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CYOE_TERTT
ID   CYOE_TERTT              Reviewed;         311 AA.
AC   C5BKU5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=TERTU_0086;
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901;
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA   Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA   Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA   Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT   endosymbiont of marine wood-boring bivalves (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
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}.
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DR   EMBL; CP001614; ACR13072.1; -; Genomic_DNA.
DR   RefSeq; WP_015819185.1; NC_012997.1.
DR   AlphaFoldDB; C5BKU5; -.
DR   SMR; C5BKU5; -.
DR   STRING; 377629.TERTU_0086; -.
DR   EnsemblBacteria; ACR13072; ACR13072; TERTU_0086.
DR   KEGG; ttu:TERTU_0086; -.
DR   eggNOG; COG0109; Bacteria.
DR   HOGENOM; CLU_029631_0_2_6; -.
DR   OMA; MYLKRAT; -.
DR   OrthoDB; 1875497at2; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000009080; 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; IPR044878; UbiA_sf.
DR   PANTHER; PTHR43448; PTHR43448; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   TIGRFAMs; TIGR01473; cyoE_ctaB; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Heme biosynthesis; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..311
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_1000203465"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ   SEQUENCE   311 AA;  33941 MW;  32EF4F3ACFE69FDB CRC64;
     MALIIRSEID KATQAITTAL PWRDYYELTK PKVVMLMLLT SLIGMLLATP SPAPLWLLVL
     GNLGIGLCAG AAAAVNHLVD RHVDVKMART FHRPVANGRI TPTNALLFSA LLGGVGLWIL
     SSFINALTAW LTLASLLGYA VIYTLFLKRA TPQNIVIGGL AGAAPPLLGW TAVTGELDGH
     GLLLVLIIFA WTPPHFWALA LYRKKEYAKA GIPMLPVTHG DSYTRLHIVL YTVILIAVTL
     LPFATRMMGY CYLVGALVLG AGFLYRALKL LVSKDPKQGL ETFKFSIIYL MALFVVMLVD
     HYLFPIPVYG V
 
 
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