ID A0A433WM28_9BACT Unreviewed; 448 AA.
AC A0A433WM28;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN Name=hemG {ECO:0000313|EMBL:NSL90606.1};
GN ORFNames=ECE50_027525 {ECO:0000313|EMBL:NSL90606.1};
OS Chitinophaga solisilvae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1233460 {ECO:0000313|EMBL:NSL90606.1, ECO:0000313|Proteomes:UP000281028};
RN [1] {ECO:0000313|EMBL:NSL90606.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Mgbs1 {ECO:0000313|EMBL:NSL90606.1};
RA Goh C.B.S., Lee M.S., Parimannan S., Pasbakhsh P., Yule C.M., Rajandas H.,
RA Loke S., Croft L., Tan J.B.L.;
RT "Chitinophaga laudate sp. nov., isolated from a tropical peat swamp.";
RL Submitted (MAY-2020) 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:NSL90606.1}.
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DR EMBL; RIAR02000001; NSL90606.1; -; Genomic_DNA.
DR Proteomes; UP000281028; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000281028}.
SQ SEQUENCE 448 AA; 48423 MW; D0D8510B1E016C74 CRC64;
MPQEPVLIIG AGISGLSIAY ELQQLQIPYV LTEAAPAAGG VIRSLHQSGF ELDAGPNTIA
ATPEVLAFFK SLGLEDKILV AAAAGKKRFL VRNNQLHAVS PHPFKIMGSP YLSRGSKWKL
FTERFRKPAP AAGEESVSSF VTRRFNKEIA EYVFDPVLSG IYAGNPDLMS VGEVLPALPR
WEREYGSVTK GLMKEKEVMA GRKIISFRGG NEVLVSRLQE LLQTPVRFGC NVKTVTRKGD
SYEVAYEEKG TAGTLTAQQV IFTGPAYTAA DQIATLDAAT AALLQDIVYP RMGVMHLGFN
TADISSPIDG FGFLVPHAEG LHFLGAICNS AIFPDKAPEG KTLLTVFIGG ARQEHYFDQP
GAEQLKQHVL REVSSLLGIT AAPVMQHFGY WDKAIPQLNI GHAKLRAAAK AFEEKYPGLH
LSGNYLQGVA IPGLLQHAAT LAASLKKN
//
