ID A0A411PFY1_9GAMM Unreviewed; 173 AA.
AC A0A411PFY1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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 ORFNames=EXU30_06050 {ECO:0000313|EMBL:QBF82312.1};
OS Shewanella maritima.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=2520507 {ECO:0000313|EMBL:QBF82312.1, ECO:0000313|Proteomes:UP000291106};
RN [1] {ECO:0000313|EMBL:QBF82312.1, ECO:0000313|Proteomes:UP000291106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D4-2 {ECO:0000313|EMBL:QBF82312.1,
RC ECO:0000313|Proteomes:UP000291106};
RA Baek K.;
RT "Shewanella sp. D4-2 isolated from Dokdo Island.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
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 membrane {ECO:0000256|HAMAP-Rule:MF_00853};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00853}.
CC -!- SIMILARITY: Belongs to the HemG family. {ECO:0000256|HAMAP-
CC Rule:MF_00853}.
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DR EMBL; CP036200; QBF82312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411PFY1; -.
DR KEGG; smai:EXU30_06050; -.
DR OrthoDB; 9795729at2; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000291106; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 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.
PE 3: Inferred from homology;
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 5..150
FT /note="Flavodoxin"
FT /evidence="ECO:0000259|Pfam:PF12724"
SQ SEQUENCE 173 AA; 19675 MW; 76EEFB035E3C58C1 CRC64;
MSQILLIHSS VHGQTVKICK YMQQKAQEQG VNITLASLAD NPSIEGFDKV FIGASIRHGK
HRPALYQFIE ANKAKLEQIP SGFFSVSLVA RKPGKNTPET NMYMQAFLKQ SVWQPKHLQV
FGGNLDYQFY GPVDRNIIRF IMWITKGPTD PHTKVEYTDW DKVDAFVDTM INA
//
