ID   E4TLS4_MARTH            Unreviewed;       177 AA.
AC   E4TLS4;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   07-OCT-2020, entry version 47.
DE   RecName: Full=Protoporphyrinogen IX oxidase {ECO:0000256|ARBA:ARBA00017504, ECO:0000256|PIRNR:PIRNR004638};
DE            EC=1.3.99.- {ECO:0000256|PIRNR:PIRNR004638};
DE   Flags: Precursor;
GN   OrderedLocusNames=Ftrac_3379 {ECO:0000313|EMBL:ADR23353.1};
OS   Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408
OS   / VKM B-1430 / H-43) (Microscilla tractuosa) (Flexibacter tractuosus).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Marivirga.
OX   NCBI_TaxID=643867 {ECO:0000313|EMBL:ADR23353.1, ECO:0000313|Proteomes:UP000008720};
RN   [1] {ECO:0000313|Proteomes:UP000008720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 /
RC   H-43 {ECO:0000313|Proteomes:UP000008720};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G.,
RA   Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Schroeder M., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of chromosome of Marivirga tractuosa DSM 4126.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADR23353.1, ECO:0000313|Proteomes:UP000008720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 /
RC   H-43 {ECO:0000313|Proteomes:UP000008720};
RX   PubMed=21677852; DOI=10.4056/sigs.1623941;
RA   Pagani I., Chertkov O., Lapidus A., Lucas S., Del Rio T.G., Tice H.,
RA   Copeland A., Cheng J.F., Nolan M., Saunders E., Pitluck S., Held B.,
RA   Goodwin L., Liolios K., Ovchinikova G., Ivanova N., Mavromatis K., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA   Han C., Tapia R., Ngatchou-Djao O.D., Rohde M., Goker M., Spring S.,
RA   Sikorski J., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Marivirga tractuosa type strain (H-43).";
RL   Stand. Genomic Sci. 4:154-162(2011).
CC   -!- FUNCTION: Catalyzes the oxidation of protoporphyrinogen IX to
CC       protoporphyrin IX. {ECO:0000256|PIRNR:PIRNR004638}.
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:0000256|ARBA:ARBA00001093,
CC         ECO:0000256|PIRNR:PIRNR004638};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|PIRNR:PIRNR004638};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000256|PIRNR:PIRNR004638};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005073, ECO:0000256|PIRNR:PIRNR004638}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the HemJ family. {ECO:0000256|ARBA:ARBA00006501,
CC       ECO:0000256|PIRNR:PIRNR004638}.
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DR   EMBL; CP002349; ADR23353.1; -; Genomic_DNA.
DR   RefSeq; WP_013455495.1; NC_014759.1.
DR   STRING; 643867.Ftrac_3379; -.
DR   EnsemblBacteria; ADR23353; ADR23353; Ftrac_3379.
DR   KEGG; mtt:Ftrac_3379; -.
DR   eggNOG; COG1981; Bacteria.
DR   HOGENOM; CLU_125006_0_0_10; -.
DR   KO; K08973; -.
DR   OMA; VRLFIYH; -.
DR   OrthoDB; 1433260at2; -.
DR   UniPathway; UPA00251; UER00324.
DR   Proteomes; UP000008720; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR005265; HemJ-like.
DR   PANTHER; PTHR40255; PTHR40255; 1.
DR   Pfam; PF03653; UPF0093; 1.
DR   PIRSF; PIRSF004638; UCP004638; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR004638};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR004638};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR004638};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR004638,
KW   ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR004638};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008720};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        87..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   177 AA;  21103 MW;  5ED30076D4C73070 CRC64;
     MYLYLKSLHI IFVVTWFAGL FYIVRLFIYQ TEALQKTEPE KSILHNQLSK MARLLWKVIT
     WPSAIITLIL ASSLLILQPF WLQQPFMHIK LTFVFFLYLY HFSCHYIYKK LQKGEIKYSS
     TQLRIWNEVA TLFLVAVVFL IVLKNELNWI WGTLGFISFG ILLMAAIKIY KALREKR
//