CYOE_ECO24
ID CYOE_ECO24 Reviewed; 296 AA.
AC A7ZII5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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};
GN OrderedLocusNames=EcE24377A_0463;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV20910.1; -; Genomic_DNA.
DR RefSeq; WP_000971336.1; NC_009801.1.
DR AlphaFoldDB; A7ZII5; -.
DR SMR; A7ZII5; -.
DR EnsemblBacteria; ABV20910; ABV20910; EcE24377A_0463.
DR GeneID; 66671270; -.
DR KEGG; ecw:EcE24377A_0463; -.
DR HOGENOM; CLU_029631_0_0_6; -.
DR OMA; QFFWQFP; -.
DR UniPathway; UPA00834; UER00712.
DR Proteomes; UP000001122; 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..296
FT /note="Protoheme IX farnesyltransferase"
FT /id="PRO_0000345997"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 10..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TOPO_DOM 29..37
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 38..56
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TOPO_DOM 57..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 79..97
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TOPO_DOM 98..107
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TOPO_DOM 127..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 198..216
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TOPO_DOM 217..228
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 229..247
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TOPO_DOM 248..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 269..287
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TOPO_DOM 288..296
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
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
