HEMG_SALTY
ID HEMG_SALTY Reviewed; 181 AA.
AC Q9L6L1;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protoporphyrinogen IX dehydrogenase [quinone] {ECO:0000255|HAMAP-Rule:MF_00853};
DE EC=1.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00853};
DE AltName: Full=Protoporphyrinogen IX dehydrogenase [menaquinone] {ECO:0000255|HAMAP-Rule:MF_00853};
DE AltName: Full=Protoporphyrinogen IX dehydrogenase [ubiquinone] {ECO:0000255|HAMAP-Rule:MF_00853};
DE AltName: Full=Protoporphyrinogen oxidase {ECO:0000255|HAMAP-Rule:MF_00853};
DE Short=PPO {ECO:0000255|HAMAP-Rule:MF_00853};
GN Name=hemG {ECO:0000255|HAMAP-Rule:MF_00853}; OrderedLocusNames=STM3987;
GN ORFNames=STMD1.2;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 condition uses ubiquinone as an
CC electron acceptor. {ECO:0000255|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:0000255|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:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_00853};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00853};
CC Note=Binds 1 FMN non-covalently per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00853}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00853}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00853}.
CC -!- SIMILARITY: Belongs to the HemG family. {ECO:0000255|HAMAP-
CC Rule:MF_00853}.
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DR EMBL; AF233324; AAF33406.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22831.1; -; Genomic_DNA.
DR RefSeq; NP_462872.1; NC_003197.2.
DR RefSeq; WP_000853952.1; NC_003197.2.
DR AlphaFoldDB; Q9L6L1; -.
DR SMR; Q9L6L1; -.
DR STRING; 99287.STM3987; -.
DR PaxDb; Q9L6L1; -.
DR EnsemblBacteria; AAL22831; AAL22831; STM3987.
DR GeneID; 1255513; -.
DR KEGG; stm:STM3987; -.
DR PATRIC; fig|99287.12.peg.4206; -.
DR HOGENOM; CLU_094839_0_1_6; -.
DR OMA; IEYTDWE; -.
DR PhylomeDB; Q9L6L1; -.
DR BioCyc; SENT99287:STM3987-MON; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000001014; Chromosome.
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; IBA:GO_Central.
DR GO; GO:0070819; F:menaquinone-dependent protoporphyrinogen oxidase activity; IBA:GO_Central.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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 Pfam; PF12724; Flavodoxin_5; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR PROSITE; PS00201; FLAVODOXIN; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Flavoprotein; FMN; Membrane;
KW Nucleotide-binding; Oxidoreductase; Porphyrin biosynthesis;
KW Reference proteome.
FT CHAIN 1..181
FT /note="Protoporphyrinogen IX dehydrogenase [quinone]"
FT /id="PRO_0000135262"
FT DOMAIN 3..172
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00853"
FT BINDING 9..13
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00853"
FT BINDING 84..152
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00853"
SQ SEQUENCE 181 AA; 21006 MW; 610191FC0A183733 CRC64;
MKTLILFSTR DGQTREIASY LASELKDMGI WADVVNLHRA EEPDWDSYDR VVIGASIRYG
HYHSAFQEFV KKYATRLNGM PSAFYSVNLV ARKAEKRTPQ TNSYARKFLM SSPWRPDYCA
VIAGALRYPR YRWYDRLMIK LIMKMSGGET DTSKEVVYTD WEQVAHFARE IAHLTNKSSA
K
