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COXX_CAUVC
ID   COXX_CAUVC              Reviewed;         333 AA.
AC   Q9A301;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=CC_3405;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK25367.1; -; Genomic_DNA.
DR   PIR; C87671; C87671.
DR   RefSeq; NP_422199.1; NC_002696.2.
DR   AlphaFoldDB; Q9A301; -.
DR   SMR; Q9A301; -.
DR   STRING; 190650.CC_3405; -.
DR   EnsemblBacteria; AAK25367; AAK25367; CC_3405.
DR   KEGG; ccr:CC_3405; -.
DR   PATRIC; fig|190650.5.peg.3413; -.
DR   eggNOG; COG0109; Bacteria.
DR   HOGENOM; CLU_029631_0_2_5; -.
DR   OMA; QFFWQFP; -.
DR   BioCyc; CAULO:CC3405-MON; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000001816; 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 inner membrane; Cell membrane; Heme biosynthesis; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..333
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_0000327036"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        223..243
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        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ   SEQUENCE   333 AA;  35663 MW;  E49751E1962DA40D CRC64;
     MTSDSAETTP LRDSSETARW QDYFQLMKPR VMSLVVFTGL TGLLAARAPI HPVLAAIAVL
     CIAVGAGASG ALNMWYDADI DQKMRRTRGR PVPAGKIKGE EAASLGVVLS LLSVMFLGFA
     VNWLAAGLLA FTIVFYAVVY TMWLKRWTAQ NIVIGGLAGA LPPAIGWAAA TGSAPLNAWL
     MVAIIFFWTP PHFWALSLYV TTDYAKAGVP MLPVVKGARE TRKQILLYSL ILFPICLSPV
     LTGLGGPIYL AVSGLGGLVF LLLAWRVFAS KAGDAADPRV ADRALYDVTE DEKAAGAKAA
     RNLFAFSILY LFALFAALLG EAVTGVRPLE LLK
 
 
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