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}.
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; 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
//