ID A0A099D4L3_9ACTN Unreviewed; 469 AA.
AC A0A099D4L3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|ARBA:ARBA00019046, ECO:0000256|RuleBase:RU364052};
DE EC=1.3.3.15 {ECO:0000256|ARBA:ARBA00012402, ECO:0000256|RuleBase:RU364052};
GN Name=hemG {ECO:0000313|EMBL:ASU79490.1};
GN ORFNames=CDG81_15755 {ECO:0000313|EMBL:ASU79490.1}, IL38_14005
GN {ECO:0000313|EMBL:KGI80881.1};
OS Actinopolyspora erythraea.
OC Bacteria; Actinomycetota; Actinomycetes; Actinopolysporales;
OC Actinopolysporaceae; Actinopolyspora.
OX NCBI_TaxID=414996 {ECO:0000313|EMBL:ASU79490.1, ECO:0000313|Proteomes:UP000215043};
RN [1] {ECO:0000313|EMBL:KGI80881.1, ECO:0000313|Proteomes:UP000029737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM90600 {ECO:0000313|EMBL:KGI80881.1,
RC ECO:0000313|Proteomes:UP000029737};
RX PubMed=25250723;
RA Chen D., Feng J., Huang L., Zhang Q., Wu J., Zhu X., Duan Y., Xu Z.;
RT "Identification and Characterization of a New Erythromycin Biosynthetic
RT Gene Cluster in Actinopolyspora erythraea YIM90600, a Novel Erythronolide-
RT Producing Halophilic Actinomycete Isolated from Salt Field.";
RL PLoS ONE 9:E108129-E108129(2014).
RN [2] {ECO:0000313|EMBL:ASU79490.1, ECO:0000313|Proteomes:UP000215043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90600 {ECO:0000313|EMBL:ASU79490.1,
RC ECO:0000313|Proteomes:UP000215043};
RA Yin M., Tang S.;
RT "The complete genome sequence of moderately halophilic actinomycete
RT Actinopolyspora erythraea YIM 90600, the producer of novel erythromycin,
RT novel actinopolysporins A-C and tubercidin.";
RL Submitted (AUG-2017) 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|ARBA:ARBA00002185, 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|ARBA:ARBA00001755};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43437;
CC Evidence={ECO:0000256|ARBA:ARBA00001755};
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|ARBA:ARBA00004744,
CC 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|ARBA:ARBA00008310, ECO:0000256|RuleBase:RU364052}.
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DR EMBL; CP022752; ASU79490.1; -; Genomic_DNA.
DR EMBL; JPMV01000025; KGI80881.1; -; Genomic_DNA.
DR RefSeq; WP_043574356.1; NZ_KN214177.1.
DR AlphaFoldDB; A0A099D4L3; -.
DR KEGG; aey:CDG81_15755; -.
DR eggNOG; COG1232; Bacteria.
DR HOGENOM; CLU_009629_3_1_11; -.
DR OrthoDB; 4496419at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000029737; Unassembled WGS sequence.
DR Proteomes; UP000215043; 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 11..462
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 469 AA; 48655 MW; 8B5E19B545813613 CRC64;
MSRVAVIGGG VAGMTAAYRL RELLGEHAEI LVFDQAERAG GKLRTVRLAD RGYDLGAEAF
LARRPEVLRL AEELELDGEL VHPGSASARV RAGGANRALP AGMLMGVPAS GRAVSGVLSD
SGVRAVEREP ELEPPRLTGG DASVGDLLRK RFGHEVVERL VEPLLGGVYG GSADALGLRA
TMPALASALD AGAESLTAAV NAAMPEPTPP GTDKPPVFGA FRDGYDTLLS ELRKRSRASF
ELGLPVRQLR PLRRGWSLSI GAAPSPRTLD VDALVLAVPP PAARRLLTEA VPRAAEGFGR
IRLASMAVIG LALPSHVELP DASGVLLARG ERHADGTPFT AKAFTFSSRK WPHLRGGGGQ
PLVRASVGRG DPADLRPDDG ELVRRVSADL AELTGVPDAP LESRVVRWGG GLPQYGVGHR
EIVAEIEEAV SRTPGLAVAG AALHGVGVPA CVATGESAAA TIADRLGAS
//
