COXX_BACAA
ID COXX_BACAA Reviewed; 307 AA.
AC C3P6V2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=BAA_4180;
OS Bacillus anthracis (strain A0248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=592021;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A0248;
RA Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., Sims D.,
RA Brettin T.;
RT "Genome sequence of Bacillus anthracis A0248.";
RL Submitted (APR-2009) 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: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 -!- SUBUNIT: Interacts with CtaA. {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; CP001598; ACQ47218.1; -; Genomic_DNA.
DR RefSeq; WP_001015052.1; NC_012659.1.
DR AlphaFoldDB; C3P6V2; -.
DR SMR; C3P6V2; -.
DR GeneID; 45023832; -.
DR KEGG; bai:BAA_4180; -.
DR HOGENOM; CLU_029631_0_0_9; -.
DR OMA; QFFWQFP; -.
DR UniPathway; UPA00834; UER00712.
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; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..307
FT /note="Protoheme IX farnesyltransferase"
FT /id="PRO_1000199637"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 251..271
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 307 AA; 34549 MW; 150FAC0D365FF3F9 CRC64;
MNHATSELHD ESAVTSIPET TRLQDLKALV KMGIVNSNTL TVFTGFWLAL HFNGLSVMDN
LDKLFFTIVG SGLVMAGVCC LNNYIDRDID PLMERTKTRP TVTGKYKPGF ALTFGLVILL
LGFVFLLLTT PMAVLMGFIG AFTYVVLYSL WTKRKYTLNT VVGSISGAVP PLIGWAAIDP
SLGHPIAWML FLIMFIWQIP HFLALAMKRV DEYRNAGIPM LPVVHGFEIT KRQIMIWTVC
LLPLPFYMSG LGITFMVIAT LLNIGWIVLG FYGFRKKDDI KWSVQMFVYS LNYLTILFVS
MIVVTFF