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Database: UniProt
Entry: S3JGK3_9ENTR
LinkDB: S3JGK3_9ENTR
Original site: S3JGK3_9ENTR 
ID   S3JGK3_9ENTR            Unreviewed;       177 AA.
AC   S3JGK3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=HMPREF0201_04886 {ECO:0000313|EMBL:EPF12294.1};
OS   Cedecea davisae DSM 4568.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cedecea.
OX   NCBI_TaxID=566551 {ECO:0000313|EMBL:EPF12294.1, ECO:0000313|Proteomes:UP000014585};
RN   [1] {ECO:0000313|EMBL:EPF12294.1, ECO:0000313|Proteomes:UP000014585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4568 {ECO:0000313|EMBL:EPF12294.1,
RC   ECO:0000313|Proteomes:UP000014585};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Palsikar V.B., Zhang X., Suruliraj S., Perna N.T., Plunkett G.,
RA   Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2013) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPF12294.1}.
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DR   EMBL; ATDT01000042; EPF12294.1; -; Genomic_DNA.
DR   RefSeq; WP_016539031.1; NZ_KE161030.1.
DR   AlphaFoldDB; S3JGK3; -.
DR   STRING; 566551.HMPREF0201_04886; -.
DR   PATRIC; fig|566551.4.peg.4468; -.
DR   HOGENOM; CLU_094839_0_1_6; -.
DR   OrthoDB; 9795729at2; -.
DR   UniPathway; UPA00251; UER00324.
DR   Proteomes; UP000014585; Unassembled WGS sequence.
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 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..177
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   177 AA;  20619 MW;  806FD7D514DA71A0 CRC64;
     MKTLILFSTR DGQTREIASY IASELKELGV DSDVVNLHRC DDIAWANYDR VVIGASIRYG
     HFHSSVDSFV KKYQQQLNQR ASAFFSVNLV ARKPEKRSPQ TNSYTRKFLL NSVWRPDHCA
     VFAGALRYPR YGWLDRFMIR LIMKMTDGET DTSKEVVYTD WQQVARFAHE IEQLNTK
//
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