(data stored in SCRATCH zone)

SWISSPROT: A4F733_SACEN

ID   A4F733_SACEN            Unreviewed;       547 AA.
AC   A4F733;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 89.
DE   RecName: Full=Phosphomethylpyrimidine synthase {ECO:0000256|HAMAP-Rule:MF_00089};
DE            EC=4.1.99.17 {ECO:0000256|HAMAP-Rule:MF_00089};
DE   AltName: Full=Hydroxymethylpyrimidine phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00089};
DE            Short=HMP-P synthase {ECO:0000256|HAMAP-Rule:MF_00089};
DE            Short=HMP-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00089};
DE            Short=HMPP synthase {ECO:0000256|HAMAP-Rule:MF_00089};
DE   AltName: Full=Thiamine biosynthesis protein ThiC {ECO:0000256|HAMAP-Rule:MF_00089};
GN   Name=thiC {ECO:0000256|HAMAP-Rule:MF_00089,
GN   ECO:0000313|EMBL:CAL99857.1};
GN   OrderedLocusNames=SACE_0511 {ECO:0000313|EMBL:CAL99857.1};
GN   ORFNames=A8924_0909 {ECO:0000313|EMBL:PFG93659.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99857.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99857.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99857.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93659.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93659.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine
CC       phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide
CC       (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent
CC       reaction. {ECO:0000256|HAMAP-Rule:MF_00089,
CC       ECO:0000256|SAAS:SAAS00956671}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-
CC         adenosyl-L-methionine = 4-amino-2-methyl-5-
CC         (phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate
CC         + 3 H(+) + L-methionine; Xref=Rhea:RHEA:24840,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:17245,
CC         ChEBI:CHEBI:17319, ChEBI:CHEBI:57844, ChEBI:CHEBI:58354,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:137981; EC=4.1.99.17;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00089,
CC         ECO:0000256|SAAS:SAAS01115025};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00089};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is
CC       coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC       methionine. {ECO:0000256|HAMAP-Rule:MF_00089};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|SAAS:SAAS00956679}.
CC   -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00089, ECO:0000256|SAAS:SAAS00976596}.
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DR   EMBL; AM420293; CAL99857.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93659.1; -; Genomic_DNA.
DR   STRING; 405948.SACE_0511; -.
DR   EnsemblBacteria; CAL99857; CAL99857; SACE_0511.
DR   KEGG; sen:SACE_0511; -.
DR   eggNOG; ENOG4105CBF; Bacteria.
DR   eggNOG; COG0422; LUCA.
DR   HOGENOM; HOG000224483; -.
DR   KO; K03147; -.
DR   OMA; LTWELFR; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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_sf.
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;
DR   PRODOM; A4F733.
DR   SWISS-2DPAGE; A4F733.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00923200};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|SAAS:SAAS00923199};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00923226};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00923244};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00923246};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00923219};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00956670};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|SAAS:SAAS00923206}.
FT   DOMAIN       20     83       ThiC-associated. {ECO:0000259|Pfam:
FT                                PF13667}.
FT   REGION      264    266       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00089}.
FT   REGION      305    308       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00089}.
FT   METAL       348    348       Zinc. {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   METAL       412    412       Zinc. {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   METAL       492    492       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   METAL       495    495       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   METAL       500    500       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   BINDING     150    150       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     179    179       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     208    208       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     244    244       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     344    344       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     371    371       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
SQ   SEQUENCE   547 AA;  60444 MW;  E816DDE03F7E65FA CRC64;
     MADVRPNLSS DHHSVTTGPI SGSRKVHHTT ESGLKVPFRR IELSNGEHLD VYDTSGAYTD
     DDVQVDVHSG LHRLRAGWTD GREHRTQLGW AKAGVVTREM EFIAAREGVS PEFVRDEVAS
     GRAVIPANRC HPESEPMIIG KNFLVKVNAN IGNSAVTSSV EEEVEKMVWA TRWGADTVMD
     LSTGKRIHET REQILRNSPV PIGTVPIYQA LEKVNGDPEK LTWEIYRDTV IEQCEQGVDY
     MTVHAGVLLR YVPLTAQRVT GIVSRGGSIM AAWCLAHHRE SFLYTHFSEL CEILRDYDVT
     FSLGDGLRPG SIADANDRAQ FAELETLGEL THIARDMDVQ VMIEGPGHVP MHKIVENVKL
     EEELCGEAPF YTLGPLTTDI APAYDHITSG IGAAVIAQAG TAMLCYVTPK EHLGLPNRDD
     VKVGVITYKI AAHAADLAKG HPRAQDWDDA LSKARFEFRW NDQFNLSLDP DTARAYHDET
     LPAEPAKTAH FCSMCGPKFC SMKITQDVRK YAEERGLTSV EAIEAGMREK SDEFSESGGK
     VYLPVVG
//

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