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COXX2_NATPD
ID   COXX2_NATPD             Reviewed;         433 AA.
AC   Q3INR7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Protoheme IX farnesyltransferase 2;
DE            EC=2.5.1.141;
DE   AltName: Full=Heme B farnesyltransferase 2;
DE   AltName: Full=Heme O synthase 2;
GN   Name=ctaB2; OrderedLocusNames=NP_4288A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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:0000250}.
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;
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; heme O biosynthesis;
CC       heme O from protoheme: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined
CC       according to the Fischer nomenclature. {ECO:0000250}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the UbiA
CC       prenyltransferase family. Protoheme IX farnesyltransferase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR936257; CAI50235.1; -; Genomic_DNA.
DR   RefSeq; WP_011323851.1; NC_007426.1.
DR   AlphaFoldDB; Q3INR7; -.
DR   SMR; Q3INR7; -.
DR   STRING; 348780.NP_4288A; -.
DR   EnsemblBacteria; CAI50235; CAI50235; NP_4288A.
DR   GeneID; 3702643; -.
DR   KEGG; nph:NP_4288A; -.
DR   eggNOG; arCOG00479; Archaea.
DR   HOGENOM; CLU_030009_1_1_2; -.
DR   OrthoDB; 97092at2157; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000002698; 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; IPR044878; UbiA_sf.
DR   PANTHER; PTHR43448; PTHR43448; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   TIGRFAMs; TIGR01473; cyoE_ctaB; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Heme biosynthesis; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..433
FT                   /note="Protoheme IX farnesyltransferase 2"
FT                   /id="PRO_0000327205"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..164
FT                   /note="Unknown"
FT   REGION          165..430
FT                   /note="Protoheme IX prenyltransferase"
SQ   SEQUENCE   433 AA;  45372 MW;  F008932238C33F64 CRC64;
     MQRFTGLVTA TTLATYLLVV LGVATELTGG VSPAAVAHYV TAGAVWLLLV AAAALAWRDS
     RLPRVKWGVT AAAVAYPAQA AVGMAVLASG GPGQLHLFGG VGVFALLLIT LTWHLDREVE
     PRERAAATAF NREGDGDDSV LLYRLPDGLR RYVELTKPRL MWLLCLLALS GMALATVTGA
     ALDGVTIAAT LFGGVLAVGA AGTFNHVYER DRDRRMNRTA DRPVATDAVG VGRATAFGVG
     LLVVSMAVLV WLVNPLAAAL TAVAVVYYAV VYTVVLKPTT TWNTVIGGGA GALPAVIGWA
     AVAGSIGLPA LLLAAVVFCW TPAHFYNLAI AYRDDYARGD YPMLPVVAGV AATRRRILYW
     LGATLLVAGA LGAVAGFGPV YALTSAVVGF GFLWTVVVQF RTESDRDAYR SFHASNAYLG
     ALLVAILVET MVI
 
 
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