(data stored in SCRATCH zone)

SWISSPROT: C5BHE6_EDWI9

ID   C5BHE6_EDWI9            Unreviewed;       643 AA.
AC   C5BHE6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 59.
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   OrderedLocusNames=NT01EI_0177 {ECO:0000313|EMBL:ACR67424.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67424.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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:SAAS00703341}.
CC   -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-
CC       adenosyl-L-methionine = 4-amino-2-methyl-5-
CC       (phosphomethyl)pyrimidine + 5'-deoxyadenosine + L-methionine +
CC       formate + CO. {ECO:0000256|HAMAP-Rule:MF_00089,
CC       ECO:0000256|SAAS:SAAS00703345}.
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:SAAS00703346}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00089}.
CC   -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00089, ECO:0000256|SAAS:SAAS00774593}.
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DR   EMBL; CP001600; ACR67424.1; -; Genomic_DNA.
DR   RefSeq; WP_015869636.1; NC_012779.2.
DR   ProteinModelPortal; C5BHE6; -.
DR   STRING; 634503.NT01EI_0177; -.
DR   EnsemblBacteria; ACR67424; ACR67424; NT01EI_0177.
DR   GeneID; 7958769; -.
DR   KEGG; eic:NT01EI_0177; -.
DR   PATRIC; fig|634503.3.peg.160; -.
DR   eggNOG; ENOG4105CBF; Bacteria.
DR   eggNOG; COG0422; LUCA.
DR   HOGENOM; HOG000224484; -.
DR   KO; K03147; -.
DR   OMA; TWELFRD; -.
DR   OrthoDB; POG091H02FB; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00089; ThiC; 1.
DR   InterPro; IPR002817; ThiC.
DR   InterPro; IPR025747; ThiC-associated_dom.
DR   PANTHER; PTHR30557:SF2; PTHR30557:SF2; 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; C5BHE6.
DR   SWISS-2DPAGE; C5BHE6.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00703335};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|SAAS:SAAS00703339};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00703333};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00703349};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00703342};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00703351};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00703334};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|SAAS:SAAS00703337}.
FT   DOMAIN       30    111       ThiC-associated. {ECO:0000259|Pfam:
FT                                PF13667}.
FT   REGION      356    358       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00089}.
FT   REGION      397    400       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00089}.
FT   METAL       440    440       Zinc. {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   METAL       504    504       Zinc. {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   METAL       584    584       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   METAL       587    587       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   METAL       592    592       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00089}.
FT   BINDING     242    242       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     271    271       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     300    300       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     336    336       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     436    436       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
FT   BINDING     463    463       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00089}.
SQ   SEQUENCE   643 AA;  72058 MW;  655607D907CA1A40 CRC64;
     MSTLTHSDAP RRQRRAQAQA FIDNLQAQAF PSSQRIYLQG SRADIRVPLR EITLSPTLIG
     GTPEQPQWRD NEAIAVYDTS GAYGDQQAEI DLRRGLPGIR CAWIAERNDS EILPGRSSDY
     TRRRQADQDL ETLRFELRSP ARRARPGHRV TQLHYARQGI ITPEMEFIAL RENMGRERIR
     SAILRQQHPG IAFGAHLPDN ITPAFVRDEV AAGRAIIPAN INHPESEPMI IGRNFLVKVN
     ANIGSSSVTS SIEEEVEKLV WATRWGADTV MDLSTGRYIH ETREWILRNS PVPIGTVPIY
     QALEKVNGIA ENLDWPLVRD TLLEQAEQGV DYFTLHAGLL LRFIPMTAER LTGIVSRGGA
     IMAKWCLSHH QENFLYTHFR EICEICSAYD IALSLGDGLR PGSIQDANDQ AQFAELHTLG
     ELTQIAWEYD VQVMIEGPGH VPMHMIQRNM EEELNHCHEA PFYTLGPLTT DIAPGYDHFT
     SGIGAAMIGW FGCALLCYVT PKEHLGLPDK DDVKQGLITY KIAAHAADLA KGHPGAQIRD
     NAMSKARFEF RWEDQFNLAL DPVTARAYHD ATLPQASGKL AHFCSMCGPK FCSMKISREV
     REHAARQQEA EPGMAQMAQQ FREQGGDIYL TNIADNAPLH KEP
//

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