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UBIX_CHLTR
ID   UBIX_CHLTR              Reviewed;         192 AA.
AC   O84222;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Flavin prenyltransferase UbiX {ECO:0000255|HAMAP-Rule:MF_01984};
DE            EC=2.5.1.129 {ECO:0000255|HAMAP-Rule:MF_01984};
GN   Name=ubiX {ECO:0000255|HAMAP-Rule:MF_01984}; OrderedLocusNames=CT_220;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
CC   -!- FUNCTION: Flavin prenyltransferase that catalyzes the synthesis of the
CC       prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic
CC       acid decarboxylase UbiD. The prenyltransferase is metal-independent and
CC       links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to
CC       the flavin N5 and C6 atoms of FMN. {ECO:0000255|HAMAP-Rule:MF_01984}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2;
CC         Xref=Rhea:RHEA:37743, ChEBI:CHEBI:43474, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:87467, ChEBI:CHEBI:88052; EC=2.5.1.129;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01984};
CC   -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01984}.
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DR   EMBL; AE001273; AAC67812.1; -; Genomic_DNA.
DR   PIR; C71543; C71543.
DR   RefSeq; NP_219724.1; NC_000117.1.
DR   RefSeq; WP_009871566.1; NC_000117.1.
DR   PDB; 7KM2; X-ray; 2.19 A; A/B/C/D/E/F/G/H/I/J/K/L=1-192.
DR   PDB; 7KM3; X-ray; 2.26 A; A/B/C/D/E/F/G/H/I/J/K/L=1-192.
DR   PDBsum; 7KM2; -.
DR   PDBsum; 7KM3; -.
DR   AlphaFoldDB; O84222; -.
DR   SMR; O84222; -.
DR   STRING; 813.O172_01185; -.
DR   EnsemblBacteria; AAC67812; AAC67812; CT_220.
DR   GeneID; 884904; -.
DR   KEGG; ctr:CT_220; -.
DR   PATRIC; fig|272561.5.peg.235; -.
DR   HOGENOM; CLU_074522_0_1_0; -.
DR   InParanoid; O84222; -.
DR   OMA; GATHIQD; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR   GO; GO:0106141; F:flavin prenyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1950; -; 1.
DR   HAMAP; MF_01984; ubiX_pad; 1.
DR   InterPro; IPR036551; Flavin_trans-like.
DR   InterPro; IPR003382; Flavoprotein.
DR   InterPro; IPR004507; UbiX-like.
DR   PANTHER; PTHR43374; PTHR43374; 1.
DR   Pfam; PF02441; Flavoprotein; 1.
DR   SUPFAM; SSF52507; SSF52507; 1.
DR   TIGRFAMs; TIGR00421; ubiX_pad; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Flavoprotein; FMN; Prenyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..192
FT                   /note="Flavin prenyltransferase UbiX"
FT                   /id="PRO_0000134961"
FT   BINDING         10..12
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         36
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         92..95
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         127
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         157
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         173
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:7KM2"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:7KM3"
FT   HELIX           14..26
FT                   /evidence="ECO:0007829|PDB:7KM2"
FT   STRAND          30..35
FT                   /evidence="ECO:0007829|PDB:7KM2"
FT   HELIX           37..40
FT                   /evidence="ECO:0007829|PDB:7KM2"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:7KM2"
FT   HELIX           58..63
FT                   /evidence="ECO:0007829|PDB:7KM2"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:7KM2"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:7KM2"
FT   STRAND          85..91
FT                   /evidence="ECO:0007829|PDB:7KM2"
FT   HELIX           93..101
FT                   /evidence="ECO:0007829|PDB:7KM2"
FT   HELIX           107..117
FT                   /evidence="ECO:0007829|PDB:7KM2"
FT   STRAND          122..126
FT                   /evidence="ECO:0007829|PDB:7KM2"
FT   HELIX           133..144
FT                   /evidence="ECO:0007829|PDB:7KM2"
FT   HELIX           163..177
FT                   /evidence="ECO:0007829|PDB:7KM2"
SQ   SEQUENCE   192 AA;  20883 MW;  3CC252DC2137D9F5 CRC64;
     MKRYVVGISG ASGIVLAVTL VSELARLGHH IDVIISPSAQ KTLYYELDTK SFLSTIPQNF
     HNQIVLHHIS SIESSVSSGS NTIDATIIVP CSVATVAAIS CGLADNLLRR VADVALKEKR
     PLILVPREAP LSAIHLENLL KLAQNGAVIL PPMPIWYFKP QTAEDIANDI VGKILAILQL
     DSPLIKRWEN PR
 
 
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