ID Q92DD1_LISIN Unreviewed; 459 AA.
AC Q92DD1;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 111.
DE RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN OrderedLocusNames=lin0883 {ECO:0000313|EMBL:CAC96115.1};
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626 {ECO:0000313|EMBL:CAC96115.1, ECO:0000313|Proteomes:UP000002513};
RN [1] {ECO:0000313|EMBL:CAC96115.1, ECO:0000313|Proteomes:UP000002513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262 {ECO:0000313|Proteomes:UP000002513};
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.D.,
RA Fsihi H., Portillo F.G., Garrido P., Gautier L., Goebel W., Gomez-Lopez N.,
RA Hain T., Hauf J., Jackson D., Jones L.M., Kaerst U., Kreft J., Kuhn M.,
RA Kunst F., Kurapkat G., Madueno E., Maitournam A., Vicente J.M., Ng E.,
RA Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.C.,
RA Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA Vazquez-Boland J.A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL596166; CAC96115.1; -; Genomic_DNA.
DR PIR; AC1543; AC1543.
DR RefSeq; WP_010990664.1; NC_003212.1.
DR AlphaFoldDB; Q92DD1; -.
DR STRING; 272626.gene:17565210; -.
DR KEGG; lin:lin0883; -.
DR eggNOG; COG1232; Bacteria.
DR HOGENOM; CLU_009629_3_0_9; -.
DR OMA; WFDQWFG; -.
DR OrthoDB; 9805195at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000002513; 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|RuleBase:RU364052}.
FT DOMAIN 11..451
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 459 AA; 50286 MW; 8CC1A3BF2E295AB9 CRC64;
MKHIVIIGGG LSGLAAAYEL QKTHPNYTWE LVEKDEKLGG KFETVKRDGF LIEKGPDSFL
ARKPAGVGLV KDLGLEDKLI ANATGRSYIY HQKALHPIPE GSVMGIPTDR EALLASTLVS
EIGKARALQE PTIEPNNQET DQPLGEFFEA RFGKELVKTI IEPLLSGIYA GDIYKMSLRA
TFPQFEQTVR KYGNLMDGLK ESTMQTTGTK GTIGAFRTLE GGLDRLPKAI ADALPAENLH
TAKQATQITK KNTSYEISFA DGDKKEADGV IIAATHDALI HLLAETTTAP FAEQPLTTLA
TVSLAYDEKD VPILPDGTGY LVARTALYKT TACTWVQKKW PHMVPKDKML LRGFVGKAGE
SWLEQASDEA IVTAVLTDYA EIMDLHAAPL FYEVSRMKSA MPQYLVDHQD RLKQLKKNIQ
TDYPGVYFAG MSYEGVGIPD CIAGAQTAVT ELADFLEEV
//