(data stored in ACNUC7421 zone)

SWISSPROT: HEM6_PSEU2

ID   HEM6_PSEU2              Reviewed;         304 AA.
AC   Q500S4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 84.
DE   RecName: Full=Oxygen-dependent coproporphyrinogen-III oxidase {ECO:0000255|HAMAP-Rule:MF_00333};
DE            Short=CPO {ECO:0000255|HAMAP-Rule:MF_00333};
DE            Short=Coprogen oxidase {ECO:0000255|HAMAP-Rule:MF_00333};
DE            Short=Coproporphyrinogenase {ECO:0000255|HAMAP-Rule:MF_00333};
DE            EC=1.3.3.3 {ECO:0000255|HAMAP-Rule:MF_00333};
GN   Name=hemF {ECO:0000255|HAMAP-Rule:MF_00333};
GN   OrderedLocusNames=Psyr_0024;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Involved in the heme biosynthesis. Catalyzes the aerobic
CC       oxidative decarboxylation of propionate groups of rings A and B of
CC       coproporphyrinogen-III to yield the vinyl groups in
CC       protoporphyrinogen-IX. {ECO:0000255|HAMAP-Rule:MF_00333}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O +
CC         protoporphyrinogen IX; Xref=Rhea:RHEA:18257, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57307, ChEBI:CHEBI:57309; EC=1.3.3.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00333};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00333};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III
CC       (O2 route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00333}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00333}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00333}.
CC   -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00333}.
DR   EMBL; CP000075; AAY35098.1; -; Genomic_DNA.
DR   RefSeq; WP_003401477.1; NC_007005.1.
DR   RefSeq; YP_233136.1; NC_007005.1.
DR   SMR; Q500S4; -.
DR   STRING; 205918.Psyr_0024; -.
DR   EnsemblBacteria; AAY35098; AAY35098; Psyr_0024.
DR   GeneID; 3365499; -.
DR   KEGG; psb:Psyr_0024; -.
DR   PATRIC; fig|205918.7.peg.24; -.
DR   eggNOG; ENOG4105DBS; Bacteria.
DR   eggNOG; COG0408; LUCA.
DR   HOGENOM; HOG000262768; -.
DR   KO; K00228; -.
DR   OMA; MDLTPYY; -.
DR   BioCyc; PSYR205918:G1G4J-24-MONOMER; -.
DR   UniPathway; UPA00251; UER00322.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.1500.10; -; 1.
DR   HAMAP; MF_00333; Coprogen_oxidas; 1.
DR   InterPro; IPR001260; Coprogen_oxidase_aer.
DR   InterPro; IPR036406; Coprogen_oxidase_aer_sf.
DR   InterPro; IPR018375; Coprogen_oxidase_CS.
DR   PANTHER; PTHR10755; PTHR10755; 1.
DR   Pfam; PF01218; Coprogen_oxidas; 1.
DR   PIRSF; PIRSF000166; Coproporphyri_ox; 1.
DR   PRINTS; PR00073; COPRGNOXDASE.
DR   SUPFAM; SSF102886; SSF102886; 1.
DR   PROSITE; PS01021; COPROGEN_OXIDASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q500S4.
DR   SWISS-2DPAGE; Q500S4.
KW   Complete proteome; Cytoplasm; Heme biosynthesis; Metal-binding;
KW   Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN         1    304       Oxygen-dependent coproporphyrinogen-III
FT                                oxidase.
FT                                /FTId=PRO_1000019490.
FT   REGION      109    111       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   REGION      241    276       Important for dimerization.
FT                                {ECO:0000255|HAMAP-Rule:MF_00333}.
FT   REGION      259    261       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   ACT_SITE    107    107       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   METAL        97     97       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00333}.
FT   METAL       107    107       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00333}.
FT   METAL       146    146       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00333}.
FT   METAL       176    176       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00333}.
FT   BINDING      93     93       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   SITE        176    176       Important for dimerization.
FT                                {ECO:0000255|HAMAP-Rule:MF_00333}.
SQ   SEQUENCE   304 AA;  34594 MW;  956DE6FC23108FE2 CRC64;
     MSTRTEAVKA YLLDLQDRIC TALEQEDGSA HFMEDAWTRP AGGGGRTRVI ENGTVIEKGG
     VNFSHVFGSN LPPSASAHRP ELAGRGFEAL GVSLVIHPHN PHVPTSHANV RFFIAEKEGE
     EAVWWFGGGF DLTPYYGVEE DCVHWHRVAE RACAPFGEDV YPRYKAWCDS YFHLKHRDEP
     RGIGGLFFDD VNQWDFDTSF AFIRAIGDAF INAYLPIVRR RKAAAYTVQQ REFQEFRRGR
     YVEFNLVYDR GTLFGLQSGG RTESILMSLP PQVRWGYDWK AAPGSEEARL TEYFLTDRDW
     LAEN
//

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