P0AEA5 (CYOE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protoheme IX farnesyltransferase
EC=2.5.1.-

Alternative name(s):
Heme B farnesyltransferase
Heme O synthase

Gene names

Name:	cyoE
Ordered Locus Names:	b0428, JW0418

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	296 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. Ref.6 Ref.7
Pathway	Porphyrin metabolism; heme O biosynthesis; heme O from protoheme: step 1/1. HAMAP-Rule MF_00154
Subcellular location	Cell inner membrane; Multi-pass membrane protein HAMAP-Rule MF_00154.
Miscellaneous	Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature. HAMAP-Rule MF_00154
Sequence similarities	Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.
Sequence caution	The sequence AAB40184.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Heme biosynthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	heme O biosynthetic process Inferred from direct assay Ref.7. Source: EcoliWiki
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.7. Source: EcoliWiki
Molecular_function	protoheme IX farnesyltransferase activity Inferred from direct assay Ref.7. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 296	296	Protoheme IX farnesyltransferase HAMAP-Rule MF_00154		PRO_0000162895
Regions
	Topological domain	1 – 9	9	Cytoplasmic Probable
	Transmembrane	10 – 28	19	Helical; Probable
	Topological domain	29 – 37	9	Periplasmic Probable
	Transmembrane	38 – 56	19	Helical; Probable
	Topological domain	57 – 78	22	Cytoplasmic Probable
	Transmembrane	79 – 97	19	Helical; Probable
	Topological domain	98 – 107	10	Periplasmic Probable
	Transmembrane	108 – 126	19	Helical; Probable
	Topological domain	127 – 197	71	Cytoplasmic Probable
	Transmembrane	198 – 216	19	Helical; Probable
	Topological domain	217 – 228	12	Periplasmic Probable
	Transmembrane	229 – 247	19	Helical; Probable
	Topological domain	248 – 268	21	Cytoplasmic Probable
	Transmembrane	269 – 287	19	Helical; Probable
	Topological domain	288 – 296	9	Periplasmic Probable

Sequences

	Sequence		Length	Mass (Da)
	P0AEA5 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: D3AFC612ECFB450E	FASTA	296	32,248
	10 20 30 40 50 60 MMFKQYLQVT KPGIIFGNLI SVIGGFLLAS KGSIDYPLFI YTLVGVSLVV ASGCVFNNYI 70 80 90 100 110 120 DRDIDRKMER TKNRVLVKGL ISPAVSLVYA TLLGIAGFML LWFGANPLAC WLGVMGFVVY 130 140 150 160 170 180 VGVYSLYMKR HSVYGTLIGS LSGAAPPVIG YCAVTGEFDS GAAILLAIFS LWQMPHSYAI 190 200 210 220 230 240 AIFRFKDYQA ANIPVLPVVK GISVAKNHIT LYIIAFAVAT LMLSLGGYAG YKYLVVAAAV 250 260 270 280 290 SVWWLGMALR GYKVADDRIW ARKLFGFSII AITALSVMMS VDFMVPDSHT LLAAVW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases." Chepuri V., Lemieux L., Au D.C.T., Gennis R.B. J. Biol. Chem. 265:11185-11192(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The use of gene fusions to determine the topology of all of the subunits of the cytochrome o terminal oxidase complex of Escherichia coli." Chepuri V., Gennis R.B. J. Biol. Chem. 265:12978-12986(1990) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[6]	"Heme O biosynthesis in Escherichia coli: the cyoE gene in the cytochrome bo operon encodes a protoheme IX farnesyltransferase." Saiki K., Mogi T., Anraku Y. Biochem. Biophys. Res. Commun. 189:1491-1497(1992) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"In vitro heme O synthesis by the cyoE gene product from Escherichia coli." Saiki K., Mogi T., Ogura K., Anraku Y. J. Biol. Chem. 268:26041-26044(1993) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY, FUNCTION.
[8]	"Identification of the functional domains in heme O synthase. Site-directed mutagenesis studies on the cyoE gene of the cytochrome bo operon in Escherichia coli." Saiki K., Mogi T., Hori H., Tsubaki M., Anraku Y. J. Biol. Chem. 268:26927-26934(1993) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[9]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J05492 Genomic DNA. Translation: AAA23635.1. U82664 Genomic DNA. Translation: AAB40184.1. Different initiation. U00096 Genomic DNA. Translation: AAC73531.1. AP009048 Genomic DNA. Translation: BAE76208.1.
PIR	E42226.
RefSeq	NP_414962.1. NC_000913.2. YP_488720.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0AEA5.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-47946N.
STRING	511145.b0428.
Protein family/group databases
TCDB	3.D.4.5.1. proton-translocating cytochrome oxidase (COX) superfamily.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73531; AAC73531; b0428. BAE76208; BAE76208; BAE76208.
GeneID	12930845. 945073.
KEGG	ecj:Y75_p0416. eco:b0428.
PATRIC	32116007. VBIEscCol129921_0445.
Organism-specific databases
EchoBASE	EB0179.
EcoGene	EG10182. cyoE.
Phylogenomic databases
eggNOG	COG0109.
HOGENOM	HOG000237290.
KO	K02301.
OMA	EPQLQHD.
ProtClustDB	PRK04375.
Enzyme and pathway databases
BioCyc	EcoCyc:HEMEOSYN-MONOMER. ECOL316407:JW0418-MONOMER. MetaCyc:HEMEOSYN-MONOMER.
UniPathway	UPA00834; UER00712.
Gene expression databases
Genevestigator	P0AEA5.
Family and domain databases
HAMAP	MF_00154. CyoE_CtaB.
InterPro	IPR006369. Protohaem_IX_farnesylTrfase. IPR000537. UbiA_prenyltransferase. [Graphical view]
Pfam	PF01040. UbiA. 1 hit. [Graphical view]
TIGRFAMs	TIGR01473. cyoE_ctaB. 1 hit.
PROSITE	PS00943. UBIA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYOE_ECOLI

Accession

Primary (citable) accession number: P0AEA5
Secondary accession number(s): P18404, P77115, Q2MBZ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program