UniProt: A0A097IDL3

Database: UniProt
Entry: A0A097IDL3_9CORY

LinkDB:  A0A097IDL3_9CORY 
Original site:  A0A097IDL3_9CORY

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (4)   
   InterPro (3)   
   Pfam (1)   
All databases (11)   

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ID   A0A097IDL3_9CORY        Unreviewed;       470 AA.
AC   A0A097IDL3;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
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   ORFNames=CDOO_02415 {ECO:0000313|EMBL:AIT60233.1};
OS   Corynebacterium doosanense CAU 212 = DSM 45436.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=558173 {ECO:0000313|EMBL:AIT60233.1, ECO:0000313|Proteomes:UP000029914};
RN   [1] {ECO:0000313|EMBL:AIT60233.1, ECO:0000313|Proteomes:UP000029914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAU 212 {ECO:0000313|EMBL:AIT60233.1,
RC   ECO:0000313|Proteomes:UP000029914};
RA   Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of Corynebacterium doosanense CAU 212(T) (=DSM
RT   45436(T)), isolated from activated sludge.";
RL   Submitted (SEP-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|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; CP006764; AIT60233.1; -; Genomic_DNA.
DR   RefSeq; WP_018021369.1; NZ_CP006764.1.
DR   AlphaFoldDB; A0A097IDL3; -.
DR   STRING; 558173.CDOO_02415; -.
DR   KEGG; cdo:CDOO_02415; -.
DR   eggNOG; COG1232; Bacteria.
DR   HOGENOM; CLU_009629_3_1_11; -.
DR   OrthoDB; 4496419at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000029914; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029914}.
FT   DOMAIN          10..460
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   470 AA;  49369 MW;  41FE112191552BC9 CRC64;
     MRYAIIGAGL AGLTAAVEIH RRDPDAQIDV YEAADRIGGK LFTAPFESGP TDVGAEAFLA
     RNSEAREFFD SLGLAESVVY PSGLASALYS GGELQLLPQN TVMGIPGTSA PVAHLVSDET
     RMRIDAEEAA EPLNWVVGED RSVGDLVRRR YGDEIADRTV SALLGGVYSC SADDLGVRAT
     IPALAEALDQ LVLSNKHTTL SAAIKIMLSA RPAPVGEPQP VFGAFRGGYA ELYEALAEES
     GADIYLDAFV SAVTRTPDGF RVTGGEDATY DKVLLATPAP TTALLLKSLA PDASQTLKSV
     KLANSVVVAM KFDSAEGLPD YSGVLVAADE PDVHAKAFTF SSKKWPHLAE RGGALVRASF
     GRFGDQIALT TDEDTLVDWA LDDLQAITGF DGREAGLSEI LTQRWFGGLP CYDADHVATV
     EKFRSELAAV AGVEATGAWA DGVGVPAVIA DARAAAARLL GDNQLGGIQP
//

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