COXX_EHRRW
ID COXX_EHRRW Reviewed; 295 AA.
AC Q5HAA6; Q5FDR0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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};
GN OrderedLocusNames=Erum7750, ERWE_CDS_08190;
OS Ehrlichia ruminantium (strain Welgevonden).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=254945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Welgevonden;
RX PubMed=15637156; DOI=10.1073/pnas.0406633102;
RA Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E.,
RA Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M.,
RA Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C.,
RA Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., Allsopp M.T.,
RA Allsopp B.A.;
RT "The genome of the heartwater agent Ehrlichia ruminantium contains multiple
RT tandem repeats of actively variable copy number.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Welgevonden;
RX PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(2006).
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 -!- 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; CR767821; CAH58509.1; -; Genomic_DNA.
DR EMBL; CR925678; CAI27313.1; -; Genomic_DNA.
DR RefSeq; WP_011155454.1; NC_006832.1.
DR AlphaFoldDB; Q5HAA6; -.
DR SMR; Q5HAA6; -.
DR STRING; 254945.Erum7750; -.
DR EnsemblBacteria; CAI27313; CAI27313; ERWE_CDS_08190.
DR GeneID; 56785551; -.
DR KEGG; eru:Erum7750; -.
DR KEGG; erw:ERWE_CDS_08190; -.
DR eggNOG; COG0109; Bacteria.
DR HOGENOM; CLU_029631_0_2_5; -.
DR OMA; MYLKRAT; -.
DR BioCyc; ERUM254945:ERUM_RS04195-MON; -.
DR UniPathway; UPA00834; UER00712.
DR Proteomes; UP000001021; Chromosome.
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 Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..295
FT /note="Protoheme IX farnesyltransferase"
FT /id="PRO_0000327051"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 93..115
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 119..136
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ SEQUENCE 295 AA; 32820 MW; 7244AA085C428CD9 CRC64;
MGIQSSTMKL PLIHEISDYW HLLKPKIMYL VVLTGVTGII IAPGNIHPLI AVISTLCIAL
GSGAAGAINM WYDSDIDALM TRTKTRPIPA GKISRSSALE VGLVLSFISV TIMMIAVNYI
SGILLAISIG FYIYVYTMYL KRRTPQNIVI GGAAGALPPI IGWTSVTGSI SIESLVLFLI
IFMWTPPHFW ALSLLNYHEY EKAKIPMLPV THGIFTTKIH ILVYSILLFP ITLLPGLFLK
DPVLYEITAI PLGLMFVVQA FQVFKSSISY HYRVMFTYSI IYLFILFTCI MLSSF
