HEMG_ECOL6
ID HEMG_ECOL6 Reviewed; 181 AA.
AC P0ACB5; P27863;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Protoporphyrinogen IX dehydrogenase [quinone] {ECO:0000255|HAMAP-Rule:MF_00853};
DE EC=1.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00853};
DE AltName: Full=Protoporphyrinogen IX dehydrogenase [menaquinone] {ECO:0000255|HAMAP-Rule:MF_00853};
DE AltName: Full=Protoporphyrinogen IX dehydrogenase [ubiquinone] {ECO:0000255|HAMAP-Rule:MF_00853};
DE AltName: Full=Protoporphyrinogen oxidase {ECO:0000255|HAMAP-Rule:MF_00853};
DE Short=PPO {ECO:0000255|HAMAP-Rule:MF_00853};
GN Name=hemG {ECO:0000255|HAMAP-Rule:MF_00853}; OrderedLocusNames=c4797;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen IX
CC to form protoporphyrin IX; under anaerobic conditions uses menaquinone
CC as an electron acceptor, under aerobic condition uses ubiquinone as an
CC electron acceptor. {ECO:0000255|HAMAP-Rule:MF_00853}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 a menaquinone + protoporphyrinogen IX = 3 a menaquinol +
CC protoporphyrin IX; Xref=Rhea:RHEA:27409, Rhea:RHEA-COMP:9537,
CC Rhea:RHEA-COMP:9539, ChEBI:CHEBI:16374, ChEBI:CHEBI:18151,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:57307; EC=1.3.5.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00853};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 a ubiquinone + protoporphyrinogen IX = 3 a ubiquinol +
CC protoporphyrin IX; Xref=Rhea:RHEA:63936, Rhea:RHEA-COMP:9565,
CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:57307; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00853};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 a quinone + protoporphyrinogen IX = 3 a quinol +
CC protoporphyrin IX; Xref=Rhea:RHEA:65032, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:57307, ChEBI:CHEBI:132124; EC=1.3.5.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00853};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00853};
CC Note=Binds 1 FMN non-covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00853};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00853}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00853}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00853}.
CC -!- SIMILARITY: Belongs to the HemG family. {ECO:0000255|HAMAP-
CC Rule:MF_00853}.
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; AE014075; AAN83230.1; -; Genomic_DNA.
DR RefSeq; WP_000853959.1; NC_004431.1.
DR AlphaFoldDB; P0ACB5; -.
DR SMR; P0ACB5; -.
DR STRING; 199310.c4797; -.
DR EnsemblBacteria; AAN83230; AAN83230; c4797.
DR GeneID; 58462188; -.
DR KEGG; ecc:c4797; -.
DR eggNOG; COG4635; Bacteria.
DR HOGENOM; CLU_094839_0_1_6; -.
DR OMA; IEYTDWE; -.
DR BioCyc; ECOL199310:C4797-MON; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070819; F:menaquinone-dependent protoporphyrinogen oxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.360; -; 1.
DR HAMAP; MF_00853; HemG; 1.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001226; Flavodoxin_CS.
DR InterPro; IPR026816; Flavodoxin_dom.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR044264; HemG.
DR Pfam; PF12724; Flavodoxin_5; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR PROSITE; PS00201; FLAVODOXIN; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Flavoprotein; FMN; Membrane;
KW Nucleotide-binding; Oxidoreductase; Porphyrin biosynthesis.
FT CHAIN 1..181
FT /note="Protoporphyrinogen IX dehydrogenase [quinone]"
FT /id="PRO_0000135261"
FT DOMAIN 3..172
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00853"
FT BINDING 9..13
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00853"
FT BINDING 84..152
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00853"
SQ SEQUENCE 181 AA; 21226 MW; BCCB5AE594010026 CRC64;
MKTLILFSTR DGQTREIASY LASELKELGI QADVANVHRI EEPQWENYDR VVIGASIRYG
HYHSAFQEFV KKHATRLNSM PSAFYSVNLV ARKPEKRTPQ TNSYARKFLM NSQWRPDRCA
VIAGALRYPR YRWYDRFMIK LIMKMSGGET DTRKEVVYTD WEQVANFARE IAHLTDKPTL
K
