GenomeNet

Database: UniProt
Entry: H8IV54_MYCIA
LinkDB: H8IV54_MYCIA
Original site: H8IV54_MYCIA 
ID   H8IV54_MYCIA            Unreviewed;       458 AA.
AC   H8IV54;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
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   OrderedLocusNames=OCU_34050 {ECO:0000313|EMBL:AFC44624.1};
OS   Mycobacterium intracellulare (strain ATCC 13950 / DSM 43223 / JCM 6384 /
OS   NCTC 13025 / 3600).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=487521 {ECO:0000313|EMBL:AFC44624.1, ECO:0000313|Proteomes:UP000008004};
RN   [1] {ECO:0000313|EMBL:AFC44624.1, ECO:0000313|Proteomes:UP000008004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13950 / DSM 43223 / JCM 6384 / NCTC 13025 / 3600
RC   {ECO:0000313|Proteomes:UP000008004};
RX   PubMed=22535933; DOI=10.1128/JB.00295-12;
RA   Kim B.J., Choi B.S., Lim J.S., Choi I.Y., Lee J.H., Chun J., Kook Y.H.,
RA   Kim B.J.;
RT   "Complete genome sequence of Mycobacterium intracellulare strain ATCC
RT   13950T.";
RL   J. Bacteriol. 194:2750-2750(2012).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003322; AFC44624.1; -; Genomic_DNA.
DR   RefSeq; WP_014380583.1; NZ_CP076382.1.
DR   AlphaFoldDB; H8IV54; -.
DR   KEGG; mia:OCU_34050; -.
DR   PATRIC; fig|487521.10.peg.3415; -.
DR   eggNOG; COG1232; Bacteria.
DR   HOGENOM; CLU_009629_3_1_11; -.
DR   OMA; EHNQAVQ; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000008004; 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:AFC44624.1}.
FT   DOMAIN          13..446
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   458 AA;  46954 MW;  52C2299D8D27FE96 CRC64;
     MTSRSYCVVG GGISGLTAAY RLRMSLGDDA AITLFDPGER LGGILRTELV GGAPMDLGAE
     AFVLRRPELP ALLDELNLTG HQLVSTGARP LIYSGQRLRP LPTGTVVGIP SSAASVAGLV
     DEATVARIDA EPSRPLEWVA GSDPAVADLV GDRFGDQVVA RSVDPLLSGV YAGSAATIGL
     RAAAPTVAAA LDRGAASLTD AVGRALPPAT GAPVFGALDG GYRVLVEELA ARARPRWVRA
     AASRLERADA GWAVFDDTGA RWLADAVILA VPVHESCRLL GGIAPRSVAA AGRIASASSV
     VLALAVPADT AFPDCSGVLV ATGERLRAKA ITLSSRKWGA RADVQLLRLS FGRFGDHVAA
     STSDDELLAW ALGDVATVFG LDVDPVDVRV QRWIDAMPQY GPGHAELVAE VRAGLPPTLA
     VAGSYLDGIG VPACVGAAGR AAEDVIRAIG GPDPEVAR
//
DBGET integrated database retrieval system