(data stored in ACNUC7421 zone)

SWISSPROT: CYOE_SHISS

ID   CYOE_SHISS              Reviewed;         296 AA.
AC   Q3Z4X5;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   05-DEC-2018, entry version 81.
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=SSON_0411;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ87187.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87187; AAZ87187; SSON_0411.
DR   KEGG; ssn:SSON_0411; -.
DR   HOGENOM; HOG000237290; -.
DR   KO; K02257; -.
DR   OMA; WQFPHFW; -.
DR   BioCyc; SSON300269:G1GL2-475-MONOMER; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000002529; 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; Q3Z4X5.
DR   SWISS-2DPAGE; Q3Z4X5.
KW   Cell inner membrane; Cell membrane; Complete proteome;
KW   Heme biosynthesis; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    296       Protoheme IX farnesyltransferase.
FT                                /FTId=PRO_0000326959.
FT   TOPO_DOM      1      9       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM     10     28       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TOPO_DOM     29     37       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM     38     56       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TOPO_DOM     57     78       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM     79     97       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TOPO_DOM     98    107       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM    108    126       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TOPO_DOM    127    197       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM    198    216       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TOPO_DOM    217    228       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM    229    247       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TOPO_DOM    248    268       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TRANSMEM    269    287       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
FT   TOPO_DOM    288    296       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00154}.
SQ   SEQUENCE   296 AA;  32283 MW;  D8733236CFF7B12D CRC64;
     MMFKQYLQVT KPGIIFGNLI SVIGGFLLAS KGSIDYPLFI YTLVGVSLVV ASGCVFNNYI
     DRDIDRKMER TKNRVLVKGL ISPAVSLVYA TLLGFAGFML LWFGANPLAC WLGVMGFVVY
     VGVYSLYMKR HSVYGTLIGS LSGAAPPVIG YCAVTGEFDS GAAILLAIFS LWQMPHSYAI
     AIFRFKDYQA ANIPVLPVVK GISVAKNHIT LYIIAFAVAT LMLSLGGYAG YKYLVVAAAV
     SVWWLGMALR GYKVADDRIW ARKLFGFSII AITALSVMMS VDFMVPDSHT LLAAVW
//

If you have problems or comments...

PBIL Back to PBIL home page