COXX_CERS4
ID COXX_CERS4 Reviewed; 310 AA.
AC Q3J5F9; Q66LN7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Protoheme IX farnesyltransferase;
DE EC=2.5.1.141;
DE AltName: Full=Heme B farnesyltransferase;
DE AltName: Full=Heme O synthase;
GN Name=ctaB; Synonyms=cox10; OrderedLocusNames=RHOS4_04070;
GN ORFNames=RSP_1827;
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], FUNCTION, AND INTERACTION.
RX PubMed=15491161; DOI=10.1021/bi048469k;
RA Brown B.M., Wang Z., Brown K.R., Cricco J.A., Hegg E.L.;
RT "Heme O synthase and heme A synthase from Bacillus subtilis and Rhodobacter
RT sphaeroides interact in Escherichia coli.";
RL Biochemistry 43:13541-13548(2004).
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: 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:0000269|PubMed:15491161}.
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;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; heme O biosynthesis;
CC heme O from protoheme: step 1/1.
CC -!- SUBUNIT: Interacts with CtaA. {ECO:0000269|PubMed:15491161}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined
CC according to the Fischer nomenclature.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. Protoheme IX
CC farnesyltransferase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY692270; AAU04882.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA77975.1; -; Genomic_DNA.
DR RefSeq; WP_002722694.1; NZ_CP030271.1.
DR RefSeq; YP_351876.1; NC_007493.2.
DR AlphaFoldDB; Q3J5F9; -.
DR SMR; Q3J5F9; -.
DR IntAct; Q3J5F9; 1.
DR STRING; 272943.RSP_1827; -.
DR EnsemblBacteria; ABA77975; ABA77975; RSP_1827.
DR GeneID; 57469169; -.
DR KEGG; rsp:RSP_1827; -.
DR PATRIC; fig|272943.9.peg.713; -.
DR eggNOG; COG0109; Bacteria.
DR OMA; QFFWQFP; -.
DR PhylomeDB; Q3J5F9; -.
DR BRENDA; 2.5.1.141; 5383.
DR UniPathway; UPA00834; UER00712.
DR Proteomes; UP000002703; Chromosome 1.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Heme biosynthesis; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..310
FT /note="Protoheme IX farnesyltransferase"
FT /id="PRO_0000327134"
FT TRANSMEM 26..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 310 AA; 33357 MW; 2FECC8D6F66CB477 CRC64;
MTDIRITGIP KEAGFGDYVA LLKPRVMSLV VFTALVGLLV APVTVHPMIA LTGILFIALG
AGASGALNMW WDEDIDRVMK RTRNRPVPSG TVAPGEALGI GLALSGIAVV MLGLATNLFA
AGLLAFTIFF YAVVYSMWLK RTTPQNIVIG GAAGAFPPMI GWAVATGGVS VESLFMFALI
FMWTPPHFWS LALFMKSDYS DAGVPMLTVT HGRRVTRAHV LVYSLLLAPL AVAGAFTGIG
GPLYLATALA LNGWLLVGAV RIWRRDEAQA EADRYRVEKG FFRFSLYYLF LHFGAILAEA
ALKPYGLGGW