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Database: UniProt
Entry: Q79EF2
LinkDB: Q79EF2
Original site: Q79EF2 
ID   COXX_SYNY3              Reviewed;         316 AA.
AC   Q79EF2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   01-MAY-2013, entry version 66.
DE   RecName: Full=Protoheme IX farnesyltransferase;
DE            EC=2.5.1.-;
DE   AltName: Full=Heme B farnesyltransferase;
DE   AltName: Full=Heme O synthase;
GN   Name=ctaB; OrderedLocusNames=sll1899;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA   Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA   Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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 (By similarity).
CC   -!- PATHWAY: Porphyrin metabolism; heme O biosynthesis; heme O from
CC       protoheme: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (Potential).
CC   -!- MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined
CC       according to the Fischer nomenclature (By similarity).
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       Protoheme IX farnesyltransferase subfamily.
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DR   EMBL; BA000022; BAA18181.1; -; Genomic_DNA.
DR   RefSeq; NP_441501.1; NC_000911.1.
DR   RefSeq; YP_005651559.1; NC_017277.1.
DR   RefSeq; YP_007451383.1; NC_020286.1.
DR   STRING; 1148.sll1899; -.
DR   EnsemblBacteria; BAA18181; BAA18181; BAA18181.
DR   GeneID; 12254211; -.
DR   GeneID; 14617043; -.
DR   GeneID; 954881; -.
DR   KEGG; syn:sll1899; -.
DR   KEGG; syy:SYNGTS_1606; -.
DR   PATRIC; 23840421; VBISynSp132158_1768.
DR   eggNOG; COG0109; -.
DR   HOGENOM; HOG000237291; -.
DR   KO; K02301; -.
DR   OMA; HTWTLAM; -.
DR   ProtClustDB; PRK04375; -.
DR   UniPathway; UPA00834; UER00712.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008495; F:protoheme IX farnesyltransferase activity; IEA:HAMAP.
DR   GO; GO:0048034; P:heme O biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00154; CyoE_CtaB; 1; -.
DR   InterPro; IPR006369; Protohaem_IX_farnesylTrfase.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
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; Complete proteome;
KW   Heme biosynthesis; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    316       Protoheme IX farnesyltransferase.
FT                                /FTId=PRO_0000327182.
FT   TRANSMEM     29     49       Helical; (Potential).
FT   TRANSMEM     54     74       Helical; (Potential).
FT   TRANSMEM    102    122       Helical; (Potential).
FT   TRANSMEM    123    143       Helical; (Potential).
FT   TRANSMEM    151    171       Helical; (Potential).
FT   TRANSMEM    179    199       Helical; (Potential).
FT   TRANSMEM    224    241       Helical; (Potential).
FT   TRANSMEM    245    267       Helical; (Potential).
FT   TRANSMEM    283    303       Helical; (Potential).
SQ   SEQUENCE   316 AA;  34858 MW;  BA376839441BF7B0 CRC64;
     MVTSTKIHRQ HDSMGAVCKS YYQLTKPRII PLLLITTAAS MWIASEGRVD LPKLLITLLG
     GTLAAASAQT LNCIYDQDID YEMLRTRARP IPAGKVQPRH ALIFALALGV LSFALLATFV
     NVLSGCLALS GIVFYMLVYT HWLKRHTAQN IVIGGAAGSI PPLVGWAAVT GDLSWTPWVL
     FALIFLWTPP HFWALALMIK DDYAQVNVPM LPVIAGEEKT VSQIWYYSLL VVPFSLLLVY
     PLHQLGILYL AIAIILGGQF LVKAWQLKQA PGDRDLARGL FKFSIFYLML LCLAMVIDSL
     PVTHQLVAQM GTLLLG
//
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