ID E1SKS8_PANVC Unreviewed; 177 AA.
AC E1SKS8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Protoporphyrinogen IX dehydrogenase [quinone] {ECO:0000256|HAMAP-Rule:MF_00853};
DE EC=1.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00853};
DE AltName: Full=Protoporphyrinogen IX dehydrogenase [menaquinone] {ECO:0000256|HAMAP-Rule:MF_00853};
DE AltName: Full=Protoporphyrinogen IX dehydrogenase [ubiquinone] {ECO:0000256|HAMAP-Rule:MF_00853};
DE AltName: Full=Protoporphyrinogen oxidase {ECO:0000256|HAMAP-Rule:MF_00853};
DE Short=PPO {ECO:0000256|HAMAP-Rule:MF_00853};
GN Name=hemG {ECO:0000256|HAMAP-Rule:MF_00853,
GN ECO:0000313|EMBL:ADO11578.1};
GN OrderedLocusNames=Pvag_3446 {ECO:0000313|EMBL:ADO11578.1};
OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO11578.1, ECO:0000313|Proteomes:UP000006631};
RN [1] {ECO:0000313|EMBL:ADO11578.1, ECO:0000313|Proteomes:UP000006631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1 {ECO:0000313|EMBL:ADO11578.1,
RC ECO:0000313|Proteomes:UP000006631};
RX PubMed=20952567; DOI=10.1128/JB.01122-10;
RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA Stockwell V.O., Frey J.E., Duffy B.;
RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL J. Bacteriol. 192:6486-6487(2010).
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 conditions uses ubiquinone as an
CC electron acceptor. {ECO:0000256|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:0000256|HAMAP-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:0000256|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:0000256|HAMAP-
CC Rule:MF_00853};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00853};
CC Note=Binds 1 FMN non-covalently per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00853}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00853}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00853}.
CC -!- SIMILARITY: Belongs to the HemG family. {ECO:0000256|HAMAP-
CC Rule:MF_00853}.
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DR EMBL; CP002206; ADO11578.1; -; Genomic_DNA.
DR RefSeq; WP_013359725.1; NC_014562.1.
DR AlphaFoldDB; E1SKS8; -.
DR KEGG; pva:Pvag_3446; -.
DR eggNOG; COG4635; Bacteria.
DR HOGENOM; CLU_094839_0_1_6; -.
DR OrthoDB; 9795729at2; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000006631; 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 PANTHER; PTHR38030; PROTOPORPHYRINOGEN IX DEHYDROGENASE [MENAQUINONE]; 1.
DR PANTHER; PTHR38030:SF2; PROTOPORPHYRINOGEN IX DEHYDROGENASE [QUINONE]; 1.
DR Pfam; PF12724; Flavodoxin_5; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR PROSITE; PS00201; FLAVODOXIN; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00853};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00853};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00853};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_00853};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00853};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00853};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00853};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW Rule:MF_00853}.
FT DOMAIN 3..171
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 177 AA; 20456 MW; AB9E8FDC4530352C CRC64;
MKALILYSTR DGQTKKIASS IAEVIRQQQP CDVLDIQDAT LPDWAQYDRV LIGASIRYGH
FQPVVDKFVK QHLKELQQRT SGFFSVNLTA RKPEKRSPET NAYTQKFLTS SPWQPDCCAV
FAGALYYPRY RWFDRVMIQL IMRMTGGETD STKEVEYTDW QQVRTFANDF AQLPGKS
//
