ID D6ELR6_STRLI Unreviewed; 494 AA.
AC D6ELR6;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 64.
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=SSPG_01586 {ECO:0000313|EMBL:EFD65946.2};
OS Streptomyces lividans TK24.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=457428 {ECO:0000313|EMBL:EFD65946.2};
RN [1] {ECO:0000313|EMBL:EFD65946.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TK24 {ECO:0000313|EMBL:EFD65946.2};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Galagan J., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces lividans strain TK24.";
RL Submitted (FEB-2009) 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}.
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; GG657756; EFD65946.2; -; Genomic_DNA.
DR RefSeq; WP_003972880.1; NZ_GG657756.1.
DR AlphaFoldDB; D6ELR6; -.
DR HOGENOM; CLU_009629_3_1_11; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000002769; 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|RuleBase:RU364052}.
FT DOMAIN 27..470
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 494 AA; 50671 MW; 4E6380BB85208826 CRC64;
MSASETPAGE FPPEQEPGHV VVVGAGIAGL AAAHRLLEAG ARVTVLEASG RVGGKLLPGE
IAGVRVDLGA ESMLARRPEA VGLARAAGLA DRLQPPSTAT ASLWTRGALR PMPKGHVMGV
PGTAAALSGV LSEEGLARIE RDAELPRTEV GDDVAVGEYV AARLGREVVD RLVEPLLGGV
YAGDAYRISL RSAVPQLFEA ARTHTSLTEA VRALQGRTAT SPPSGPVFMG IEGGIGTLPP
AVADSVRARG GEIVTQAPVT ELRRTASDGW RIVAGDRVLH AGAVVVAVPA GPAAELLRAE
APAAAAELSA VEYASMALVT LAYRRSEAAA LPEGSGFLVP PVDGHTIKAS TFASRKWGWI
ADEDPDLVVL RTSVGRYGDT EILGRDDAGL VAVSRHDLAE ATGLTAAPVA TRVTRWQDGL
PQYPVGHHAR VARVREHVAK LPGLAVCGAA YDGVGIPASI ASAYAAADQI RGDLGGVEEL
TAHPVQSLHG GAGE
//