(data stored in ACNUC7421 zone)

SWISSPROT: CYOE_STRM5

ID   CYOE_STRM5              Reviewed;         297 AA.
AC   B4SHI1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   16-JAN-2019, entry version 59.
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=Smal_0319;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts heme B (protoheme IX) to heme O by substitution
CC       of the vinyl group on carbon 2 of heme B porphyrin ring with a
CC       hydroxyethyl farnesyl side group. {ECO:0000255|HAMAP-
CC       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
CC       biosynthesis; heme O from protoheme: step 1/1. {ECO:0000255|HAMAP-
CC       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.
CC       Protoheme IX farnesyltransferase subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00154}.
DR   EMBL; CP001111; ACF50024.1; -; Genomic_DNA.
DR   RefSeq; WP_004138490.1; NC_011071.1.
DR   STRING; 391008.Smal_0319; -.
DR   EnsemblBacteria; ACF50024; ACF50024; Smal_0319.
DR   KEGG; smt:Smal_0319; -.
DR   eggNOG; ENOG4105F1R; Bacteria.
DR   eggNOG; COG0109; LUCA.
DR   HOGENOM; HOG000237291; -.
DR   KO; K02257; -.
DR   OMA; HRKEEYA; -.
DR   OrthoDB; 1875497at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01670-MONOMER; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000001867; 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   HAMAP; MF_00154; CyoE_CtaB; 1.
DR   InterPro; IPR006369; Protohaem_IX_farnesylTrfase.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR030470; UbiA_prenylTrfase_CS.
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;
DR   PRODOM; B4SHI1.
DR   SWISS-2DPAGE; B4SHI1.
KW   Cell inner membrane; Cell membrane; Complete proteome;
KW   Heme biosynthesis; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    297       Protoheme IX farnesyltransferase.
FT                                /FTId=PRO_1000096927.
FT   TRANSMEM     16     36       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM     45     65       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM     93    113       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM    114    134       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM    141    161       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM    172    192       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM    223    243       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM    244    264       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM    277    297       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
SQ   SEQUENCE   297 AA;  33163 MW;  00C3B34D22A1F334 CRC64;
     MFSNYRQYWD LTKPKVVALI VFTALVGMVL AIPGVPSWEQ VRAGVLGFLG IWLAASAAAA
     INQLLDAHID AQMARTSWRP LVVGKVKPWQ VLVFASVLIV LSMVILVLWV NLITAVLTFA
     SLIGYAVIYT VYLKRATSQN IVIGGLAGAM PPMLGWAAVT GMQGSSDWAY SSLLVLIIFI
     WTPPHFWALA IFRREDYAKA EIPMLPVTHG VVHTRKQIMV YSVVLALVCL LPYLVGMSGA
     FYLGGAIVLN AVFLWYAWRM LDPPDELFSM KMFYYSIVYL MALFAFLLVD HWILPWL
//

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