HEMG_ECOLI
ID HEMG_ECOLI Reviewed; 181 AA.
AC P0ACB4; P27863; Q2M8F3;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
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, ECO:0000269|PubMed:19583219, ECO:0000269|PubMed:20484676};
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, ECO:0000303|PubMed:7916647};
DE Short=PPO {ECO:0000255|HAMAP-Rule:MF_00853, ECO:0000303|PubMed:7916647};
GN Name=hemG {ECO:0000255|HAMAP-Rule:MF_00853, ECO:0000303|PubMed:390093};
GN Synonyms=yihB; OrderedLocusNames=b3850, JW3827;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2243799; DOI=10.1093/nar/18.21.6439;
RA Nakahigashi K., Inokuchi H.;
RT "Nucleotide sequence between the fadB gene and the rrnA operon from
RT Escherichia coli.";
RL Nucleic Acids Res. 18:6439-6439(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18,
RP CHARACTERIZATION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / SASX38;
RX PubMed=7916647; DOI=10.1139/m93-174;
RA Sasarman A., Letowski J., Czaika G., Ramirez V., Nead M.A., Jacobs J.M.,
RA Morais R.;
RT "Nucleotide sequence of the hemG gene involved in the protoporphyrinogen
RT oxidase activity of Escherichia coli K12.";
RL Can. J. Microbiol. 39:1155-1161(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=7788523; DOI=10.1093/dnares/2.1.1;
RA Nishimura K., Nakahigashi K., Inokuchi H.;
RT "Cloning and identification of the hemG gene encoding protoporphyrinogen
RT oxidase (PPO) of Escherichia coli K-12.";
RL DNA Res. 2:1-8(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / SASX38;
RX PubMed=390093; DOI=10.1099/00221287-113-2-297;
RA Sasarman A., Chartrand P., Lavoie M., Tardif D., Proschek R., Lapointe C.;
RT "Mapping of a new hem gene in Escherichia coli K12.";
RL J. Gen. Microbiol. 113:297-303(1979).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, POSSIBLE COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / SASX38;
RX PubMed=19583219; DOI=10.1021/bi900850y;
RA Boynton T.O., Daugherty L.E., Dailey T.A., Dailey H.A.;
RT "Identification of Escherichia coli HemG as a novel, menadione-dependent
RT flavodoxin with protoporphyrinogen oxidase activity.";
RL Biochemistry 48:6705-6711(2009).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=20484676; DOI=10.1073/pnas.1000956107;
RA Moebius K., Arias-Cartin R., Breckau D., Haennig A.L., Riedmann K.,
RA Biedendieck R., Schroeder S., Becher D., Magalon A., Moser J., Jahn M.,
RA Jahn D.;
RT "Heme biosynthesis is coupled to electron transport chains for energy
RT generation.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10436-10441(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 condition uses ubiquinone as an
CC electron acceptor. {ECO:0000255|HAMAP-Rule:MF_00853}.
CC -!- FUNCTION: Anaerobically in vitro transfers electrons to fumarate
CC reductase and nitrate reductase; transfer to nitrate reductase couples
CC this reaction to electron transfer across the cell inner membrane and
CC thus ATP synthesis (PubMed:19583219, PubMed:20484676). Neither
CC mesoporphyrinogen nor coproporphyrinogen are substrates
CC (PubMed:19583219). Under aerobic conditions in vitro forms
CC protoporphyrin IX using ubiquinone as an electron acceptor, is able to
CC transfer electrons to cytochrome bd oxidase and cytochrome bo oxidase;
CC transfer to these oxidases couples this reaction to electron transfer
CC across the cell inner membrane and thus ATP synthesis. In cell free
CC extracts deletion of both cytochrome oxidases prevents formation of
CC protoporphyrin IX (PubMed:20484676). {ECO:0000269|PubMed:19583219,
CC ECO:0000269|PubMed:20484676}.
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 ECO:0000269|PubMed:19583219, ECO:0000269|PubMed:20484676};
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, ECO:0000269|PubMed:20484676};
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 ECO:0000269|PubMed:20484676};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00853,
CC ECO:0000269|PubMed:20484676, ECO:0000305|PubMed:19583219};
CC Note=Binds 1 FMN non-covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00853, ECO:0000269|PubMed:20484676};
CC -!- ACTIVITY REGULATION: Anaerobic activity is inhibited by
CC pentachlorophenol. {ECO:0000269|PubMed:20484676}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.0 uM for protoporphyrinogen IX {ECO:0000269|PubMed:19583219};
CC KM=3.76 uM for menadione (a soluble menaquinone analog)
CC {ECO:0000269|PubMed:19583219};
CC KM=17.3 uM for menaquinone {ECO:0000269|PubMed:20484676};
CC Vmax=960 umol/h/mg enzyme {ECO:0000269|PubMed:20484676};
CC Note=kcat for protoporphyrinogen IX is 17.52 min(-1) and for
CC menadione is 16.86 min(-1). {ECO:0000269|PubMed:19583219};
CC Redox potential:
CC E(0) are -241 mV and -412 for the first and second reduction steps of
CC HemG respectively. {ECO:0000269|PubMed:19583219};
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, ECO:0000305|PubMed:19583219,
CC ECO:0000305|PubMed:7916647}.
