ID D3PRT5_MEIRD Unreviewed; 459 AA.
AC D3PRT5;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN OrderedLocusNames=Mrub_1406 {ECO:0000313|EMBL:ADD28168.1};
GN ORFNames=K649_06690 {ECO:0000313|EMBL:AGK04638.1};
OS Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus
OS ruber).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK04638.1, ECO:0000313|Proteomes:UP000013026};
RN [1] {ECO:0000313|EMBL:ADD28168.1, ECO:0000313|Proteomes:UP000006655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC {ECO:0000313|Proteomes:UP000006655}, and DSM 1279
RC {ECO:0000313|EMBL:ADD28168.1};
RX PubMed=21304689; DOI=10.4056/sigs.1032748;
RA Tindall B.J., Sikorski J., Lucas S., Goltsman E., Copeland A.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A.,
RA Fahnrich R., Goodwin L., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Meiothermus ruber type strain (21).";
RL Stand. Genomic Sci. 3:26-36(2010).
RN [2] {ECO:0000313|EMBL:AGK04638.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK04638.1};
RA Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J.,
RA Eichler E., Turner S.W.;
RT "Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT
RT Sequencing Data.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AGK04638.1, ECO:0000313|Proteomes:UP000013026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC {ECO:0000313|Proteomes:UP000013026}, and DSM 1279
RC {ECO:0000313|EMBL:AGK04638.1};
RA Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL Submitted (APR-2013) 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; CP001743; ADD28168.1; -; Genomic_DNA.
DR EMBL; CP005385; AGK04638.1; -; Genomic_DNA.
DR RefSeq; WP_013013687.1; NC_021081.1.
DR AlphaFoldDB; D3PRT5; -.
DR STRING; 504728.K649_06690; -.
DR KEGG; mrb:Mrub_1406; -.
DR KEGG; mre:K649_06690; -.
DR PATRIC; fig|504728.9.peg.1376; -.
DR eggNOG; COG1232; Bacteria.
DR OMA; WFDQWFG; -.
DR OrthoDB; 9805195at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000006655; Chromosome.
DR Proteomes; UP000013026; 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 ECO:0000313|EMBL:ADD28168.1}.
FT DOMAIN 12..445
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 459 AA; 49306 MW; 01D15454A3BBA72D CRC64;
MASVVVVGGG AAGLSTAYYL HRAAPHLHIT LLEADARLGG KITTVAEHGF VLEGGPDAVV
RYKPWALELM HQLGLENQIV GTKPAHPSAL IHDGREALPI PAGLQMVIPG DLKALAQSPL
LSPFGKARAA LELLLPKGTP EDEPFGAFIE RRLGRQVWER LVAPLSGGIY GGDPYELSTL
AAFPQLKALE QQHGSLIRGA IQQRKARGSR EKGQLFASLE GGLGRLVEAI QARLGRVEIR
LNTTVTALER SGGWRIHTTQ GSLQADALVL ATPAPVTGCL LEPLHPEAAA ALRQIPYGPS
STVTFAFAKE KLPPRVGHGM LMAAHRGFSV RGFTWADQKW PGRAPEGYGL VRAYFSGLEA
SKEELAQLAL RDLARLWGQV PEPLHTWVFR WPEGLPRYTV GHRERVAQAL KAEELSGLFL
VGAAYQGVGL PEVIRMGQEV AERVLAYTGA QARDGAPVG
//