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THIC_XANCB
ID   THIC_XANCB              Reviewed;         625 AA.
AC   B0RP37;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Phosphomethylpyrimidine synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE            EC=4.1.99.17 {ECO:0000255|HAMAP-Rule:MF_00089};
DE   AltName: Full=Hydroxymethylpyrimidine phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE            Short=HMP-P synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE            Short=HMP-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE            Short=HMPP synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE   AltName: Full=Thiamine biosynthesis protein ThiC {ECO:0000255|HAMAP-Rule:MF_00089};
GN   Name=thiC {ECO:0000255|HAMAP-Rule:MF_00089};
GN   OrderedLocusNames=xcc-b100_0879;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
CC   -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine
CC       phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR)
CC       in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
CC       {ECO:0000255|HAMAP-Rule:MF_00089}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-
CC         methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-
CC         deoxyadenosine + CO + formate + 3 H(+) + L-methionine;
CC         Xref=Rhea:RHEA:24840, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:17245, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58354, ChEBI:CHEBI:59789, ChEBI:CHEBI:137981;
CC         EC=4.1.99.17; Evidence={ECO:0000255|HAMAP-Rule:MF_00089};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00089};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated
CC       with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000255|HAMAP-Rule:MF_00089};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00089}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00089}.
CC   -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00089}.
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DR   EMBL; AM920689; CAP50222.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RP37; -.
DR   SMR; B0RP37; -.
DR   KEGG; xca:xcc-b100_0879; -.
DR   HOGENOM; CLU_013181_2_1_6; -.
DR   OMA; TWELFRD; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001188; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.540; -; 1.
DR   HAMAP; MF_00089; ThiC; 1.
DR   InterPro; IPR037509; ThiC.
DR   InterPro; IPR025747; ThiC-associated_dom.
DR   InterPro; IPR038521; ThiC/Bza_core_dom.
DR   InterPro; IPR002817; ThiC/BzaA/B.
DR   PANTHER; PTHR30557; PTHR30557; 1.
DR   Pfam; PF13667; ThiC-associated; 1.
DR   Pfam; PF01964; ThiC_Rad_SAM; 1.
DR   SFLD; SFLDF00407; phosphomethylpyrimidine_syntha; 1.
DR   TIGRFAMs; TIGR00190; thiC; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; S-adenosyl-L-methionine;
KW   Thiamine biosynthesis; Zinc.
FT   CHAIN           1..625
FT                   /note="Phosphomethylpyrimidine synthase"
FT                   /id="PRO_1000093246"
FT   BINDING         230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         344..346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         385..388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         424
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         428
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         451
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         492
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         572
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         575
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         580
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
SQ   SEQUENCE   625 AA;  69174 MW;  43EA4014CA3404E8 CRC64;
     MNAAPTVLLQ QTQTLSAAVT QPIPGSRKIF VQGSRADLQV PMREIVLTRT PTLFGGQDNP
     PLSVYDTSGP YTDPQAAIDL AAGLAPLRAD WIAERGDTLP LEALSSSFGR GREHDARLDA
     VRFPSRRLPR VARSGANVTQ MHYARRGIIT PEMEFVAIRE NQRLEAVTDA VLRKQHPGEA
     FGAAIQQRIT PEFVREEIAR GRAILPNNIN HPESEPMIIG RNFLTKINAN IGNSAVSSGI
     AEEVEKLVWS IRWGGDTVMD LSTGKHIHET RDWIIRNSPV PIGTVPIYQA LEKVDGRAEE
     LTWEIFRDTL IEQAEQGVDY FTIHAGVLLR YVPLTARRVT GIVSRGGSIL AKWCLAHHKE
     NFLYTHFEDI CEIMKAYDVA FSLGDGLRPG CIADANDAAQ FGELETLGEL TKLAWKHDVQ
     TMIEGPGHVP MQLIKENMDK QLRECGEAPF YTLGPLTTDI APGYDHITSA IGAAMIGWFG
     TAMLCYVTPK EHLGLPNRQD VRDGIMAYKI AAHAADLAKG HPGVQVRDNA LSKARFEFRW
     DDQFHLGLDP EKAKEFHDET LPKDAHKLAH FCSMCGPHFC SMKITQDVRD YAAEHGISED
     HALEAGMQEK SGEFVAQGAQ VYRAS
 
 
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