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Database: UniProt
Entry: A0A0B7H549_9FLAO
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ID   A0A0B7H549_9FLAO        Unreviewed;       174 AA.
AC   A0A0B7H549;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=CCYN2B_140027 {ECO:0000313|EMBL:CEN33072.1};
OS   Capnocytophaga cynodegmi.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=28189 {ECO:0000313|EMBL:CEN33072.1, ECO:0000313|Proteomes:UP000038055};
RN   [1] {ECO:0000313|Proteomes:UP000038055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ccyn2B {ECO:0000313|Proteomes:UP000038055};
RA   MANFREDI Pablo;
RL   Submitted (JAN-2015) 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; CDOD01000006; CEN33072.1; -; Genomic_DNA.
DR   RefSeq; WP_041990572.1; NZ_CDOD01000006.1.
DR   AlphaFoldDB; A0A0B7H549; -.
DR   STRING; 28189.CCYN74_210055; -.
DR   eggNOG; COG4635; Bacteria.
DR   UniPathway; UPA00251; UER00324.
DR   Proteomes; UP000038055; Unassembled WGS 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:UP000038055}.
FT   DOMAIN          5..152
FT                   /note="Flavodoxin"
FT                   /evidence="ECO:0000259|Pfam:PF12724"
SQ   SEQUENCE   174 AA;  20038 MW;  F286A057A6DBBA3A CRC64;
     MEKSVIIYAS VDGQTKKICD HINGVLLSKK QDVKLVSIAD FRDNLKDFDK IILASSIRYG
     KHNQDIINLI NQNYELLNAK KSAFISVNLV ARKEEKRQAH TNPYVVKFLD KIKWKPTVVE
     VFAGKINYKI YGFFDKLIIK LIMVITKGPT NSDTEIEYTN WDNVTAFAEK FSEM
//
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