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Database: UniProt
Entry: D8PCL4_9BACT
LinkDB: D8PCL4_9BACT
Original site: D8PCL4_9BACT 
ID   D8PCL4_9BACT            Unreviewed;       484 AA.
AC   D8PCL4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 59.
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:CBK40973.1};
GN   ORFNames=NIDE1217 {ECO:0000313|EMBL:CBK40973.1};
OS   Nitrospira defluvii.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Nitrospira.
OX   NCBI_TaxID=330214 {ECO:0000313|EMBL:CBK40973.1, ECO:0000313|Proteomes:UP000001660};
RN   [1] {ECO:0000313|EMBL:CBK40973.1, ECO:0000313|Proteomes:UP000001660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20624973; DOI=10.1073/pnas.1003860107;
RA   Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B.,
RA   Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.;
RT   "A Nitrospira metagenome illuminates the physiology and evolution of
RT   globally important nitrite-oxidizing bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 0:13479-13484(2010).
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; FP929003; CBK40973.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8PCL4; -.
DR   STRING; 330214.NIDE1217; -.
DR   KEGG; nde:NIDE1217; -.
DR   eggNOG; COG1232; Bacteria.
DR   HOGENOM; CLU_009629_3_0_0; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000001660; 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,
KW   ECO:0000313|EMBL:CBK40973.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001660}.
FT   DOMAIN          15..476
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   484 AA;  52269 MW;  DDC368C665F14D07 CRC64;
     MARTPRSVVI VGGGISGLST AFALQEQAAA AGMALTCTIL DAAPVWGGKI LTHRVGQLVM
     EAGPDSFLSQ KPWGMELCRR LGIADQLINT NPVEKKASVL RGGQLHELPE GLVTFTPTQL
     GPFFRSGLLS WVDLARMGCD VLIPPRRSTD DESLASFFRR RFGRHACERV MEPLMAGIYA
     GDAEQMSLRA TFPRFYELEQ AHGSVIRGMM AARRARAQKV SGGGPRHTMF VTLKNGLADL
     VAGLTAQIQQ AGGVLKAGVQ AEALRVRSHQ AGRWMYDVMC TDGTAISAEA LVLATPAYVS
     AELVRPLTPM AAGLMDMIPY ASTATISLIY PAEAVGNRLQ GFGFVVPRSE GRDLIAATWT
     SLKWPHRAPP EDVSVRCYLG GVGREVILQR DDEALVRCVR EELASIVGLQ ATPHYVEVNR
     WNRAMPQYTL GHLDRLVQLD AALSRFGGLA VTGAGYRGVG LPDCIRDGAD TAAKILHYLH
     TAPM
//
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