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
//