COXX_THET2
ID COXX_THET2 Reviewed; 608 AA.
AC Q72H22;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Protoheme IX farnesyltransferase;
DE EC=2.5.1.141;
DE AltName: Full=Heme B farnesyltransferase;
DE AltName: Full=Heme O synthase;
GN Name=ctaB; OrderedLocusNames=TT_C1673;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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:0000250}.
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;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; heme O biosynthesis;
CC heme O from protoheme: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined
CC according to the Fischer nomenclature (By similarity). Protoheme IX
CC farnesyltransferase subfamily. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the COX15/CtaA
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the UbiA
CC prenyltransferase family. Protoheme IX farnesyltransferase subfamily.
CC {ECO:0000305}.
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DR EMBL; AE017221; AAS82015.1; -; Genomic_DNA.
DR RefSeq; WP_011174039.1; NC_005835.1.
DR AlphaFoldDB; Q72H22; -.
DR SMR; Q72H22; -.
DR STRING; 262724.TT_C1673; -.
DR EnsemblBacteria; AAS82015; AAS82015; TT_C1673.
DR KEGG; tth:TT_C1673; -.
DR eggNOG; COG0109; Bacteria.
DR eggNOG; COG1612; Bacteria.
DR HOGENOM; CLU_030009_0_0_0; -.
DR OMA; MKPRLMW; -.
DR OrthoDB; 1875497at2; -.
DR UniPathway; UPA00834; UER00712.
DR Proteomes; UP000000592; 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:0016653; F:oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor; IEA:InterPro.
DR GO; GO:0008495; F:protoheme IX farnesyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006784; P:heme A biosynthetic process; IEA:InterPro.
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; IPR003780; COX15/CtaA_fam.
DR InterPro; IPR006369; Protohaem_IX_farnesylTrfase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR43448; PTHR43448; 1.
DR Pfam; PF02628; COX15-CtaA; 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 Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..608
FT /note="Protoheme IX farnesyltransferase"
FT /id="PRO_0000327192"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..304
FT /note="COX15/CtaA"
FT REGION 339..606
FT /note="Protoheme IX prenyltransferase"
SQ SEQUENCE 608 AA; 65770 MW; 189B566599BEDCD6 CRC64;
MKTPAWSRLA GYAWGVLLWN VLVALFGAYV RATGSGAGCG AHWPTCNGEV IPRAPQVETL
IEFTHRATSG LAFLSVLALF LWALRAFPKG HPARFGAGLA LFFMVTESLV GASLVLFGWT
ADNVSRERAV VQMVHLANTY FLLAALALTA WWASGGGPLR LRGQGAVGLA LFLGLLALLF
LGMSGAVTAL GDLLFPVGST LEALERSLTP GEHFLVRLRV LHPLIAVSVG LYVVFAGYLV
AHLRPSPLTR RLAQGLAYLY GAQLLAGLIN VALKAPVWMQ ILHLLLAYAV WLLFVFLATS
ALERGAKRVE LGEGGEAVHR GTGGATWRDY LALTKPRVIS LLLFTALFGA LIAAKGWPGL
GVFLAVALGG YMMAGAANAI NMVVDRDIDA RMKRTAKRPT VTQRVSSRDA LLFAFALAVL
GFAVLWWGAN LLAATLALMG LIWYVLVYTL YLKRRTWHNI VIGGAAGAFP PLVGWAAVTG
ELSLFAWYLF ALIFFWTPVH FWALALMIQD DYRAVGVPML PVVLGERATV IQIALYALLT
ALISLMPLLL GELGLLYLAA SLLLNALLLL KSLALYRRPE RRTAVSLYKY SMLYLALLFA
AMAVDRAV
