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COXX_KINRD
ID   COXX_KINRD              Reviewed;         339 AA.
AC   A6WC46;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=ctaB {ECO:0000255|HAMAP-Rule:MF_00154}; OrderedLocusNames=Krad_2921;
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; Kineococcus.
OX   NCBI_TaxID=266940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216;
RX   PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA   Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA   Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT   "Survival in nuclear waste, extreme resistance, and potential applications
RT   gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL   PLoS ONE 3:e3878-e3878(2008).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00154};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-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; CP000750; ABS04385.1; -; Genomic_DNA.
DR   RefSeq; WP_012087369.1; NC_009664.2.
DR   AlphaFoldDB; A6WC46; -.
DR   SMR; A6WC46; -.
DR   STRING; 266940.Krad_2921; -.
DR   EnsemblBacteria; ABS04385; ABS04385; Krad_2921.
DR   KEGG; kra:Krad_2921; -.
DR   eggNOG; COG0109; Bacteria.
DR   HOGENOM; CLU_029631_0_1_11; -.
DR   OMA; QFFWQFP; -.
DR   OrthoDB; 1875497at2; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000001116; 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; IPR030470; UbiA_prenylTrfase_CS.
DR   InterPro; IPR044878; UbiA_sf.
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;
KW   Cell membrane; Heme biosynthesis; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..339
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_0000346051"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        117..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        140..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   339 AA;  36475 MW;  93F3A48A585B77C9 CRC64;
     MTVADPRLTD APAHSRTSLL GRRRGGRPPR FPRAAAYVAL TKPRIVELLL ITTIPVMLFA
     AGGLPSGWLI LTTFVGGALA AGCANTLNCY FDRDIDALMK RTENRPLVTG EVSPRQALVF
     ATVLGIASTA IFVAFVNVLS AALALGAILL YVVGYTLLLK RRTSQNIVWG GVAGCMQVLI
     GWTAVRDSLD WAPFVLFGVI FLWTPPHYWP LSVRYREDYA NAGVPMLPVV AKPTTVSRQI
     VLYTIAMVLC SLLLVPLGGA GVVYGAAALV LGIGFLVQTI GLHRRATRFE VETGGRDAGT
     LEQLKRISPM GVFHGSITYL TLLSAAVAVD PFVRVGWPF
 
 
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