COXX_THET8
ID COXX_THET8 Reviewed; 608 AA.
AC Q5SLI3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=TTHA0310;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. {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; AP008226; BAD70133.1; -; Genomic_DNA.
DR RefSeq; WP_011227849.1; NC_006461.1.
DR RefSeq; YP_143576.1; NC_006461.1.
DR AlphaFoldDB; Q5SLI3; -.
DR SMR; Q5SLI3; -.
DR STRING; 300852.55771692; -.
DR EnsemblBacteria; BAD70133; BAD70133; BAD70133.
DR GeneID; 3169720; -.
DR KEGG; ttj:TTHA0310; -.
DR PATRIC; fig|300852.9.peg.310; -.
DR eggNOG; COG0109; Bacteria.
DR eggNOG; COG1612; Bacteria.
DR HOGENOM; CLU_030009_0_0_0; -.
DR OMA; MKPRLMW; -.
DR UniPathway; UPA00834; UER00712.
DR Proteomes; UP000000532; 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 Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..608
FT /note="Protoheme IX farnesyltransferase"
FT /id="PRO_0000346082"
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..338
FT /note="COX15/CtaA"
FT REGION 339..608
FT /note="Protoheme IX prenyltransferase"
SQ SEQUENCE 608 AA; 65784 MW; F44FA4707AB4E241 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 ILHLLLAYAI 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
