HEMG_LEIMA
ID HEMG_LEIMA Reviewed; 231 AA.
AC Q4QIU7;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Protoporphyrinogen IX dehydrogenase [quinone] {ECO:0000305};
DE EC=1.3.5.3 {ECO:0000269|PubMed:24962471};
DE AltName: Full=Protoporphyrinogen IX dehydrogenase [menaquinone] {ECO:0000305};
DE AltName: Full=Protoporphyrinogen IX dehydrogenase [ubiquinone] {ECO:0000305};
DE AltName: Full=Protoporphyrinogen oxidase {ECO:0000303|PubMed:24962471};
DE Short=PPO {ECO:0000303|PubMed:24962471};
GN Name=hemG {ECO:0000303|PubMed:24962471}; ORFNames=LMJF_06_1280;
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin;
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B.G., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin;
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L1989/05;
RX PubMed=26730948; DOI=10.1371/journal.pntd.0004326;
RA Vikeved E., Backlund A., Alsmark C.;
RT "The Dynamics of Lateral Gene Transfer in Genus Leishmania - A Route for
RT Adaptation and Species Diversification.";
RL PLoS Negl. Trop. Dis. 10:E0004326-E0004326(2016).
RN [4]
RP FUNCTION, EXPRESSION IN E.COLI, COFACTOR, PATHWAY, AND MUTAGENESIS OF
RP TYR-134; TYR-137 AND ARG-142.
RX PubMed=24962471; DOI=10.1042/bsr20140081;
RA Zwerschke D., Karrie S., Jahn D., Jahn M.;
RT "Leishmania major possesses a unique HemG-type protoporphyrinogen IX
RT oxidase.";
RL Biosci. Rep. 34:0-0(2014).
CC -!- FUNCTION: In E.coli extracts under anerobic conditions catalyzes the 6-
CC electron oxidation of protoporphyrinogen IX to form protoporphyrin IX,
CC transferring electrons to fumarate reductase, presumably via
CC menaquinone. In vitro under aerobic conditions forms protoporphyrin IX
CC using ubiquinone as an electron acceptor. Complements an E.coli hemG
CC deletion, allowing normal growth in vivo.
CC {ECO:0000269|PubMed:24962471}.
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:0000305|PubMed:24962471};
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;
CC Evidence={ECO:0000269|PubMed:24962471};
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:0000269|PubMed:24962471};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:24962471};
CC Note=Binds 1 FMN non-covalently per subunit.
CC {ECO:0000269|PubMed:24962471};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC {ECO:0000305|PubMed:24962471}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Leishmania is not able to completely synthesize heme; it
CC is thought that the amastigote form localized in macrophages utilizes
CC coproporphyrinogen from the host to produce heme via the successive
CC action of HemF, HemG and HemH. {ECO:0000305|PubMed:24962471}.
CC -!- SIMILARITY: Belongs to the HemG family. {ECO:0000305}.
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DR EMBL; KM411732; AKK31181.1; -; Genomic_DNA.
DR EMBL; FR796402; CAJ02176.1; -; Genomic_DNA.
DR RefSeq; XP_001680901.1; XM_001680849.1.
DR AlphaFoldDB; Q4QIU7; -.
DR SMR; Q4QIU7; -.
DR STRING; 5664.LmjF.06.1280; -.
DR EnsemblProtists; CAJ02176; CAJ02176; LMJF_06_1280.
DR GeneID; 5649153; -.
DR KEGG; lma:LMJF_06_1280; -.
DR VEuPathDB; TriTrypDB:LmjF.06.1280; -.
DR VEuPathDB; TriTrypDB:LMJLV39_060019700; -.
DR VEuPathDB; TriTrypDB:LMJSD75_060019800; -.
DR eggNOG; ENOG502S4T4; Eukaryota.
DR HOGENOM; CLU_094839_0_0_1; -.
DR InParanoid; Q4QIU7; -.
DR OMA; IEYTDWE; -.
DR BRENDA; 1.3.3.4; 2950.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000000542; Chromosome 6.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0070819; F:menaquinone-dependent protoporphyrinogen oxidase activity; IDA:UniProtKB.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0006783; P:heme biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IDA:UniProtKB.
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 Pfam; PF12724; Flavodoxin_5; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; Membrane; Nucleotide-binding; Oxidoreductase;
KW Porphyrin biosynthesis; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..231
FT /note="Protoporphyrinogen IX dehydrogenase [quinone]"
FT /id="PRO_0000450662"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 8..178
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000250|UniProtKB:P0ACB4"
FT BINDING 14..18
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0ACB4"
FT BINDING 90..158
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0ACB4"
FT MUTAGEN 134
FT /note="Y->F: Greatly reduced formation of protoporphyrin
FT IX."
FT /evidence="ECO:0000269|PubMed:24962471"
FT MUTAGEN 137
FT /note="Y->A,F,S: No formation of protoporphyrin IX."
FT /evidence="ECO:0000269|PubMed:24962471"
FT MUTAGEN 142
FT /note="R->A: Greatly reduced formation of protoporphyrin
FT IX."
FT /evidence="ECO:0000269|PubMed:24962471"
SQ SEQUENCE 231 AA; 25434 MW; 02C7EE3712507B68 CRC64;
MASQSPKCLM LYSTTDGHTK TIMDTIARQL ADETKVRCDV VDIKDGNSYV LADYEKVLLG
ASIRYGHFSA AFINYVKQHH SELSAMPSAF FSVNLTARKL DKNTATTNVY TRKFLNQSSW
SPQLVGVFAG ALWYPRYNFF DRVLIQFIMK VTGGETDSTK EIVYTDWAAV RRFASDFAAL
PLAVPPRPKA NTVEKPDGIL RSGSGAHCLL AIVGMSAAVI VGIRIIAAKR G