CGOX_STAA8
ID CGOX_STAA8 Reviewed; 466 AA.
AC Q2FXA5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Coproporphyrinogen III oxidase {ECO:0000303|PubMed:25908396};
DE EC=1.3.3.15 {ECO:0000269|PubMed:25908396};
DE AltName: Full=Coproporphyrin III synthase {ECO:0000303|PubMed:25908396};
GN Name=cgoX {ECO:0000250|UniProtKB:P32397};
GN Synonyms=hemY {ECO:0000303|PubMed:25908396};
GN OrderedLocusNames=SAOUHSC_01960 {ECO:0000312|EMBL:ABD31021.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=NCTC 8325 / PS 47;
RX PubMed=25908396; DOI=10.1111/mmi.13041;
RA Lobo S.A., Scott A., Videira M.A., Winpenny D., Gardner M., Palmer M.J.,
RA Schroeder S., Lawrence A.D., Parkinson T., Warren M.J., Saraiva L.M.;
RT "Staphylococcus aureus haem biosynthesis: characterisation of the enzymes
RT involved in final steps of the pathway.";
RL Mol. Microbiol. 97:472-487(2015).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=27597779; DOI=10.1042/bcj20160696;
RA Hobbs C., Dailey H.A., Shepherd M.;
RT "The HemQ coprohaem decarboxylase generates reactive oxygen species:
RT implications for the evolution of classical haem biosynthesis.";
RL Biochem. J. 473:3997-4009(2016).
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis
CC (PubMed:25908396). Catalyzes the oxidation of coproporphyrinogen III to
CC coproporphyrin III (PubMed:25908396, PubMed:27597779). Can also oxidize
CC protoporphyrinogen IX (PubMed:27597779). {ECO:0000269|PubMed:25908396,
CC ECO:0000269|PubMed:27597779}.
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:0000269|PubMed:25908396, ECO:0000269|PubMed:27597779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43437;
CC Evidence={ECO:0000269|PubMed:25908396, ECO:0000269|PubMed:27597779};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:25908396};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P32397};
CC -!- ACTIVITY REGULATION: The generation of protoporphyrin IX, but not
CC coproporphyrin III, is stimulated by heme-bound HemQ. This stimulatory
CC effect is mediated by superoxide (PubMed:27597779). Inhibited by
CC acifluorfen analogs (PubMed:25908396). {ECO:0000269|PubMed:25908396,
CC ECO:0000269|PubMed:27597779}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.31 uM for coproporphyrinogen III {ECO:0000269|PubMed:25908396};
CC KM=6.7 uM for coproporphyrinogen III {ECO:0000269|PubMed:27597779};
CC Note=kcat is 1.33 min(-1) with coproporphyrinogen III as substrate
CC (PubMed:25908396). kcat is 0.46 min(-1) with coproporphyrinogen III
CC as substrate (PubMed:27597779). kcat is 0.44 min(-1) with
CC protoporphyrinogen IX as substrate (PubMed:27597779).
CC {ECO:0000269|PubMed:25908396, ECO:0000269|PubMed:27597779};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000269|PubMed:25908396}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Coproporphyrinogen III oxidase subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000253; ABD31021.1; -; Genomic_DNA.
DR RefSeq; WP_000167538.1; NZ_LS483365.1.
DR RefSeq; YP_500459.1; NC_007795.1.
DR AlphaFoldDB; Q2FXA5; -.
DR SMR; Q2FXA5; -.
DR STRING; 1280.SAXN108_1861; -.
DR EnsemblBacteria; ABD31021; ABD31021; SAOUHSC_01960.
DR GeneID; 3920905; -.
DR KEGG; sao:SAOUHSC_01960; -.
DR PATRIC; fig|93061.5.peg.1785; -.
DR eggNOG; COG1232; Bacteria.
DR HOGENOM; CLU_009629_3_0_9; -.
DR OMA; WFDQWFG; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000008816; 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:InterPro.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00562; proto_IX_ox; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; Heme biosynthesis; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..466
FT /note="Coproporphyrinogen III oxidase"
FT /id="PRO_0000450281"
FT BINDING 9..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
FT BINDING 34..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
FT BINDING 42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
FT BINDING 56..59
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
FT BINDING 254
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P56601"
FT BINDING 446..448
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
SQ SEQUENCE 466 AA; 51983 MW; F732B045F34C4B79 CRC64;
MTKSVAIIGA GITGLSSAYF LKQQDPNIDV TIFEASNRPG GKIQSYRKDG YMIELGPESY
LGRKTIMTEL AKDIGLEQDI VTNTTGQSYI FAKNKLYPIP GGSIMGIPTD IKPFVTTKLI
SPLGKLRAGF DLLKKPTQMQ DGDISVGAFF RARLGNEVLE NLIEPLMGGI YGTDIDKLSL
MSTFPNFKEK EEAFGSLIKG MKDEKNKRLK QRQLYPGAPK GQFKQFKHGL SSFIEALEQD
VKNKGVTIRY NTSVDDIITS QKQYKIVYND QLEEVYDGVL VTTPHQVFLN WFGQDPAFDY
FKTMDSTTVA TVVLAFDEKD IENTHDGTGF VIARTSDTDI TACTWTSKKW PFTTPEGKVL
IRAYVGKPGD TVVDDHTDNE LVSIVRRDLS QMMTFKGDPE FTIVNRLPKS MPQYHVGHIQ
QIRQIQAHIK QTYPRLRVTG ASFEAVGLPD CITQGKVAAE EVIAEL
