(data stored in SCRATCH zone)

SWISSPROT: Q3IDI8_PSEHT

ID   Q3IDI8_PSEHT            Unreviewed;       324 AA.
AC   Q3IDI8;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 100.
DE   RecName: Full=Oxygen-dependent coproporphyrinogen-III oxidase {ECO:0000256|HAMAP-Rule:MF_00333};
DE            Short=CPO {ECO:0000256|HAMAP-Rule:MF_00333};
DE            Short=Coprogen oxidase {ECO:0000256|HAMAP-Rule:MF_00333};
DE            Short=Coproporphyrinogenase {ECO:0000256|HAMAP-Rule:MF_00333};
DE            EC=1.3.3.3 {ECO:0000256|HAMAP-Rule:MF_00333};
GN   Name=hemF {ECO:0000256|HAMAP-Rule:MF_00333,
GN   ECO:0000313|EMBL:CAI85143.1};
GN   OrderedLocusNames=PSHAa0029 {ECO:0000313|EMBL:CAI85143.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85143.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85143.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(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:0000256|HAMAP-Rule:MF_00333}.
CC   -!- CATALYTIC ACTIVITY: Coproporphyrinogen-III + O(2) + 2 H(+) =
CC       protoporphyrinogen-IX + 2 CO(2) + 2 H(2)O. {ECO:0000256|HAMAP-
CC       Rule:MF_00333, ECO:0000256|SAAS:SAAS00658031}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00333,
CC       ECO:0000256|SAAS:SAAS00658025}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00333,
CC       ECO:0000256|SAAS:SAAS00658015}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00333}.
CC   -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00333,
CC       ECO:0000256|SAAS:SAAS00658014}.
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DR   EMBL; CR954246; CAI85143.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q3IDI8; -.
DR   STRING; 326442.PSHAa0029; -.
DR   EnsemblBacteria; CAI85143; CAI85143; PSHAa0029.
DR   KEGG; pha:PSHAa0029; -.
DR   eggNOG; ENOG4105DBS; Bacteria.
DR   eggNOG; COG0408; LUCA.
DR   HOGENOM; HOG000262768; -.
DR   KO; K00228; -.
DR   OMA; MDLTPYY; -.
DR   OrthoDB; POG091H03H2; -.
DR   UniPathway; UPA00251; UER00322.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-HAMAP.
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; 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; Q3IDI8.
DR   SWISS-2DPAGE; Q3IDI8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00333};
KW   Heme biosynthesis {ECO:0000256|HAMAP-Rule:MF_00333,
KW   ECO:0000256|SAAS:SAAS00637192};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00333};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00333,
KW   ECO:0000256|SAAS:SAAS00658016, ECO:0000313|EMBL:CAI85143.1};
KW   Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00333,
KW   ECO:0000256|SAAS:SAAS00658029};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843}.
FT   REGION      118    120       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00333}.
FT   REGION      250    285       Important for dimerization.
FT                                {ECO:0000256|HAMAP-Rule:MF_00333}.
FT   REGION      268    270       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00333}.
FT   ACT_SITE    116    116       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00333}.
FT   METAL       106    106       Divalent cation. {ECO:0000256|HAMAP-Rule:
FT                                MF_00333}.
FT   METAL       116    116       Divalent cation. {ECO:0000256|HAMAP-Rule:
FT                                MF_00333}.
FT   METAL       155    155       Divalent cation. {ECO:0000256|HAMAP-Rule:
FT                                MF_00333}.
FT   METAL       185    185       Divalent cation. {ECO:0000256|HAMAP-Rule:
FT                                MF_00333}.
FT   BINDING     102    102       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00333}.
FT   SITE        185    185       Important for dimerization.
FT                                {ECO:0000256|HAMAP-Rule:MF_00333}.
SQ   SEQUENCE   324 AA;  37178 MW;  6D63E6F2AAD75B71 CRC64;
     MAKYLEVNMQ SKLLEQVKAY FMALQDTISQ GLEAADGKAK FIEDNWQRSE GGGGRTRVIT
     NGNIIEQGGV NYSHVFGASM PASATAHRPE LAGRSFHACG VSLVIHPKNP HIPTSHANVR
     FFIAEKEGEQ PIWWFGGGFD LTPFYPVLDD VVHWHQVAHD LCAPFGDELY PKYKTWCDEY
     FYLKHRDETR GVGGLFFDDL NELGFEQSFA FTQAVGNGFL EAYLPIIERR KKDEYTAQQR
     DFQLYRRGRY VEFNLVWDRG TLFGLQTGGR TESILMSMPP LARWEYNYTP NAESAEAKLY
     QYYLRPQQWL STQPNDLIAR ECQL
//

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