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COXX_LEIXX
ID   COXX_LEIXX              Reviewed;         307 AA.
AC   Q6AF34;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=Lxx11630;
OS   Leifsonia xyli subsp. xyli (strain CTCB07).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia.
OX   NCBI_TaxID=281090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTCB07;
RX   PubMed=15305603; DOI=10.1094/mpmi.2004.17.8.827;
RA   Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P.,
RA   Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D.,
RA   de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R.,
RA   Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L.,
RA   El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S.,
RA   Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M.,
RA   Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F.,
RA   Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A.,
RA   Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
RT   "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli
RT   subsp. xyli.";
RL   Mol. Plant Microbe Interact. 17:827-836(2004).
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; AE016822; AAT89011.1; -; Genomic_DNA.
DR   RefSeq; WP_011186007.1; NC_006087.1.
DR   AlphaFoldDB; Q6AF34; -.
DR   SMR; Q6AF34; -.
DR   STRING; 281090.Lxx11630; -.
DR   EnsemblBacteria; AAT89011; AAT89011; Lxx11630.
DR   KEGG; lxx:Lxx11630; -.
DR   eggNOG; COG0109; Bacteria.
DR   HOGENOM; CLU_029631_0_1_11; -.
DR   OMA; QFFWQFP; -.
DR   OrthoDB; 1875497at2; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000001306; 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..307
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_0000327066"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        244..264
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;  33628 MW;  72C1E9095DFD4816 CRC64;
     MDVAVESRVE PVGRIGVSRK VKAYISLTKP RVVELLLVTT VPTMILAARG IPNLWLVLAT
     VVGGYMSAGS AGAFNCYIDR DIDRVMRRTK NRPLVTGELS DREALVFAWA LGVASVLVLG
     FFTNWLAAGL SVAAILIYVV FYTLILKRRT TQNIVWGGVA GCMPVLIGWA VVTNSVGWAP
     VILFGVIFLW TPPHYWPLSM KYREDYKDAG VPMLAVVRGR AVVGLQVVLY AWAMVACSLL
     LIPVARMGVL YTAVALVAGG WFLYESHRLY NLAICHATVS PMRVFHGSIA YLTLIFLAVA
     IDPLLPF
 
 
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