(data stored in SCRATCH zone)

SWISSPROT: C6WHU1_ACTMD

ID   C6WHU1_ACTMD            Unreviewed;       547 AA.
AC   C6WHU1;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 63.
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=Amir_0425 {ECO:0000313|EMBL:ACU34392.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34392.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34392.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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   -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00089, ECO:0000256|SAAS:SAAS00774593}.
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DR   EMBL; CP001630; ACU34392.1; -; Genomic_DNA.
DR   RefSeq; WP_012783055.1; NC_013093.1.
DR   ProteinModelPortal; C6WHU1; -.
DR   STRING; 446462.Amir_0425; -.
DR   EnsemblBacteria; ACU34392; ACU34392; Amir_0425.
DR   KEGG; ami:Amir_0425; -.
DR   eggNOG; ENOG4105CBF; Bacteria.
DR   eggNOG; COG0422; LUCA.
DR   HOGENOM; HOG000224483; -.
DR   KO; K03147; -.
DR   OMA; TWELFRD; -.
DR   OrthoDB; POG091H02FB; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000002213; 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; C6WHU1.
DR   SWISS-2DPAGE; C6WHU1.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00089,
KW   ECO:0000256|SAAS:SAAS00703335};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
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:UP000002213};
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       18     80       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;  59982 MW;  C334974791E48770 CRC64;
     MTALGDGSVR PSVTTGPIRG SRKVHRDAED GVRVPFRRVE LTDGDHFDLY DTSGPYTAGD
     VDVREGLEKI RAGWISAREP VNGAATQLAW ARAGVITPEM RFAALRESLA PEFVRDEVAA
     GRAVIPANRN HPESEPMVIG KGFLVKVNAN IGNSAVTSSV EEEVEKMVWA TRWGADTVMD
     LSTGKRIHET REWIIRNSPV PVGTVPIYQA LEKVGGDPAA LSWEVYRDTV VEQAEQGVDY
     MTVHAGVLLR YVPLTARRVT GIVSRGGSIM AAWCLAHHEE SFLYTRFAEL CEILRQYDVT
     FSLGDGLRPG SIADANDEAQ FAELRTLGEL ARVARAHDVQ VMIEGPGHVP LHKIAENVRL
     EQEWCDGAPF YTLGPLATDV APAYDHITSA IGAAQIGALG TAMLCYVTPK EHLGLPDRDD
     VKTGVITYKI AAHAADLAKG HPGAQAWDDA LSRARFEFRW EDQFNLSLDP DTAREFHDRT
     LPAEPAKTAH FCSMCGPKFC SMRITQDVRR YAEERGLSTV EAIEAGMAEK AHEFDDRGGK
     VYLPVVD
//

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