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Database: UniProt
Entry: I0I3W7_CALAS
LinkDB: I0I3W7_CALAS
Original site: I0I3W7_CALAS 
ID   I0I3W7_CALAS            Unreviewed;       473 AA.
AC   I0I3W7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE            EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN   Name=hemY {ECO:0000313|EMBL:BAL99954.1};
GN   OrderedLocusNames=CLDAP_19150 {ECO:0000313|EMBL:BAL99954.1};
OS   Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS   STL-6-O1).
OC   Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC   Caldilinea.
OX   NCBI_TaxID=926550 {ECO:0000313|EMBL:BAL99954.1, ECO:0000313|Proteomes:UP000007880};
RN   [1] {ECO:0000313|EMBL:BAL99954.1, ECO:0000313|Proteomes:UP000007880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC   {ECO:0000313|Proteomes:UP000007880};
RA   Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA   Hanada S., Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT   102666).";
RL   Submitted (FEB-2012) 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|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}.
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DR   EMBL; AP012337; BAL99954.1; -; Genomic_DNA.
DR   RefSeq; WP_014433190.1; NC_017079.1.
DR   AlphaFoldDB; I0I3W7; -.
DR   STRING; 926550.CLDAP_19150; -.
DR   KEGG; cap:CLDAP_19150; -.
DR   PATRIC; fig|926550.5.peg.2125; -.
DR   eggNOG; COG1232; Bacteria.
DR   HOGENOM; CLU_009629_3_0_0; -.
DR   OrthoDB; 9805195at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000007880; 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:UP000007880}.
FT   DOMAIN          13..465
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   473 AA;  52039 MW;  D06B7CD781EF6E09 CRC64;
     MSRYPVAIIG GGIAGLSAAW WLQKAGIDYT LLEQDARWGG KIHTERVALD DCEETPFIVE
     AGPDSFITQK PWGVALAREV GLGDSLIGTN EDLKQTYVLH RGRPTPLPDG VLMIVPTRIK
     PFLLSPLISP WGKLRMGMEL FIPPRRDDGD ETLADFVRRR LGSEALDKIA EPLMSGIYNA
     EADKQSLLAT FPRFRELEQK HGSLIRGMVA SQRLRSQHAA SSNGKPLPFF VTPSEGVEAL
     VTALQRRLRG DLRLRTGVEA LEPVAGGYRL HLGDGTTLDA GQVILATPAY VAARLLRPLT
     PEAADLLDGI RYVSTGTISL AFHSGAVRNP LHGYGLVIPM SERRPINAVT LSSVKFAYRA
     PEGCLLLRVF FGGSRSPRSM ELNDEDLYTT VRRELDALLG INAEPLFHRI YRWFHSNPQY
     DVGHLERVAA IERHLPPGVH LAGSAYRGVG LPDCIRQGQE AAERVVSGKK ERS
//
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