTKEKV SL //