GenomeNet

Database: UniProt
Entry: E1SRD7_FERBD
LinkDB: E1SRD7_FERBD
Original site: E1SRD7_FERBD 
ID   E1SRD7_FERBD            Unreviewed;       176 AA.
AC   E1SRD7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 52.
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   OrderedLocusNames=Fbal_1684 {ECO:0000313|EMBL:ADN75888.1};
OS   Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Ferrimonadaceae; Ferrimonas.
OX   NCBI_TaxID=550540 {ECO:0000313|EMBL:ADN75888.1, ECO:0000313|Proteomes:UP000006683};
RN   [1] {ECO:0000313|EMBL:ADN75888.1, ECO:0000313|Proteomes:UP000006683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9799 / CCM 4581 / KCTC 23876 / PAT
RC   {ECO:0000313|Proteomes:UP000006683};
RX   DOI=10.4056/sigs.1161239;
RA   Nolan M., Sikorski J., Davenport K., Lucas S., Glavina Del Rio T., Tice H.,
RA   Cheng J., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y., Jeffries C., Tapia R., Brettin T., Detter J., Han C.,
RA   Yasawong M., Rohde M., Tindall B., Goker M., Woyke T., Bristow J.,
RA   Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Lapidus A.;
RT   "Complete genome sequence of Ferrimonas balearica type strain (PAT).";
RL   Stand. Genomic Sci. 3:174-182(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}.
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; CP002209; ADN75888.1; -; Genomic_DNA.
DR   RefSeq; WP_013345194.1; NC_014541.1.
DR   AlphaFoldDB; E1SRD7; -.
DR   STRING; 550540.Fbal_1684; -.
DR   GeneID; 67181892; -.
DR   KEGG; fbl:Fbal_1684; -.
DR   eggNOG; COG4635; Bacteria.
DR   HOGENOM; CLU_094839_0_1_6; -.
DR   OMA; ADTNIEY; -.
DR   UniPathway; UPA00251; UER00324.
DR   Proteomes; UP000006683; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000006683}.
FT   DOMAIN          5..152
FT                   /note="Flavodoxin"
FT                   /evidence="ECO:0000259|Pfam:PF12724"
SQ   SEQUENCE   176 AA;  20443 MW;  C968D5B0F168494C CRC64;
     MSKTLLIYAS QFGQTHKICQ RIAEHLQSQG ETVEMKPLAE APQSLDGYGK VLLACSIYHG
     KYRPELYQYI TDHQAELDAI PNAFFSVNLV ARKPHKNAPD TNPYVKQFLQ KTPWQPKLLG
     VFGGVIHYQR YNWFDRNIIR FIMWLTKGPT DPNSHIEYTQ WERVDQFATE FAGLRP
//
DBGET integrated database retrieval system