ID   COXX_HALWD              Reviewed;         479 AA.
AC   Q18JU9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Protoheme IX farnesyltransferase;
DE            EC=2.5.1.141;
DE   AltName: Full=Heme B farnesyltransferase;
DE   AltName: Full=Heme O synthase;
GN   Name=ctaB; OrderedLocusNames=HQ_1577A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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: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 {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined
CC       according to the Fischer nomenclature. {ECO:0000250}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the UbiA
CC       prenyltransferase family. Protoheme IX farnesyltransferase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AM180088; CAJ51705.1; -; Genomic_DNA.
DR   RefSeq; WP_011570857.1; NC_008212.1.
DR   AlphaFoldDB; Q18JU9; -.
DR   SMR; Q18JU9; -.
DR   STRING; 362976.HQ_1577A; -.
DR   EnsemblBacteria; CAJ51705; CAJ51705; HQ_1577A.
DR   GeneID; 4193878; -.
DR   KEGG; hwa:HQ_1577A; -.
DR   eggNOG; arCOG00479; Archaea.
DR   HOGENOM; CLU_030009_1_1_2; -.
DR   OMA; MKPRLMW; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000001975; 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; IPR044878; UbiA_sf.
DR   PANTHER; PTHR43448; PTHR43448; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   TIGRFAMs; TIGR01473; cyoE_ctaB; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Heme biosynthesis; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..479
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_0000327203"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        459..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..207
FT                   /note="Unknown"
FT   REGION          155..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..476
FT                   /note="Protoheme IX prenyltransferase"
SQ   SEQUENCE   479 AA;  50506 MW;  9F920A920EEFC00D CRC64;
     MAEQTATTTS AIDIRRFHGL LAGTAMGVYL LVLVGVTTAV TDAAAACAAW PICGNGWATP
     GSAIGWLAVG HRVVAVIIGI CAVVTLGVGI REHIERRVLI TVAVGSFLYP IQAAVGAVVA
     VQGPDLTLSV IHLIGGLSIF LTLAIALAWS LETETGDPTE TQTTPSKPEP DQDLPPASEY
     DPDLPADPRD RLLATLRAYI RLTKPRLMWL LCLVASAGMT LGATTTGQLT PGIALATLGG
     GVLSIGASGT FNHVLERDVD RRMQRTSDRP LATDLVPVWN AIAFGILLTV ISIVLFSWVN
     MLAAILGGVA IVFYSVVYTL LLKPNTVQNT VIGGAAGALP ALIGWVAVTG DIGFGGLALA
     TVIFLWTPAH FYNLALAYKE DYERGGFPMM PVVRGETETR KHVIWWLALT LVAAGGLATI
     EALGIVYAVA SIVFGAVFLY FAIKLHYEQT KAAAFHSFHA SNAYLGAVLI AIVFDTLVI