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COXX_ROSCS
ID   COXX_ROSCS              Reviewed;         535 AA.
AC   A7NRY4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Rcas_4304;
OS   Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=383372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13941 / HLO8;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT   "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000804; ABU60330.1; -; Genomic_DNA.
DR   RefSeq; WP_012122751.1; NC_009767.1.
DR   AlphaFoldDB; A7NRY4; -.
DR   SMR; A7NRY4; -.
DR   STRING; 383372.Rcas_4304; -.
DR   EnsemblBacteria; ABU60330; ABU60330; Rcas_4304.
DR   KEGG; rca:Rcas_4304; -.
DR   eggNOG; COG0109; Bacteria.
DR   eggNOG; COG1612; Bacteria.
DR   HOGENOM; CLU_030009_1_1_0; -.
DR   OMA; MKPRLMW; -.
DR   OrthoDB; 727661at2; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000000263; 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; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..535
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_0000346081"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        412..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        474..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        509..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..263
FT                   /note="Unknown"
FT   REGION          264..535
FT                   /note="Protoheme IX prenyltransferase"
SQ   SEQUENCE   535 AA;  57083 MW;  28159A167A34329C CRC64;
     MRRENARVVA LPLFRTSWMV IALALVAYGA ILAGSIIPTM TGAAVSSIAT AVLGGALAMY
     TGMRTRAAPV RLGGRATAAR RSYLTLAFAA VGMLYLAVVA GALNTSAGTL WTCQTWPGCE
     ASGSGDWPAL AHRGLAGVAT ILIAALAMQT WRIRHERALR VAVACALGLM LVQNIVGLVQ
     VLLAQAGESL PLAVARLTHL GLSATAWGAL VVLVTLALRR PFPSVVAAPS PATVARPGLT
     DTTLLEGKPS LLKDYVSLTK PGVISLLILT TITSMYITPA GIPEWSLVLW TTIGGWLMAS
     GSHSINCYLD KDIDINMGRT SRRPIPSGRI PAWHALALGV VLGMIAFAIL AIFVNMLTAL
     LALAGFFYYV VIYTIWLKRT SKHNIVIGGG AGAFPPLVGW AAVTGSLAPE ALLLWLIVFF
     WTPPHFWALA LIREKDYARA GVPMLPVVAG DVETRRQIVL YTLSMLALTA LPPLLGMLGW
     SYLLMASIFG GLFLYYALKL RRDGTTATAW ALYKYSLLYL ALLFVAMVVD RAVFA
 
 
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