UniProt: A0A0B8NJI7

Database: UniProt
Entry: A0A0B8NJI7_9NOCA

LinkDB:  A0A0B8NJI7_9NOCA 
Original site:  A0A0B8NJI7_9NOCA

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (4)   
   InterPro (3)   
   Pfam (1)   
All databases (10)   

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ID   A0A0B8NJI7_9NOCA        Unreviewed;       448 AA.
AC   A0A0B8NJI7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=NS07_v2contig00070-0010 {ECO:0000313|EMBL:GAM48303.1};
OS   Nocardia seriolae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=37332 {ECO:0000313|EMBL:GAM48303.1, ECO:0000313|Proteomes:UP000019401};
RN   [1] {ECO:0000313|EMBL:GAM48303.1, ECO:0000313|Proteomes:UP000019401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N-2927 {ECO:0000313|EMBL:GAM48303.1,
RC   ECO:0000313|Proteomes:UP000019401};
RA   Imajoh M., Fukumoto Y., Yamane J., Sukeda M., Shimizu M., Ohnishi K.,
RA   Oshima S.;
RT   "Draft Genome Sequence of Nocardia seriolae Strain N-2927 (NBRC 110360),
RT   Isolated as the Causal Agent of Nocardiosis of Yellowtail (Seriola
RT   quinqueradiata) in Kochi Prefecture, Japan.";
RL   Genome Announc. 3:e00082-15(2015).
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}.
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:GAM48303.1}.
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DR   EMBL; BAWD02000070; GAM48303.1; -; Genomic_DNA.
DR   RefSeq; WP_036546379.1; NZ_BBYQ01000075.1.
DR   AlphaFoldDB; A0A0B8NJI7; -.
DR   STRING; 37332.NS506_05839; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000019401; 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:UP000019401}.
FT   DOMAIN          10..443
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   448 AA;  46123 MW;  C16827968F574B9A CRC64;
     MRVAVVGGGI SGLVAAYRVR KALGDAAELV LIERRDRVGG ILRTVEIEGD PVDLGAEAFV
     GRRPEIPELM GELGIGDQLV YPAGKRPLVW SQGSGHRLPE RTLMGIPGAA ESVAGLVDAQ
     TLAVIADEPN RPMAWQPGGD VSVGELVRDR FGEQVVRRSV DPLLGGVYAG LADSIGVRAA
     LPPLAAALDR GATSLTQAVS DALPAPGPTP VFGGIRDGYR VLLDALREAA DVKVEIGTAA
     TGLTHTAAGW RLDPVGEVDA VILATPAPVT AELLRGVAPE AAALAAGIEL ASSAVVAMAL
     PAETALPDNS GILVATGEPL RAKAFTLSSR KWPHLAARDV ALVRASFGRF GDDSPLSWPD
     DDLIEAAVED LATVTGLEIR PLRTFVQRWP GGLPQYAPGH TTRIADLRSA TADLPGLALA
     GAYLDGVGVP ACAASGTVAA ARIAEHLA
//

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