COXX2_BACCN
ID COXX2_BACCN Reviewed; 307 AA.
AC A7GRX3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Protoheme IX farnesyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00154};
DE EC=2.5.1.141 {ECO:0000255|HAMAP-Rule:MF_00154};
DE AltName: Full=Heme B farnesyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00154};
DE AltName: Full=Heme O synthase 2 {ECO:0000255|HAMAP-Rule:MF_00154};
GN Name=ctaB2 {ECO:0000255|HAMAP-Rule:MF_00154};
GN OrderedLocusNames=Bcer98_2647;
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABS22881.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000764; ABS22881.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041809950.1; NC_009674.1.
DR AlphaFoldDB; A7GRX3; -.
DR SMR; A7GRX3; -.
DR STRING; 315749.Bcer98_2647; -.
DR EnsemblBacteria; ABS22881; ABS22881; Bcer98_2647.
DR GeneID; 56418190; -.
DR KEGG; bcy:Bcer98_2647; -.
DR eggNOG; COG0109; Bacteria.
DR HOGENOM; CLU_029631_0_0_9; -.
DR OMA; QFFWQFP; -.
DR OrthoDB; 1875497at2; -.
DR UniPathway; UPA00834; UER00712.
DR Proteomes; UP000002300; 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; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..307
FT /note="Protoheme IX farnesyltransferase 2"
FT /id="PRO_0000346025"
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 106..128
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 132..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; 34542 MW; 53BE9BB4201D0478 CRC64;
MNHATSELHD ESAVTDVPET TRVQDLLALV KMGIVNSNTL TVFTGFWLAL HFNGLNALEH
LDKMFFTIVG SALIMAGSCS LNNYIDRDID HLMERTKNRP TVTGKYKPGF VLTLGVTLLL
LGFVFLLLTT AMAALIGFIG AFTYVVLYSL WTKRAYTLNT VVGSVSGAVP PLIGWAAIHP
SLDHPIAWML FLIMFIWQIP HFLALAMKRV DEYRNAGIPM LPVVHGFDIT KRQIMIWTVC
LLPLPFYMSG LGITFMIIAT LLNIGWIVLG FYGFRKKDDI KWSVQMFVYS LNYLTILFVS
MIVVTFF
