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COXX_HALSA
ID   COXX_HALSA              Reviewed;         442 AA.
AC   Q9HRJ8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Protoheme IX farnesyltransferase;
DE            EC=2.5.1.141;
DE   AltName: Full=Heme B farnesyltransferase;
DE   AltName: Full=Heme O synthase;
GN   Name=ctaB; OrderedLocusNames=VNG_0666G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; AE004437; AAG19160.1; -; Genomic_DNA.
DR   PIR; D84224; D84224.
DR   RefSeq; WP_010902456.1; NC_002607.1.
DR   AlphaFoldDB; Q9HRJ8; -.
DR   SMR; Q9HRJ8; -.
DR   STRING; 64091.VNG_0666G; -.
DR   PaxDb; Q9HRJ8; -.
DR   EnsemblBacteria; AAG19160; AAG19160; VNG_0666G.
DR   GeneID; 5953661; -.
DR   GeneID; 62886284; -.
DR   KEGG; hal:VNG_0666G; -.
DR   PATRIC; fig|64091.14.peg.508; -.
DR   HOGENOM; CLU_030009_1_1_2; -.
DR   InParanoid; Q9HRJ8; -.
DR   OMA; MKPRLMW; -.
DR   OrthoDB; 97092at2157; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000000554; 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:0004311; F:farnesyltranstransferase activity; IBA:GO_Central.
DR   GO; GO:0008495; F:protoheme IX farnesyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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..442
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_0000327195"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..167
FT                   /note="Unknown"
FT   REGION          168..439
FT                   /note="Prenyltransferase"
SQ   SEQUENCE   442 AA;  46128 MW;  A951E2B87C9FFE30 CRC64;
     MGVYSLLVLG ATTSLTGAAS ACQTWPSCNG QWFALQSLDL VVVWGHRTAA ALTGLAVVGA
     AVLAWRTGAS RRVRTAVTLA LALYPVQVVI GAYTAMSAGA APFTGVHLTL GVGIFASLVV
     ALAWTLDAQT GDLPSAEWEG EPRHTDDGDP TQPGIVRAYV QLMKPRLMWL LCLVAGAGMA
     LASSQLGAGQ QLSAATVVLT LGGGVLSIGA SGTFNHVLER EQDEKMARTD DRPVVTDRIP
     PRNALAFGVV LGVASLAAFA AVNLLTAVLG LTAIAFYSIV YTLVLKPNTR QSTVIGGAAG
     ALPALIGWVA VTGAVGVGGV VLAGVIFLWT PAHFYNLALA YKDDYERGGF PLMPVVEGEA
     KTRRHIVYYI GATLASAVVL AELTGLGPLY AATTVLLGAV FLYFAIRLHR ERDRRAAMRS
     FHASNAYLGC LLVAVVLDTM VV
 
 
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