CYOE_ECOLI
ID CYOE_ECOLI Reviewed; 296 AA.
AC P0AEA5; P18404; P77115; Q2MBZ8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protoheme IX farnesyltransferase;
DE EC=2.5.1.141 {ECO:0000269|PubMed:8253713};
DE AltName: Full=Heme B farnesyltransferase;
DE AltName: Full=Heme O synthase {ECO:0000303|PubMed:8253713};
GN Name=cyoE; OrderedLocusNames=b0428, JW0418;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2162835; DOI=10.1016/s0021-9258(19)38574-6;
RA Chepuri V., Lemieux L., Au D.C.T., Gennis R.B.;
RT "The sequence of the cyo operon indicates substantial structural
RT similarities between the cytochrome o ubiquinol oxidase of Escherichia coli
RT and the aa3-type family of cytochrome c oxidases.";
RL J. Biol. Chem. 265:11185-11192(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP TOPOLOGY.
RX PubMed=2165491; DOI=10.1016/s0021-9258(19)38256-0;
RA Chepuri V., Gennis R.B.;
RT "The use of gene fusions to determine the topology of all of the subunits
RT of the cytochrome o terminal oxidase complex of Escherichia coli.";
RL J. Biol. Chem. 265:12978-12986(1990).
RN [6]
RP FUNCTION.
RX PubMed=1336371; DOI=10.1016/0006-291x(92)90243-e;
RA Saiki K., Mogi T., Anraku Y.;
RT "Heme O biosynthesis in Escherichia coli: the cyoE gene in the cytochrome
RT bo operon encodes a protoheme IX farnesyltransferase.";
RL Biochem. Biophys. Res. Commun. 189:1491-1497(1992).
RN [7]
RP TOPOLOGY, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=8253713; DOI=10.1016/s0021-9258(19)74272-0;
RA Saiki K., Mogi T., Ogura K., Anraku Y.;
RT "In vitro heme O synthesis by the cyoE gene product from Escherichia
RT coli.";
RL J. Biol. Chem. 268:26041-26044(1993).
RN [8]
RP MUTAGENESIS.
RX PubMed=8262927; DOI=10.1016/s0021-9258(19)74199-4;
RA Saiki K., Mogi T., Hori H., Tsubaki M., Anraku Y.;
RT "Identification of the functional domains in heme O synthase. Site-directed
RT mutagenesis studies on the cyoE gene of the cytochrome bo operon in
RT Escherichia coli.";
RL J. Biol. Chem. 268:26927-26934(1993).
RN [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(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:0000269|PubMed:1336371,
CC ECO:0000269|PubMed:8253713}.
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 Evidence={ECO:0000269|PubMed:8253713};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; heme O biosynthesis;
CC heme O from protoheme: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8253713};
CC Multi-pass membrane protein.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAB40184.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J05492; AAA23635.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40184.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73531.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76208.1; -; Genomic_DNA.
DR PIR; E42226; E42226.
DR RefSeq; NP_414962.1; NC_000913.3.
DR RefSeq; WP_000971336.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; P0AEA5; -.
DR SMR; P0AEA5; -.
DR BioGRID; 4259839; 24.
DR DIP; DIP-47946N; -.
DR STRING; 511145.b0428; -.
DR PaxDb; P0AEA5; -.
DR PRIDE; P0AEA5; -.
DR EnsemblBacteria; AAC73531; AAC73531; b0428.
DR EnsemblBacteria; BAE76208; BAE76208; BAE76208.
DR GeneID; 66671270; -.
DR GeneID; 945073; -.
DR KEGG; ecj:JW0418; -.
DR KEGG; eco:b0428; -.
DR PATRIC; fig|1411691.4.peg.1849; -.
DR EchoBASE; EB0179; -.
DR eggNOG; COG0109; Bacteria.
DR HOGENOM; CLU_029631_0_0_6; -.
DR InParanoid; P0AEA5; -.
DR OMA; QFFWQFP; -.
DR PhylomeDB; P0AEA5; -.
DR BioCyc; EcoCyc:HEMEOSYN-MON; -.
DR BioCyc; MetaCyc:HEMEOSYN-MON; -.
DR BRENDA; 2.5.1.141; 2026.
DR UniPathway; UPA00834; UER00712.
DR PRO; PR:P0AEA5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IBA:GO_Central.
DR GO; GO:0008495; F:protoheme IX farnesyltransferase activity; IDA:EcoliWiki.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR GO; GO:0048034; P:heme O biosynthetic process; IDA:EcoliWiki.
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..296
FT /note="Protoheme IX farnesyltransferase"
FT /id="PRO_0000162895"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..28
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 29..37
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 38..56
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 57..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 79..97
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 98..107
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 127..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 198..216
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 217..228
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 229..247
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 248..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 269..287
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 288..296
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 32248 MW; D3AFC612ECFB450E CRC64;
MMFKQYLQVT KPGIIFGNLI SVIGGFLLAS KGSIDYPLFI YTLVGVSLVV ASGCVFNNYI
DRDIDRKMER TKNRVLVKGL ISPAVSLVYA TLLGIAGFML LWFGANPLAC WLGVMGFVVY
VGVYSLYMKR HSVYGTLIGS LSGAAPPVIG YCAVTGEFDS GAAILLAIFS LWQMPHSYAI
AIFRFKDYQA ANIPVLPVVK GISVAKNHIT LYIIAFAVAT LMLSLGGYAG YKYLVVAAAV
SVWWLGMALR GYKVADDRIW ARKLFGFSII AITALSVMMS VDFMVPDSHT LLAAVW
