CYOE_PSEU2
ID CYOE_PSEU2 Reviewed; 295 AA.
AC Q4ZXC3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
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=Psyr_1145;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(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 ---------------------------------------------------------------------------
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; CP000075; AAY36199.1; -; Genomic_DNA.
DR RefSeq; WP_003314082.1; NC_007005.1.
DR RefSeq; YP_234237.1; NC_007005.1.
DR AlphaFoldDB; Q4ZXC3; -.
DR SMR; Q4ZXC3; -.
DR STRING; 205918.Psyr_1145; -.
DR EnsemblBacteria; AAY36199; AAY36199; Psyr_1145.
DR GeneID; 64442323; -.
DR GeneID; 65075121; -.
DR KEGG; psb:Psyr_1145; -.
DR PATRIC; fig|205918.7.peg.1178; -.
DR eggNOG; COG0109; Bacteria.
DR HOGENOM; CLU_029631_0_0_6; -.
DR OMA; QFFWQFP; -.
DR UniPathway; UPA00834; UER00712.
DR Proteomes; UP000000426; 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..295
FT /note="Protoheme IX farnesyltransferase"
FT /id="PRO_0000326931"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ SEQUENCE 295 AA; 32358 MW; EF95F01C2FD96E7C CRC64;
MSLKHFIQIT KPGIIFGNVL SVAGGFFLAS KGNIDFGVFL AAVIGTSLVV ASGCVFNNCI
DRDIDQRMER TRNRVLVQGL VSLKLALLYA TLLGIAGVGL LYTEANPLAA LFAVIGFVIY
VGLYSLYLKR RSVHGTLVGS LSGAMPPVIG YCAVSNSFDF AALTLLVMFS LWQMPHSYAI
AIFRFNDYRA AKIPVLPVKR GILVTKRHIM LYILAFLVAT LMLTVGGYAG LNYLAVAAGM
GMYWLYMAWK GYKAVDDTVW ARKLFVFSIF TITALSVMMS VDFQVTKELL VTYAF
