COXX_DESVV
ID COXX_DESVV Reviewed; 287 AA.
AC A1VD51;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=Dvul_1349;
OS Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=391774;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DP4;
RX PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA Stahl D.A.;
RT "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT plasticity.";
RL Environ. Microbiol. 11:2244-2252(2009).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00154}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC 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; CP000527; ABM28367.1; -; Genomic_DNA.
DR RefSeq; WP_011792210.1; NC_008751.1.
DR AlphaFoldDB; A1VD51; -.
DR SMR; A1VD51; -.
DR EnsemblBacteria; ABM28367; ABM28367; Dvul_1349.
DR KEGG; dvl:Dvul_1349; -.
DR HOGENOM; CLU_029631_3_1_7; -.
DR OMA; PPLMGYC; -.
DR UniPathway; UPA00834; UER00712.
DR Proteomes; UP000009173; 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 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; IPR044878; UbiA_sf.
DR PANTHER; PTHR43448; PTHR43448; 1.
DR Pfam; PF01040; UbiA; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Heme biosynthesis; Membrane;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..287
FT /note="Protoheme IX farnesyltransferase"
FT /id="PRO_0000346042"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ SEQUENCE 287 AA; 30907 MW; 2E0A8AC5134D54A5 CRC64;
MGRCTIADVA MLIRWRVSLM VAGATFFGAM LAVPHVTITH LLASLATFLL AGGCSAINQV
QEADLDAVIP RTASRPIPCG RIGHMYGSLM GLALVTVGWM VLCLAGGLTS LLVGIGIVAV
YNGLYTPLKR RTSFALLVGA AAGAMPPVVG WLAVGGHPAS PMLVVVYTLY LLWQIPHFWL
HAARDREAYR KARLPLPLLS LPHERYARLL KVWFHAYAVA VLMVPAFPLL EGVGMRIMVT
LCGIALLFAA MLAVRKRRVA LHIADAVLCA VMVVLLIDRL AIPVSLF
