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Database: UniProt/TrEMBL
Entry: B7GGM1_ANOFW
LinkDB: B7GGM1_ANOFW
Original site: B7GGM1_ANOFW 
ID   B7GGM1_ANOFW            Unreviewed;       301 AA.
AC   B7GGM1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   29-OCT-2014, entry version 41.
DE   RecName: Full=Protoheme IX farnesyltransferase {ECO:0000256|HAMAP-Rule:MF_00154};
DE            EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_00154};
DE   AltName: Full=Heme B farnesyltransferase {ECO:0000256|HAMAP-Rule:MF_00154};
DE   AltName: Full=Heme O synthase {ECO:0000256|HAMAP-Rule:MF_00154};
GN   Name=ctaB {ECO:0000256|HAMAP-Rule:MF_00154,
GN   ECO:0000313|EMBL:ACJ34230.1};
GN   OrderedLocusNames=Aflv_1869 {ECO:0000313|EMBL:ACJ34230.1};
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ34230.1, ECO:0000313|Proteomes:UP000000742};
RN   [1] {ECO:0000313|EMBL:ACJ34230.1, ECO:0000313|Proteomes:UP000000742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742};
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. {ECO:0000256|HAMAP-
CC       Rule:MF_00154}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; heme O
CC       biosynthesis; heme O from protoheme: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_00154}.
CC   -!- SUBUNIT: Interacts with CtaA. {ECO:0000256|HAMAP-Rule:MF_00154}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00154}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00154}.
CC   -!- MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined
CC       according to the Fischer nomenclature. {ECO:0000256|HAMAP-
CC       Rule:MF_00154}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       Protoheme IX farnesyltransferase subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00154}.
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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; PTVNDRI; -.
DR   OrthoDB; EOG6DVJQB; -.
DR   BioCyc; AFLA491915:GHEO-1940-MONOMER; -.
DR   UniPathway; UPA00834; UER00712.
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-HAMAP.
DR   GO; GO:0048034; P:heme O biosynthetic process; IEA:UniProtKB-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 {ECO:0000256|HAMAP-Rule:MF_00154,
KW   ECO:0000256|SAAS:SAAS00078075};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000742};
KW   Heme biosynthesis {ECO:0000256|HAMAP-Rule:MF_00154,
KW   ECO:0000256|SAAS:SAAS00078060};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00154,
KW   ECO:0000256|SAAS:SAAS00078054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000742};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00154,
KW   ECO:0000256|SAAS:SAAS00078085};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00154,
KW   ECO:0000256|SAAS:SAAS00078068};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00154,
KW   ECO:0000256|SAAS:SAAS00078063}.
FT   TRANSMEM     27     47       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
FT   TRANSMEM     56     76       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
FT   TRANSMEM    106    126       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
FT   TRANSMEM    127    147       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
FT   TRANSMEM    153    173       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
FT   TRANSMEM    179    199       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
FT   TRANSMEM    232    252       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
FT   TRANSMEM    280    300       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00154}.
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
//
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