ID B7GGM1_ANOFW Unreviewed; 301 AA.
AC B7GGM1;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 32.
DE RecName: Full=Protoheme IX farnesyltransferase;
DE EC=2.5.1.-;
DE AltName: Full=Heme B farnesyltransferase;
DE AltName: Full=Heme O synthase;
GN Name=ctaB; OrderedLocusNames=Aflv_1869;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L.,
RA Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(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 metabolism; heme O biosynthesis; heme O from
CC protoheme: step 1/1.
CC -!- SUBUNIT: Interacts with CtaA (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC (By similarity).
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; CP000922; ACJ34230.1; -; Genomic_DNA.
DR RefSeq; YP_002316215.1; NC_011567.1.
DR STRING; 491915.Aflv_1869; -.
DR EnsemblBacteria; ACJ34230; ACJ34230; Aflv_1869.
DR GeneID; 7038122; -.
DR KEGG; afl:Aflv_1869; -.
DR PATRIC; 20955627; VBIAnoFla45531_1922.
DR eggNOG; COG0109; -.
DR HOGENOM; HOG000237290; -.
DR KO; K02301; -.
DR OMA; VGYCAVT; -.
DR ProtClustDB; PRK04375; -.
DR BioCyc; AFLA491915:GHEO-1940-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 TRANSMEM 27 47 Helical; (By similarity).
FT TRANSMEM 56 76 Helical; (By similarity).
FT TRANSMEM 106 126 Helical; (By similarity).
FT TRANSMEM 127 147 Helical; (By similarity).
FT TRANSMEM 153 173 Helical; (By similarity).
FT TRANSMEM 179 199 Helical; (By similarity).
FT TRANSMEM 232 252 Helical; (By similarity).
FT TRANSMEM 280 300 Helical; (By similarity).
SQ SEQUENCE 301 AA; 33238 MW; 7B75200F59976464 CRC64;
MADVVEDVKP TKLQSGVFKD VLAVVKIGIV NSNLITTFTG LWLALHFTGK GFLSNLHIVF
FALVGSALVI AGSCALNNFI DRDIDHLMER TKGRPTVSGS VDPKRVLWFG VLLVVIGTLS
LLMTTVTAAV IGLVGVVTYV FLYTMWSKRS NTFNTVIGSI SGAVPPVIGW TAVDDGFHIV
PVILFLLMFL WQPPHFLALA MKRCEEYRAA GIPMLPVVHG FAMTKRQIVI WIVALLPLPF
YLFSLGVPFL VIATLLNVGW LALGLAGFKM KDDMKWAKWM FIYSLNYLTI LFVTMVIVTI
D
//
