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Database: UniProt
Entry: D1PTD0_9BACT
LinkDB: D1PTD0_9BACT
Original site: D1PTD0_9BACT 
ID   D1PTD0_9BACT            Unreviewed;       395 AA.
AC   D1PTD0;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE            EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN   Name=hemG {ECO:0000313|EMBL:EFA45354.1};
GN   ORFNames=HMPREF0645_0215 {ECO:0000313|EMBL:EFA45354.1};
OS   Hallella bergensis DSM 17361.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hallella.
OX   NCBI_TaxID=585502 {ECO:0000313|EMBL:EFA45354.1, ECO:0000313|Proteomes:UP000003160};
RN   [1] {ECO:0000313|EMBL:EFA45354.1, ECO:0000313|Proteomes:UP000003160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17361 {ECO:0000313|EMBL:EFA45354.1,
RC   ECO:0000313|Proteomes:UP000003160};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (OCT-2009) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFA45354.1}.
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DR   EMBL; ACKS01000014; EFA45354.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1PTD0; -.
DR   eggNOG; COG1232; Bacteria.
DR   HOGENOM; CLU_009629_3_0_10; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000003160; Unassembled WGS sequence.
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:UP000003160}.
FT   DOMAIN          12..373
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   395 AA;  44347 MW;  26D0582A29D8359B CRC64;
     MKHPEVAELF EQLADKCQLE TALESSKRRL IWKDDRFHNL PSSLPTAIAT PLFTWKDKLR
     ILGEPWRKRG TDPNESVGSL AERRLGKSYV DYAVDPFLSG VYAGDPYKLP TRLALPKLYR
     LEQDYGSFIR GSIAKARQPK TDRDRKATKA VFSARGGFNK LVDALAEAIG ADRITTSARH
     IRVMPDGDGW MVSYEKDGET RAIRSRRVVT TCGSYSLPDL LPFVDRTVMA DLSNLRYAPV
     VQIGVGLRDT HYHDWLAFGG LVPSKERREV LGILFPSACF SGRAPENGAS LAYFMGGMRH
     PEMVGKSDEK LTEIVDRTLV DMLKYPVGTH PDTLRIFRHE RAIPQYEAST DRRIAAVERL
     RKLYSTLTIA GNLRDGIGIG DRIKQGCDVA ANENY
//
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