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COXX_TROWT
ID   COXX_TROWT              Reviewed;         300 AA.
AC   Q83GF8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 107.
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}; OrderedLocusNames=TWT_339;
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=203267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist;
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(2003).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00154};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-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; AE014184; AAO44436.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q83GF8; -.
DR   SMR; Q83GF8; -.
DR   STRING; 203267.TWT_339; -.
DR   EnsemblBacteria; AAO44436; AAO44436; TWT_339.
DR   KEGG; twh:TWT_339; -.
DR   eggNOG; COG0109; Bacteria.
DR   HOGENOM; CLU_029631_0_1_11; -.
DR   OMA; QFFWQFP; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000002200; 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 membrane; Heme biosynthesis; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..300
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_0000327187"
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        145..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        171..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ   SEQUENCE   300 AA;  33279 MW;  1A53E25CCD345AF8 CRC64;
     MGMQGRSFAR QIRAYVSLTK PRVVELLLLT TVPTMILAQR GVPNPLSVLS VLLGGAMSAG
     AAGAFNCYID RDIDSKMSRT RNRPLVTGAL SPKASLIFAW MLCVISVLWF LLFVNWLSAL
     LSAIAVFLYA FFYSIVLKKR TPQNIVWGGL AGCMPVLIAW AAVTGSIDWP AIVLFAVVFL
     WTPPHYWPLS IHYSEDYRLT SIPMLGAIFP RKLVVLQVLL YAFAVVACTL LLIPVAHMTP
     LYGLFSAVLG AWFVYEIYRL YVRVVRGHEI KAMHIFSLSN TYLSLVFLSV GIDGVVSQLL
 
 
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