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COXX_BRASO
ID   COXX_BRASO              Reviewed;         312 AA.
AC   A4Z2D2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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}; Synonyms=coxE;
GN   OrderedLocusNames=BRADO6705;
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=114615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278;
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
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; CU234118; CAL80308.1; -; Genomic_DNA.
DR   RefSeq; WP_012030175.1; NC_009445.1.
DR   AlphaFoldDB; A4Z2D2; -.
DR   SMR; A4Z2D2; -.
DR   STRING; 114615.BRADO6705; -.
DR   EnsemblBacteria; CAL80308; CAL80308; BRADO6705.
DR   KEGG; bra:BRADO6705; -.
DR   eggNOG; COG0109; Bacteria.
DR   HOGENOM; CLU_029631_0_2_5; -.
DR   OMA; QFFWQFP; -.
DR   OrthoDB; 1875497at2; -.
DR   BioCyc; BSP114615:BRADO_RS31145-MON; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000001994; 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..312
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_0000327019"
FT   TRANSMEM        34..54
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        119..139
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        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        225..245
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        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ   SEQUENCE   312 AA;  33823 MW;  63BFB9947EE645B1 CRC64;
     MSVIDQNAIA VGPRISEADV GDYIALLKPR VMSLVIFTAL IGLLIAPGHF HPVLAITSLL
     CIAVGAGASG ALNMALEGDI DSLMSRTANR PIPRGRVTRQ EALAFGITLS FFSVLTLGIL
     VNWFAGALLA FTIFFYVVIY TLWLKRWTAQ NIVIGGAAGA LPPVVAWAAV TGSIAPEPVW
     LFLIIFFWTP PHFWALALFR TDDYARAGVP MLPVVAGPDA TRLQILLYTI VLVAIAAAPW
     PLGYFDAVYG VVSLALGAGM LWLAIEVFRK RDRIPSLRAN RKLFGFSILY LFALFATLGL
     EAIARMIAPL IW
 
 
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