COXX_AFIC5
ID COXX_AFIC5 Reviewed; 313 AA.
AC B6JDB7; F8BSL0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 73.
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};
GN OrderedLocusNames=OCAR_4687, OCA5_c32620;
OS Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS (Oligotropha carboxidovorans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Afipia.
OX NCBI_TaxID=504832;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=18539730; DOI=10.1128/jb.00614-08;
RA Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.;
RT "Genome sequence of the chemolithoautotrophic bacterium Oligotropha
RT carboxidovorans OM5T.";
RL J. Bacteriol. 190:5531-5532(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=21742883; DOI=10.1128/jb.05619-11;
RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA Meyer O.;
RT "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT carboxidovorans strains OM4 and OM5.";
RL J. Bacteriol. 193:5043-5043(2011).
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; CP001196; ACI91829.1; -; Genomic_DNA.
DR EMBL; CP002826; AEI07938.1; -; Genomic_DNA.
DR RefSeq; WP_012561860.1; NC_015684.1.
DR AlphaFoldDB; B6JDB7; -.
DR SMR; B6JDB7; -.
DR STRING; 504832.OCAR_4687; -.
DR EnsemblBacteria; AEI07938; AEI07938; OCA5_c32620.
DR KEGG; oca:OCAR_4687; -.
DR KEGG; ocg:OCA5_c32620; -.
DR PATRIC; fig|504832.7.peg.3430; -.
DR eggNOG; COG0109; Bacteria.
DR HOGENOM; CLU_029631_0_2_5; -.
DR OMA; QFFWQFP; -.
DR OrthoDB; 1875497at2; -.
DR UniPathway; UPA00834; UER00712.
DR Proteomes; UP000007730; 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..313
FT /note="Protoheme IX farnesyltransferase"
FT /id="PRO_1000096923"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ SEQUENCE 313 AA; 33678 MW; E78B2FBD215CEBE1 CRC64;
MSVIEQNSVE YPPLIVSEAG VSDYIALLKP RVMSLVVFTA LVGLVIAPVH LHPVLAATSI
LCIAVGGGAA GALNMWYESD IDALMTRTAN RPIPRGRVSS PEAAAFGITL AIFSVATLGV
LVNWLAGALL AFTIFFYAVV YTMWLKRWTA QNIVIGGAAG ALPPVVAWAA ATGSLAPQPI
ILFLIIFLWT PPHFWALALF RSDDYARAKV PMLPVVAGPD ATRLQILLYT IVLVTVAILP
WPLGYFGAAY GLTSVALGAG MLWFAFNVYR YRTGTQANRA ARALFKFSLL YLFLLFAVLP
LEVAAHAVAA MIW