(data stored in ACNUC7421 zone)

SWISSPROT: B7UJQ1_ECO27

ID   B7UJQ1_ECO27            Unreviewed;       296 AA.
AC   B7UJQ1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=Protoheme IX farnesyltransferase {ECO:0000256|HAMAP-Rule:MF_00154};
DE            EC=2.5.1.141 {ECO:0000256|HAMAP-Rule:MF_00154};
DE   AltName: Full=Heme B farnesyltransferase {ECO:0000256|HAMAP-Rule:MF_00154};
DE   AltName: Full=Heme O synthase {ECO:0000256|HAMAP-Rule:MF_00154};
GN   Name=cyoE {ECO:0000256|HAMAP-Rule:MF_00154,
GN   ECO:0000313|EMBL:CAS07911.1};
GN   OrderedLocusNames=E2348C_0363 {ECO:0000313|EMBL:CAS07911.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07911.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07911.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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:0000256|HAMAP-
CC       Rule:MF_00154, ECO:0000256|SAAS:SAAS00958916}.
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:0000256|HAMAP-
CC         Rule:MF_00154, ECO:0000256|SAAS:SAAS01123687};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; heme O
CC       biosynthesis; heme O from protoheme: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_00154, ECO:0000256|SAAS:SAAS00958899}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00154}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00154}.
CC   -!- MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined
CC       according to the Fischer nomenclature. {ECO:0000256|HAMAP-
CC       Rule:MF_00154}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       Protoheme IX farnesyltransferase subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00154, ECO:0000256|SAAS:SAAS00958900}.
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DR   EMBL; FM180568; CAS07911.1; -; Genomic_DNA.
DR   RefSeq; WP_000576425.1; NC_011601.1.
DR   EnsemblBacteria; CAS07911; CAS07911; E2348C_0363.
DR   KEGG; ecg:E2348C_0363; -.
DR   HOGENOM; HOG000237290; -.
DR   KO; K02257; -.
DR   OMA; WQFPHFW; -.
DR   BioCyc; ECOL574521:E2348C_RS01905-MONOMER; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000008205; 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; B7UJQ1.
DR   SWISS-2DPAGE; B7UJQ1.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00154};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00154,
KW   ECO:0000256|SAAS:SAAS00964118};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Heme biosynthesis {ECO:0000256|HAMAP-Rule:MF_00154,
KW   ECO:0000256|SAAS:SAAS00964124};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00154,
KW   ECO:0000256|SAAS:SAAS00181105, ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00154,
KW   ECO:0000256|SAAS:SAAS00181134, ECO:0000313|EMBL:CAS07911.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00154,
KW   ECO:0000256|SAAS:SAAS00181127, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00154,
KW   ECO:0000256|SAAS:SAAS00181088, ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM      1      9       Cytoplasmic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
FT   TRANSMEM     12     30       Helical. {ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM     29     37       Periplasmic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
FT   TRANSMEM     36     60       Helical. {ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM     57     78       Cytoplasmic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
FT   TRANSMEM     80    102       Helical. {ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM     98    107       Periplasmic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
FT   TRANSMEM    108    127       Helical. {ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM    127    197       Cytoplasmic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
FT   TRANSMEM    134    156       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    162    183       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    209    227       Helical. {ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM    217    228       Periplasmic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
FT   TRANSMEM    233    252       Helical. {ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM    248    268       Cytoplasmic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
FT   TRANSMEM    264    285       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   296 AA;  32230 MW;  D7FFC04C951E84B9 CRC64;
     MIFKQYLQVT 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
//

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