ID K7RJ09_THEOS Unreviewed; 452 AA.
AC K7RJ09;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN ORFNames=Theos_1370 {ECO:0000313|EMBL:AFV76402.1};
OS Thermus oshimai JL-2.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=751945 {ECO:0000313|EMBL:AFV76402.1, ECO:0000313|Proteomes:UP000000211};
RN [1] {ECO:0000313|EMBL:AFV76402.1, ECO:0000313|Proteomes:UP000000211}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JL-2 {ECO:0000313|EMBL:AFV76402.1,
RC ECO:0000313|Proteomes:UP000000211};
RX PubMed=23405355; DOI=10.1128/genomeA.00106-12;
RA Murugapiran S.K., Huntemann M., Wei C.L., Han J., Detter J.C., Han C.S.,
RA Erkkila T.H., Teshima H., Chen A., Kyrpides N., Mavrommatis K.,
RA Markowitz V., Szeto E., Ivanova N., Pagani I., Lam J., McDonald A.I.,
RA Dodsworth J.A., Pati A., Goodwin L., Peters L., Pitluck S., Woyke T.,
RA Hedlund B.P.;
RT "Whole Genome Sequencing of Thermus oshimai JL-2 and Thermus thermophilus
RT JL-18, Incomplete Denitrifiers from the United States Great Basin.";
RL Genome Announc. 1:E00106-E00112(2013).
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis.
CC Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin
CC III. {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|RuleBase:RU364052};
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|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|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; CP003249; AFV76402.1; -; Genomic_DNA.
DR RefSeq; WP_016329588.1; NC_019386.1.
DR AlphaFoldDB; K7RJ09; -.
DR STRING; 751945.Theos_1370; -.
DR KEGG; tos:Theos_1370; -.
DR PATRIC; fig|751945.3.peg.1354; -.
DR eggNOG; COG1232; Bacteria.
DR HOGENOM; CLU_009629_3_1_0; -.
DR OrthoDB; 9805195at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000000211; 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 PRINTS; PR00420; RNGMNOXGNASE.
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}.
FT DOMAIN 12..441
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 452 AA; 48438 MW; E55502E7B3D61832 CRC64;
MAQVVVVGGG WAGLSAALAL KEAGAEVLLL EGNLRLGGKV RTHRQEGFLL EGGPDASVRY
KKEVLELGER FGLEPVGTLP AKPSAYILKG GKAHPLPEGL LQVVPGDLRA LAKTPLLSFS
GKLRALLDLL LPRGGAPDEG LKAFVERRLG PEVYRALVAP LSGGIYGGEP DELSMRAAFP
QLLELERKHR SLILGAMRAR KARGSREGGS LFFSFREGLS ALTRKMAEAL SESVLLGTPA
LGLEAQGSRY RVHTPRGFLE AEAVVLATPA PQAAALLRPF LPEATALLKG IPHTPAATVS
LAFAEALPLS GHGLLIAKGE GYRVRGFTWT HQKWPERAPE GFSLVRAYLS GEEARLGEAE
LIRLALEDLA RFLGFTPKVH RAWAFRFPEG MPAYRVGHLE RIERLEMALL KAPGVFLAGN
YLEGVGLPEV VRSGRKAAAR AVAYLALEKA PG
//
