HEMJ_CERS4
ID HEMJ_CERS4 Reviewed; 165 AA.
AC Q53229; Q3IYH1; Q53230; Q53231;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protoporphyrinogen IX oxidase {ECO:0000250|UniProtKB:P72793};
DE Short=PPO {ECO:0000250|UniProtKB:P72793};
DE EC=1.3.99.- {ECO:0000250|UniProtKB:P72793};
DE AltName: Full=ORF1;
GN OrderedLocusNames=RHOS4_28450; ORFNames=RSP_1232;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8606169; DOI=10.1128/jb.178.7.1946-1954.1996;
RA Gomelsky M., Kaplan S.;
RT "The Rhodobacter sphaeroides 2.4.1 rho gene: expression and genetic
RT analysis of structure and function.";
RL J. Bacteriol. 178:1946-1954(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000250|UniProtKB:P72793}.
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:0000250|UniProtKB:P72793};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P72793};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000250|UniProtKB:P72793};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC {ECO:0000250|UniProtKB:P72793}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P72793}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P72793};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the HemJ family. {ECO:0000255|HAMAP-
CC Rule:MF_02239, ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1, Met-3 or Met-12 is the
CC initiator. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB02032.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAB02033.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L76097; AAB02031.1; -; Genomic_DNA.
DR EMBL; L76097; AAB02032.1; ALT_INIT; Genomic_DNA.
DR EMBL; L76097; AAB02033.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000143; ABA80413.1; -; Genomic_DNA.
DR PIR; JC6036; JC6036.
DR RefSeq; WP_043764028.1; NZ_CP030271.1.
DR RefSeq; YP_354314.2; NC_007493.2.
DR AlphaFoldDB; Q53229; -.
DR STRING; 272943.RSP_1232; -.
DR EnsemblBacteria; ABA80413; ABA80413; RSP_1232.
DR KEGG; rsp:RSP_1232; -.
DR PATRIC; fig|272943.9.peg.3213; -.
DR eggNOG; COG1981; Bacteria.
DR PhylomeDB; Q53229; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000002703; Chromosome 1.
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 PIRSF; PIRSF004638; UCP004638; 1.
DR TIGRFAMs; TIGR00701; TIGR00701; 1.
PE 3: Inferred from homology;
KW Cell membrane; Heme; Iron; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..165
FT /note="Protoporphyrinogen IX oxidase"
FT /id="PRO_0000217660"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
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:0000250|UniProtKB:P72793"
FT BINDING 105
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:0000250|UniProtKB:P72793"
SQ SEQUENCE 165 AA; 19196 MW; 2474FCFCDCC2CEC8 CRC64;
MRMADHFEET TMGTFLADYY LWTKSLHVIS VLAWMAGLFY LPRLFVYHAE VVKAGTETDA
LFQTMERRLL RAIMNPAMIA TWIFGLLLVF TPGIVDWSML WPWTKAACVL AMTGFHMWLA
ARRRDFAAGA NRHKGRTYRM MNELPTLLML VIVFSAVAKW NYWGF
