HEMJ_SYNY3
ID HEMJ_SYNY3 Reviewed; 210 AA.
AC P72793;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protoporphyrinogen IX oxidase {ECO:0000303|PubMed:20823222, ECO:0000303|PubMed:29925590};
DE Short=PPO {ECO:0000303|PubMed:29925590};
DE Short=Protox {ECO:0000303|PubMed:20823222};
DE EC=1.3.99.- {ECO:0000305|PubMed:29925590};
GN Name=hemJ {ECO:0000303|PubMed:20823222, ECO:0000303|PubMed:29925590};
GN OrderedLocusNames=slr1790;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20823222; DOI=10.1073/pnas.1000771107;
RA Kato K., Tanaka R., Sano S., Tanaka A., Hosaka H.;
RT "Identification of a gene essential for protoporphyrinogen IX oxidase
RT activity in the cyanobacterium Synechocystis sp. PCC6803.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:16649-16654(2010).
RN [3]
RP FUNCTION, COFACTOR, PATHWAY, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION
RP WITH SLL1106, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=29925590; DOI=10.1074/jbc.ra118.003441;
RA Skotnicova P., Sobotka R., Shepherd M., Hajek J., Hrouzek P., Tichy M.;
RT "The cyanobacterial protoporphyrinogen oxidase HemJ is a new b-type heme
RT protein functionally coupled with coproporphyrinogen III oxidase.";
RL J. Biol. Chem. 293:12394-12404(2018).
CC -!- FUNCTION: Catalyzes the oxidation of protoporphyrinogen IX to
CC protoporphyrin IX. Is involved in the biosynthesis of tetrapyrrole
CC molecules like heme and chlorophyll. Does not use oxygen or artificial
CC electron acceptors such as menadione or benzoquinone. Is functionally
CC coupled with coproporphyrinogen III oxidase (CPO) (PubMed:29925590). Is
CC essential for growth (PubMed:20823222). {ECO:0000269|PubMed:20823222,
CC ECO:0000269|PubMed:29925590}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 A + protoporphyrinogen IX = 3 AH2 + protoporphyrin IX;
CC Xref=Rhea:RHEA:62000, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:57307;
CC Evidence={ECO:0000305|PubMed:29925590};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:29925590};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000269|PubMed:29925590};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC {ECO:0000305|PubMed:29925590}.
CC -!- SUBUNIT: Homodimer. Can also form higher oligomers, most probably
CC tetramers. Interacts with Sll1106, however it is unlikely that Sll1106
CC is required for PPO function. {ECO:0000269|PubMed:29925590}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29925590};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Attempts to disrupt this gene in the wild-type
CC background of Synechocystis only allow to obtain heteroplasmic
CC disruptants. These cells accumulate a substantial amount of
CC protoporphyrin IX. {ECO:0000269|PubMed:20823222}.
CC -!- SIMILARITY: Belongs to the HemJ family. {ECO:0000255|HAMAP-
CC Rule:MF_02239, ECO:0000305}.
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DR EMBL; BA000022; BAA16808.1; -; Genomic_DNA.
DR PIR; S74656; S74656.
DR AlphaFoldDB; P72793; -.
DR STRING; 1148.1651881; -.
DR PaxDb; P72793; -.
DR EnsemblBacteria; BAA16808; BAA16808; BAA16808.
DR KEGG; syn:slr1790; -.
DR eggNOG; COG1981; Bacteria.
DR InParanoid; P72793; -.
DR OMA; VRLFIYH; -.
DR PhylomeDB; P72793; -.
DR BioCyc; MetaCyc:MON-17460; -.
DR BRENDA; 1.3.3.4; 382.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070818; F:protoporphyrinogen oxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_02239; HemJ; 1.
DR InterPro; IPR005265; HemJ-like.
DR PANTHER; PTHR40255; PTHR40255; 1.
DR Pfam; PF03653; UPF0093; 1.
DR TIGRFAMs; TIGR00701; TIGR00701; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Heme; Iron; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..210
FT /note="Protoporphyrinogen IX oxidase"
FT /id="PRO_0000217662"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 27
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:29925590"
FT BINDING 108
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:29925590"
SQ SEQUENCE 210 AA; 24064 MW; 137CF30151F75EF2 CRC64;
MPKREYFSLP CPLSTFTMAY YWFKAFHLIG IVVWFAGLFY LVRLFVYHAE ADQEPEPAKT
ILKKQYELME KRLYNIITTP GMVVTVAMAI GLIFTEPEIL KSGWLHIKLT FVALLLLYHF
YCGRVMKKLA QGESQWSGQQ FRALNEAPTI LLVVIVLLAV FKNNLPLDAT TWLIVALVIA
MAASIQLYAK KRRRDQALLT EQQKAASAQN
