ID COXX1_BACCN Reviewed; 305 AA.
AC A7GNP0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 29-MAY-2013, entry version 46.
DE RecName: Full=Protoheme IX farnesyltransferase 1;
DE EC=2.5.1.-;
DE AltName: Full=Heme B farnesyltransferase 1;
DE AltName: Full=Heme O synthase 1;
GN Name=ctaB1; OrderedLocusNames=Bcer98_1429;
OS Bacillus cereus subsp. cytotoxis (strain NVH 391-98).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NVH 391-98;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B.,
RA Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H.,
RA Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P.,
RA Weissenbach J., Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
CC -!- FUNCTION: Converts heme B (protoheme IX) to heme O by substitution
CC of the vinyl group on carbon 2 of heme B porphyrin ring with a
CC hydroxyethyl farnesyl side group (By similarity).
CC -!- PATHWAY: Porphyrin-containing compound metabolism; heme O
CC biosynthesis; heme O from protoheme: step 1/1.
CC -!- SUBUNIT: Interacts with CtaA (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC (Potential).
CC -!- MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined
CC according to the Fischer nomenclature (By similarity).
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC Protoheme IX farnesyltransferase subfamily.
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DR EMBL; CP000764; ABS21748.1; -; Genomic_DNA.
DR RefSeq; YP_001374743.1; NC_009674.1.
DR STRING; 315749.Bcer98_1429; -.
DR EnsemblBacteria; ABS21748; ABS21748; Bcer98_1429.
DR GeneID; 5346250; -.
DR KEGG; bcy:Bcer98_1429; -.
DR PATRIC; 18931320; VBIBacCyt128034_1504.
DR eggNOG; COG0109; -.
DR HOGENOM; HOG000237290; -.
DR KO; K02301; -.
DR OMA; EPQLQHD; -.
DR ProtClustDB; PRK04375; -.
DR BioCyc; BCYT315749:GH2A-1542-MONOMER; -.
DR UniPathway; UPA00834; UER00712.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008495; F:protoheme IX farnesyltransferase activity; IEA:HAMAP.
DR GO; GO:0048034; P:heme O biosynthetic process; IEA:HAMAP.
DR HAMAP; MF_00154; CyoE_CtaB; 1; -.
DR InterPro; IPR006369; Protohaem_IX_farnesylTrfase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR Pfam; PF01040; UbiA; 1.
DR TIGRFAMs; TIGR01473; cyoE_ctaB; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 3: Inferred from homology;
KW Cell membrane; Complete proteome; Heme biosynthesis; Membrane;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 305 Protoheme IX farnesyltransferase 1.
FT /FTId=PRO_0000346024.
FT TRANSMEM 22 42 Helical; (Potential).
FT TRANSMEM 53 73 Helical; (Potential).
FT TRANSMEM 94 114 Helical; (Potential).
FT TRANSMEM 115 135 Helical; (Potential).
FT TRANSMEM 154 174 Helical; (Potential).
FT TRANSMEM 179 199 Helical; (Potential).
FT TRANSMEM 230 250 Helical; (Potential).
FT TRANSMEM 283 303 Helical; (Potential).
SQ SEQUENCE 305 AA; 34265 MW; F1A3138DA28AD247 CRC64;
MGRKKEVTNA QRQRPEILAQ TIKTGIIKSN LVPMFAGLTL ALYKYKISPF EKIPEILFAF
IGSILIIGAA GAFNNLYDRD IDSIMERTKN RPTVTGDISP KTALWLGIFM TIFGLVFLAL
TTYLAAILGF IGLFLYVVPY TMWSKRRTIY NTEIGSVSGA MPPLIGWAAI YPDVTHPAII
GLFIIMIIWQ MPHFYAIAIR KHKEYEAANV PMLPVVKGVK RTYIQTNVYL VILIIISILL
GSLSIGLMLV SLLLSILWLA LSIYGYKKMD SEKWAKSLFI FSLFHMTILF STVIIYSLVG
IFFGS
//