CC -!- SUBUNIT: Homotetramer (Probable). Homohexamer. Purified from membrane
CC fractions associated with fumarate reductase (subunit FrdA)
CC (PubMed:20484676). {ECO:0000269|PubMed:20484676,
CC ECO:0000305|PubMed:19583219}.
CC -!- INTERACTION:
CC P0ACB4; P00363: frdA; NbExp=2; IntAct=EBI-1115706, EBI-550480;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00853, ECO:0000305|PubMed:20484676}; Peripheral membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00853, ECO:0000305|PubMed:20484676}.
CC -!- DISRUPTION PHENOTYPE: Loss of protoporphyrinogen IX dehydrogenase
CC activity, grows very slowly unless supplemented with heme
CC (PubMed:390093, PubMed:7916647, PubMed:19583219). Accumulates
CC intermediates of heme synthesis such as uroporphyrinogen III,
CC coproprophyrin III and protoporphyrinogen IX (PubMed:390093,
CC PubMed:7788523). {ECO:0000269|PubMed:19583219,
CC ECO:0000269|PubMed:390093, ECO:0000269|PubMed:7788523,
CC ECO:0000269|PubMed:7916647}.
CC -!- SIMILARITY: Belongs to the HemG family. {ECO:0000255|HAMAP-
CC Rule:MF_00853}.
CC -!- SEQUENCE CAUTION:
CC Sequence=X54687; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X54687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X68660; CAA48626.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67647.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76853.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77453.1; -; Genomic_DNA.
DR PIR; JC2513; JC2513.
DR RefSeq; NP_418292.1; NC_000913.3.
DR RefSeq; WP_000853959.1; NZ_STEB01000021.1.
DR AlphaFoldDB; P0ACB4; -.
DR SMR; P0ACB4; -.
DR BioGRID; 4262620; 2.
DR DIP; DIP-35890N; -.
DR IntAct; P0ACB4; 19.
DR STRING; 511145.b3850; -.
DR jPOST; P0ACB4; -.
DR PaxDb; P0ACB4; -.
DR PRIDE; P0ACB4; -.
DR EnsemblBacteria; AAC76853; AAC76853; b3850.
DR EnsemblBacteria; BAE77453; BAE77453; BAE77453.
DR GeneID; 58462188; -.
DR GeneID; 948331; -.
DR KEGG; ecj:JW3827; -.
DR KEGG; eco:b3850; -.
DR PATRIC; fig|1411691.4.peg.2860; -.
DR EchoBASE; EB1448; -.
DR eggNOG; COG4635; Bacteria.
DR HOGENOM; CLU_094839_0_1_6; -.
DR InParanoid; P0ACB4; -.
DR OMA; IEYTDWE; -.
DR PhylomeDB; P0ACB4; -.
DR BioCyc; EcoCyc:PROTOPORGENOXI-MON; -.
DR BioCyc; MetaCyc:PROTOPORGENOXI-MON; -.
DR SABIO-RK; P0ACB4; -.
DR UniPathway; UPA00251; UER00324.
DR PRO; PR:P0ACB4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
DR GO; GO:0070819; F:menaquinone-dependent protoporphyrinogen oxidase activity; IDA:EcoCyc.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0006785; P:heme B biosynthetic process; IMP:EcoCyc.
DR GO; GO:0006783; P:heme biosynthetic process; IMP:EcoCyc.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP:EcoliWiki.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Flavoprotein; FMN; Membrane; Nucleotide-binding; Oxidoreductase;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..181
FT /note="Protoporphyrinogen IX dehydrogenase [quinone]"
FT /id="PRO_0000135259"
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; 21226 MW; BCCB5AE594010026 CRC64;
MKTLILFSTR DGQTREIASY LASELKELGI QADVANVHRI EEPQWENYDR VVIGASIRYG
HYHSAFQEFV KKHATRLNSM PSAFYSVNLV ARKPEKRTPQ TNSYARKFLM NSQWRPDRCA
VIAGALRYPR YRWYDRFMIK LIMKMSGGET DTRKEVVYTD WEQVANFARE IAHLTDKPTL
K
