ID Q2JVE9_SYNJA Unreviewed; 485 AA.
AC Q2JVE9;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
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:ABC99290.1};
GN OrderedLocusNames=CYA_1101 {ECO:0000313|EMBL:ABC99290.1};
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=321327 {ECO:0000313|EMBL:ABC99290.1, ECO:0000313|Proteomes:UP000008818};
RN [1] {ECO:0000313|EMBL:ABC99290.1, ECO:0000313|Proteomes:UP000008818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab {ECO:0000313|EMBL:ABC99290.1,
RC ECO:0000313|Proteomes:UP000008818};
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000239; ABC99290.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2JVE9; -.
DR SMR; Q2JVE9; -.
DR STRING; 321327.CYA_1101; -.
DR KEGG; cya:CYA_1101; -.
DR eggNOG; COG1232; Bacteria.
DR HOGENOM; CLU_009629_3_0_3; -.
DR OrthoDB; 25353at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000008818; 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:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
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:SF40; PROTOPORPHYRINOGEN OXIDASE 1, CHLOROPLASTIC; 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:ABC99290.1}.
FT DOMAIN 20..482
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 485 AA; 52201 MW; 12AE6753E8907244 CRC64;
MNPATPEPLN AEVVVIGAGI SGLTLAWRLQ QGLSARGGSP QAVLLAEASS RVGGCISTQS
KDGYRWEEGP NSFTPTPALL NLIAEVGLTD QLVLADAKLP RYIYWEGALL PVPLSPAAAL
GSRLLSVGGK LRALQGLLGF VPPPPGHEET VRQFFRRQLG SEVAERLVEP FTSGVYAGDP
DQLSAVAAFP RVAGLEERYG SLFAGALQAL RQRPQPSPAA IQPPPKRGQL GNLRQGLQQL
PEALAQKLGD SLRLGWRALQ LKRAGELYWV GFETPEGSRW VAARQVVLAL PAYEAAALLQ
ELNPPASQLL AEILYPPVAV VALAYPQEAL PQPLRGFGHL IPRSQGLRTL GTIWASCLFP
ERAPQGYHSF LSFLGGATDA ALARRRGIPP IPALSPEERA QIAHAELSQV LLTRRAEPVY
LGERLWPRAI PQYTLGHRQR IAQVQAHLAS QTPGIWVCAN YLDGVALGDC VRRAEALAQQ
LLSQV
//
