ID A0A090IHW3_9GAMM Unreviewed; 171 AA.
AC A0A090IHW3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
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:CED62280.1};
GN ORFNames=MVIS_4403 {ECO:0000313|EMBL:CED62280.1};
OS Moritella viscosa.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Moritellaceae; Moritella.
OX NCBI_TaxID=80854 {ECO:0000313|EMBL:CED62280.1, ECO:0000313|Proteomes:UP000032438};
RN [1] {ECO:0000313|Proteomes:UP000032438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hjerde E.;
RL Submitted (SEP-2014) 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}.
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; LN554852; CED62280.1; -; Genomic_DNA.
DR RefSeq; WP_045112312.1; NZ_FRDW01000051.1.
DR AlphaFoldDB; A0A090IHW3; -.
DR STRING; 80854.MVIS_4403; -.
DR GeneID; 61296380; -.
DR KEGG; mvs:MVIS_4403; -.
DR PATRIC; fig|80854.5.peg.4665; -.
DR HOGENOM; CLU_094839_0_1_6; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000032438; Chromosome complete sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000032438}.
FT DOMAIN 5..152
FT /note="Flavodoxin"
FT /evidence="ECO:0000259|Pfam:PF12724"
SQ SEQUENCE 171 AA; 19629 MW; 680C14ACA21F1DA4 CRC64;
MKKMLVLYST VDGQTLKIIK AIEESIADKY HCEVMSLEEC QHLDMAIFDK VVIGGSVRYG
HLNKKLYQFV AAHKEELEVK ENSFFCVNLT ARKAEKNTPE TNAYMQAFLE KSNWVPKQQA
VFAGALLYSK YNWWQTLIIQ LIMKITGGST DTTKDIEFTD WAKVKSFAKT L
//
