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COXX_PARDP
ID   COXX_PARDP              Reviewed;         305 AA.
AC   A1BA40;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Protoheme IX farnesyltransferase {ECO:0000255|HAMAP-Rule:MF_00154};
DE            EC=2.5.1.141 {ECO:0000255|HAMAP-Rule:MF_00154};
DE   AltName: Full=Heme B farnesyltransferase {ECO:0000255|HAMAP-Rule:MF_00154};
DE   AltName: Full=Heme O synthase {ECO:0000255|HAMAP-Rule:MF_00154};
GN   Name=ctaB {ECO:0000255|HAMAP-Rule:MF_00154}; OrderedLocusNames=Pden_4320;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts heme B (protoheme IX) to heme O by substitution of
CC       the vinyl group on carbon 2 of heme B porphyrin ring with a
CC       hydroxyethyl farnesyl side group. {ECO:0000255|HAMAP-Rule:MF_00154}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate +
CC         Fe(II)-heme o; Xref=Rhea:RHEA:28070, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:60344, ChEBI:CHEBI:60530,
CC         ChEBI:CHEBI:175763; EC=2.5.1.141; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00154};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; heme O biosynthesis;
CC       heme O from protoheme: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00154}.
CC   -!- SUBUNIT: Interacts with CtaA. {ECO:0000255|HAMAP-Rule:MF_00154}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00154}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00154}.
CC   -!- MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined
CC       according to the Fischer nomenclature. {ECO:0000255|HAMAP-
CC       Rule:MF_00154}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. Protoheme IX
CC       farnesyltransferase subfamily. {ECO:0000255|HAMAP-Rule:MF_00154}.
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DR   EMBL; CP000490; ABL72384.1; -; Genomic_DNA.
DR   RefSeq; WP_011750546.1; NC_008687.1.
DR   AlphaFoldDB; A1BA40; -.
DR   SMR; A1BA40; -.
DR   STRING; 318586.Pden_4320; -.
DR   PRIDE; A1BA40; -.
DR   EnsemblBacteria; ABL72384; ABL72384; Pden_4320.
DR   KEGG; pde:Pden_4320; -.
DR   eggNOG; COG0109; Bacteria.
DR   HOGENOM; CLU_029631_0_2_5; -.
DR   OMA; MYLKRAT; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000000361; Chromosome 2.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008495; F:protoheme IX farnesyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048034; P:heme O biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd13957; PT_UbiA_Cox10; 1.
DR   Gene3D; 1.10.357.140; -; 1.
DR   HAMAP; MF_00154; CyoE_CtaB; 1.
DR   InterPro; IPR006369; Protohaem_IX_farnesylTrfase.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR   InterPro; IPR044878; UbiA_sf.
DR   PANTHER; PTHR43448; PTHR43448; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   TIGRFAMs; TIGR01473; cyoE_ctaB; 1.
DR   PROSITE; PS00943; UBIA; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Heme biosynthesis; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..305
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_0000327108"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ   SEQUENCE   305 AA;  33261 MW;  7A9D19FCC0898EFF CRC64;
     MADINAYEGP AEAGFGDYVA LLKPRVMSLV VFTAFVGLWI APQPVNPFVA FCAVLFIALG
     GGASGALNMW YDADIDAVMR RTAGRPVPSG RVTSQEALAV GIALSGLSVM MLGLAANWFA
     AGFLAFTIFF YAVVYTIWLK RSTPQNIVIG GAAGAFPPMI GWACATGGIG IESLLMFALI
     FFWTPPHFWA LALFMKDDYS KAGVPMLTVT HGRKVTRCHI FAYTLVLAPF ALWLGFTSVG
     GPLYLAVSVV LNALFIAGGW QILRRSEDQA QADGYRVEKR YFRLSLYYTF LHFLALLVQH
     WVGGW
 
 
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