COXX_BURPS
ID COXX_BURPS Reviewed; 300 AA.
AC Q63XS7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=BPSL0462;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571965; CAH34451.1; -; Genomic_DNA.
DR RefSeq; WP_004522902.1; NZ_CP009538.1.
DR RefSeq; YP_107088.1; NC_006350.1.
DR AlphaFoldDB; Q63XS7; -.
DR SMR; Q63XS7; -.
DR STRING; 272560.BPSL0462; -.
DR EnsemblBacteria; CAH34451; CAH34451; BPSL0462.
DR GeneID; 56527293; -.
DR KEGG; bps:BPSL0462; -.
DR PATRIC; fig|272560.51.peg.1194; -.
DR eggNOG; COG0109; Bacteria.
DR OMA; QFFWQFP; -.
DR UniPathway; UPA00834; UER00712.
DR Proteomes; UP000000605; 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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Heme biosynthesis; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..300
FT /note="Protoheme IX farnesyltransferase"
FT /id="PRO_0000327028"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ SEQUENCE 300 AA; 32874 MW; 335F2BEA1D5BD597 CRC64;
MDTTLSHTPG SRLSQYLALT KPRVTQLAVF CAVIGMFLAT PGMVPWKVLL GGTIGIGLLA
GSAFAINCLV EQKIDAMMRR TAWRPSARGE ITTLQILAFS TVLGGLGAWT LYTFTNPLTM
WLTIATFVGY AVIYTLLLKP MTPQNIVIGG ASGAMPPALG WAAVTGAVPG DAWILVLIIF
VWTPPHFWVL ALYRRKDYEN AGLPMLPVTH GEQFTRLHIL LYTVILFAVT MMPFISGMSG
AVYLTSAVLL GALFLAYAWK IYRDYSDALA RRAFRYSIVY LSLLFAALLV DHYARPVIGM
