ID Q7UEZ1_RHOBA Unreviewed; 485 AA.
AC Q7UEZ1;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-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 Name=hemY {ECO:0000313|EMBL:CAD78893.1};
GN OrderedLocusNames=RB10459 {ECO:0000313|EMBL:CAD78893.1};
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD78893.1, ECO:0000313|Proteomes:UP000001025};
RN [1] {ECO:0000313|EMBL:CAD78893.1, ECO:0000313|Proteomes:UP000001025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC {ECO:0000313|Proteomes:UP000001025};
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294151; CAD78893.1; -; Genomic_DNA.
DR RefSeq; NP_869436.1; NC_005027.1.
DR RefSeq; WP_011122777.1; NC_005027.1.
DR AlphaFoldDB; Q7UEZ1; -.
DR STRING; 243090.RB10459; -.
DR EnsemblBacteria; CAD78893; CAD78893; RB10459.
DR KEGG; rba:RB10459; -.
DR PATRIC; fig|243090.15.peg.5056; -.
DR eggNOG; COG1232; Bacteria.
DR HOGENOM; CLU_009629_3_0_0; -.
DR InParanoid; Q7UEZ1; -.
DR OrthoDB; 9805195at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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:UP000001025}.
FT DOMAIN 10..484
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 485 AA; 52855 MW; CD4ED0359E259A26 CRC64;
MNIAIIGGGL SGLSTSVHIR LLAQKQNKPL PNITLFEASD RLGGVIHTET LTDDHGRTFV
IDHGADMFAT APSAAIDLCE QLGVADQLLR PSPLGRGAMI ARGNRLIPIP EGFVLMRPTK
LGSMLTTPLL SLTAKLRLLQ ERFIARRVES VTDESVGSFV RRRLGEECLD NIVAPLVAGI
YTADVDRLSM AATMKPIWDM ETSDGSLAKA TLRRIRTGED STEQASSGAR YEKFRAFPNG
MKQWIDTLAD FTGRENIRLN TAVQSIVPLP DNRYQLNVKS DIDGQSTQEF DQVVVSTPAH
VAATLLQPLS EEAASTLRSI PFASTAIVVM AVRRECISRL PTTFGFVVPP KENRRVLAGS
FASTKFPQRA PDDYVIVRAF VGGVMQPEIL DSSDNEIIDI VRAELGELIG LDQTQSLQDI
TAMVKVVRWN DAMPQYEVGH LDKVQRIRTA LASLEGLHLN TNALGGVGIA PVIAASKRTA
ERILK
//
