UniProt: A0A0M4LES1

Database: UniProt
Entry: A0A0M4LES1_9MICC

LinkDB:  A0A0M4LES1_9MICC 
Original site:  A0A0M4LES1_9MICC

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

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ID   A0A0M4LES1_9MICC        Unreviewed;       492 AA.
AC   A0A0M4LES1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=AL755_16870 {ECO:0000313|EMBL:ALE07933.1};
OS   Arthrobacter sp. ERGS1:01.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE07933.1, ECO:0000313|Proteomes:UP000060433};
RN   [1] {ECO:0000313|EMBL:ALE07933.1, ECO:0000313|Proteomes:UP000060433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE07933.1,
RC   ECO:0000313|Proteomes:UP000060433};
RX   PubMed=26415659; DOI=10.1016/j.jbiotec.2015.09.025;
RA   Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT   "Complete genome sequence of Arthrobacter sp. ERGS1:01, a putative novel
RT   bacterium with prospective cold active industrial enzymes, isolated from
RT   East Rathong glacier in India.";
RL   J. Biotechnol. 214:139-140(2015).
RN   [2] {ECO:0000313|Proteomes:UP000060433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS1:01 {ECO:0000313|Proteomes:UP000060433};
RA   Kumar R., Swarnkar M.K., Singh A.K., Singh D.;
RT   "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01.";
RL   Submitted (AUG-2015) 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; CP012479; ALE07933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M4LES1; -.
DR   STRING; 1704044.AL755_16870; -.
DR   KEGG; are:AL755_16870; -.
DR   PATRIC; fig|1704044.3.peg.2705; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000060433; 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:UP000060433}.
FT   DOMAIN          7..475
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   492 AA;  49024 MW;  0DB525A0F2A53ED2 CRC64;
     MVVGGGVSGL VAAKDLAAAG YRVDVYDAAA SWGGCVGVHE VAGVVLDSGA ESFATRSTAV
     ADLAAELGLA ENITTPDPSG AWVWLPGGPV PLPRTGVLGI PADLHAPEVR EALGTSGILR
     AALDATMPAT VGTTEAVSSV ADLVRARMGR RVLERLVAPV VGGIHSADPE VLDVDMVAPG
     LRAGIRKHGS LAAAVAAQRA GGSKPGSAVG GLRGGMHTLV TALVAQLRES GVALHAGHTV
     TAVRGEAANE ATNEAAGEVS GAAGRWSIDW SAGTDSGNTP GTTTAELLVV ATDGPTAVKL
     LAAELPGLLP HAPAPGPDIR LVTLVVDVPE LDSKPRGTGI LVAPQSEGIT AKALTHATAK
     WEWLAESTGP GTHVLRLSYG KAGIAAADAV RLTARVVTDA DLIATALADA TTLLGVSVTD
     ADLVGADVVR WRGALPFAAV GHLAKVAQIQ ELADAREGLV LTGGWLSGNG LAAVVAGTRR
     QIAAVTGAPP AA
//

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