CYOE_COLP3
ID CYOE_COLP3 Reviewed; 306 AA.
AC Q48AB7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 25-MAY-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=cyoE {ECO:0000255|HAMAP-Rule:MF_00154}; OrderedLocusNames=CPS_0229;
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H / ATCC BAA-681;
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ24423.1; Type=Erroneous initiation; Evidence={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; CP000083; AAZ24423.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_049757975.1; NC_003910.7.
DR AlphaFoldDB; Q48AB7; -.
DR SMR; Q48AB7; -.
DR STRING; 167879.CPS_0229; -.
DR EnsemblBacteria; AAZ24423; AAZ24423; CPS_0229.
DR KEGG; cps:CPS_0229; -.
DR eggNOG; COG0109; Bacteria.
DR HOGENOM; CLU_029631_0_2_6; -.
DR UniPathway; UPA00834; UER00712.
DR Proteomes; UP000000547; 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 Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..306
FT /note="Protoheme IX farnesyltransferase"
FT /id="PRO_0000326888"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 249..269
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 306 AA; 33720 MW; 1587C2933CDC5069 CRC64;
MPSVINTGHH HFSISNIFAN WRAYYDITKP KVVALLVLTA LVGMSLSVPG ALPWQRLIPA
MLGIGLLSSA AAAINHIVDE KIDTVMGRTH NRPLPAGKIS VTNAIVFATS IALLGFIILY
ALVNPLTAFL TLAGLVGYSF VYTMYLKRAT PQNITIGGLA GAIPPLLGWT AMTNEVVPNA
LLLVLIIFTW TPPHFWALAI HRKNDYAKVN IPMLPVTHGV SFTKTQILLY TVLLFVVCLL
PYLVGMSNWL YLIGACSLNL IFFGYAWQLK FNAKEGTAMA TFKFSIIHLM LLFIILLLDH
YWLPMG
