ID Q8GMY6_CORGT Unreviewed; 448 AA.
AC Q8GMY6;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 Name=hemY {ECO:0000313|EMBL:AAN38295.1};
OS Corynebacterium glutamicum (Brevibacterium saccharolyticum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1718 {ECO:0000313|EMBL:AAN38295.1};
RN [1] {ECO:0000313|EMBL:AAN38295.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R {ECO:0000313|EMBL:AAN38295.1};
RA Vertes A.A., Kos P.B., Inui M., Yukawa H.;
RT "Evolutionary Considerations on the Heme Biosynthetic Pathway of
RT Corynebacteria and Mycobacteria.";
RL Submitted (SEP-2002) 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}.
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DR EMBL; AF545862; AAN38295.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GMY6; -.
DR UniPathway; UPA00252; -.
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}.
FT DOMAIN 10..376
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 448 AA; 45709 MW; EB813B4BB6E1C1EB CRC64;
MRFAIIGAGL AGLTAAYEIH KADPTAQIDV LEAGERIGGK LFTVPFASGP TDIGAEAFLA
ARSDAVEFFT ELGLADSLVS PSAAKSQYFA GGALHAFPAG GVMGIPSNPP AGAQDTAFDW
TPGHDISVGA LVRRQYGDEI VDTVVSSLLG GVYSSTADDL GVRASVPALA AALDQLAEAG
EPVTLSAAVK AVEAQREAAK TTSETRPVFQ TFKGGYAELY EALAEQCGAD IHLDSFVSAI
TKDGEGFAIK GGGEGTYDKV ILAVPAPTAA VLLRDLAPTA APHLRAIKLA SSAVVGMRFD
SSEGLPDNSG VLVAVNEPGI TAKAFTFSSK KWPHLEARGG ALVRASFGRL GDEASARMDE
DLLVDAALDD LLTITGFDGR AAGLGEIFVQ RWFGGLPAYG VDHIAAVSAA RAEIAAVPGV
EAIGAWAGGV GVPAVIADAQ AAVHRLLG
//
