COXX_ALKPO
ID COXX_ALKPO Reviewed; 312 AA.
AC Q04444; D3FU51;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protoheme IX farnesyltransferase;
DE EC=2.5.1.141;
DE AltName: Full=Heme O synthase;
GN Name=ctaB; OrderedLocusNames=BpOF4_00920;
OS Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4)
OS (Bacillus pseudofirmus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX NCBI_TaxID=398511;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7678007; DOI=10.1016/s0021-9258(18)54205-8;
RA Quirk P.G., Hicks D.B., Krulwich T.A.;
RT "Cloning of the cta operon from alkaliphilic Bacillus firmus OF4 and
RT characterization of the pH-regulated cytochrome caa3 oxidase it encodes.";
RL J. Biol. Chem. 268:678-685(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2126 / JCM 17055 / OF4;
RX PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J.,
RA Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B.,
RA Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y.,
RA Hu F.Z., Krulwich T.A.;
RT "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that
RT support the ability to grow in an external pH range from 7.5 to 11.4.";
RL Environ. Microbiol. 13:3289-3309(2011).
CC -!- FUNCTION: Converts protoheme IX and farnesyl diphosphate to heme O.
CC {ECO:0000250}.
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;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; heme O biosynthesis;
CC heme O from protoheme: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; M94110; AAA22363.1; -; Genomic_DNA.
DR EMBL; CP001878; ADC48253.1; -; Genomic_DNA.
DR RefSeq; WP_012959535.1; NC_013791.2.
DR AlphaFoldDB; Q04444; -.
DR SMR; Q04444; -.
DR STRING; 398511.BpOF4_00920; -.
DR EnsemblBacteria; ADC48253; ADC48253; BpOF4_00920.
DR KEGG; bpf:BpOF4_00920; -.
DR eggNOG; COG0109; Bacteria.
DR HOGENOM; CLU_029631_0_0_9; -.
DR OMA; QFFWQFP; -.
DR OrthoDB; 1875497at2; -.
DR UniPathway; UPA00834; UER00712.
DR Proteomes; UP000001544; 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..312
FT /note="Protoheme IX farnesyltransferase"
FT /id="PRO_0000162904"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..69
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..312
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 312 AA; 34325 MW; 2B6C3CD518EF6128 CRC64;
MNKSNTAIDP TNVIEAGPDS SVADVQQKSW KDYLVLAKQG IVTSNLITTF AGIYLAIVYT
GTVFTMHLDT MIFALLGAAL VMAGGCTLNN YIDRDIDHLM ERTKERPTVT GRFSAKHVLL
VGLAQAALGI IFLALTTPTA AVIGLIGLFI YVVLYTMWTK RTTTLNTIVG SFSGAVPPLI
GWAAIDGGLH LYAWLLFFIM FLWQPPHFLA LAMKRVEEYR AAGIPMLPVV AGFEMTKRQM
VVYVAALLPV SLMLYPFGLV YTIVAAVLGV GWLALGIAGF KMKDDIKWAR LMFVYSLNYL
TILFVLMVIV HF
