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COXX1_NATPD
ID   COXX1_NATPD             Reviewed;         454 AA.
AC   Q3IRC9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Protoheme IX farnesyltransferase 1;
DE            EC=2.5.1.141;
DE   AltName: Full=Heme B farnesyltransferase 1;
DE   AltName: Full=Heme O synthase 1;
GN   Name=ctaB1; OrderedLocusNames=NP_2446A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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; CR936257; CAI49314.1; -; Genomic_DNA.
DR   RefSeq; WP_011322940.1; NC_007426.1.
DR   AlphaFoldDB; Q3IRC9; -.
DR   SMR; Q3IRC9; -.
DR   STRING; 348780.NP_2446A; -.
DR   EnsemblBacteria; CAI49314; CAI49314; NP_2446A.
DR   GeneID; 3702642; -.
DR   KEGG; nph:NP_2446A; -.
DR   eggNOG; arCOG00479; Archaea.
DR   HOGENOM; CLU_030009_1_1_2; -.
DR   OMA; MKPRLMW; -.
DR   OrthoDB; 97092at2157; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000002698; 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..454
FT                   /note="Protoheme IX farnesyltransferase 1"
FT                   /id="PRO_0000327204"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        377..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        398..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        433..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..186
FT                   /note="Unknown"
FT   REGION          137..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..451
FT                   /note="Protoheme IX prenyltransferase"
SQ   SEQUENCE   454 AA;  46819 MW;  6D7B6240C3F5AC27 CRC64;
     MRTTGFSGLL SATVVGVYVL VVVGATAALA DAAAACQGWP LCGGDLSDPS VPVAVLHRGV
     AAVVGLLVIA TAVVGWSETT ARVKTTLALA LALYPAQVVL GALVATGSAL ANLHLFVAMA
     IFAVLVVGLA WHLEAETGSD DAPESPPELA PPVDEEPAAT EQPALSGLAR AKATARAYFE
     LTKPRLMWLL CLVAGAGMVI AGTPTVRTVV FTLGGGVLAI GASGTFNHVL ERDIDRRMER
     TSDRPIATHE VPVANALAFG GLLAVASLWA FLSVNLLAAA LGLAAIAFYS VVYTLILKPN
     TVQNTVIGGA AGALPALIGY AAVTGTIGIG GLVLAAVIFL WTPAHFYNLA LAYKDDYERG
     GFPMMPVVRG ETETRKHIVF YLGATLLGAG ALAAVTDLGW LYAATAVLAA GVFLWAVVEL
     HYEQTDRAAF RSFHASNAYL GLVLVAILID SLAV
 
 
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