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Multifunctional fusion protein [Includes: Phosphomethylpyrimidine synthase (EC 4.1.99.17) (Hydroxymethylpyrimidine phosphate synthase) (Thiamine biosynthesis protein ThiC) (HMP-P synthase) (HMP-phosphate synthase) (HMPP synthase); Thiamine-phosphate synthase (TP synthase) (TPS) (EC 2.5.1.3) (Thiamine-phosphate pyrophosphorylase) (TMP pyrophosphorylase) (TMP-PPase)]

 V6XXG4_BIFLN            Unreviewed;       917 AA.
V6XXG4;
19-FEB-2014, integrated into UniProtKB/TrEMBL.
19-FEB-2014, sequence version 1.
25-OCT-2017, entry version 32.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|HAMAP-Rule:MF_00097};
Includes:
RecName: Full=Phosphomethylpyrimidine synthase {ECO:0000256|HAMAP-Rule:MF_00089};
EC=4.1.99.17 {ECO:0000256|HAMAP-Rule:MF_00089};
AltName: Full=Hydroxymethylpyrimidine phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00089};
AltName: Full=Thiamine biosynthesis protein ThiC {ECO:0000256|HAMAP-Rule:MF_00089};
Short=HMP-P synthase {ECO:0000256|HAMAP-Rule:MF_00089};
Short=HMP-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00089};
Short=HMPP synthase {ECO:0000256|HAMAP-Rule:MF_00089};
Includes:
RecName: Full=Thiamine-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00097};
Short=TP synthase {ECO:0000256|HAMAP-Rule:MF_00097};
Short=TPS {ECO:0000256|HAMAP-Rule:MF_00097};
EC=2.5.1.3 {ECO:0000256|HAMAP-Rule:MF_00097};
AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00097};
Short=TMP pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00097};
Short=TMP-PPase {ECO:0000256|HAMAP-Rule:MF_00097};
Name=thiC {ECO:0000256|HAMAP-Rule:MF_00089,
ECO:0000313|EMBL:ESV33883.1};
Synonyms=thiE {ECO:0000256|HAMAP-Rule:MF_00097,
ECO:0000313|EMBL:ESV33883.1};
ORFNames=BLONG_1438 {ECO:0000313|EMBL:ESV33883.1};
Bifidobacterium longum E18.
Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
Bifidobacterium.
NCBI_TaxID=1322347 {ECO:0000313|EMBL:ESV33883.1, ECO:0000313|Proteomes:UP000018321};
[1] {ECO:0000313|Proteomes:UP000018321}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=24356845;
Zhurina D., Dudnik A., Waidmann M.S., Grimm V., Westermann C.,
Breitinger K.J., Yuan J., van Sinderen D., Riedel C.U.;
"High-Quality Draft Genome Sequence of Bifidobacterium longum E18,
Isolated from a Healthy Adult.";
Genome Announc. 1:e01084-13(2013).
-!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine
phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide
(AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent
reaction. {ECO:0000256|HAMAP-Rule:MF_00089,
ECO:0000256|SAAS:SAAS00723510}.
-!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole
monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl
pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate
(TMP). {ECO:0000256|HAMAP-Rule:MF_00097,
ECO:0000256|SAAS:SAAS00709677}.
-!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine +
2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate
= diphosphate + thiamine phosphate + CO(2). {ECO:0000256|HAMAP-
Rule:MF_00097, ECO:0000256|SAAS:SAAS00709728}.
-!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine +
2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate = diphosphate +
thiamine phosphate + CO(2). {ECO:0000256|HAMAP-Rule:MF_00097,
ECO:0000256|SAAS:SAAS00709678}.
-!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine +
4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine
phosphate. {ECO:0000256|HAMAP-Rule:MF_00097,
ECO:0000256|SAAS:SAAS00709726}.
-!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-
adenosyl-L-methionine = 4-amino-2-methyl-5-
(phosphomethyl)pyrimidine + 5'-deoxyadenosine + L-methionine +
formate + CO. {ECO:0000256|HAMAP-Rule:MF_00089,
ECO:0000256|SAAS:SAAS00723460}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00097};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_00097};
-!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
thiamine phosphate from 4-amino-2-methyl-5-
diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-
thiazole: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00097,
ECO:0000256|SAAS:SAAS00709682}.
-!- SIMILARITY: Belongs to the ThiC family. {ECO:0000256|HAMAP-
Rule:MF_00089}.
-!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
{ECO:0000256|HAMAP-Rule:MF_00097}.
-----------------------------------------------------------------------
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EMBL; CM002287; ESV33883.1; -; Genomic_DNA.
RefSeq; WP_023658466.1; NZ_CM002287.1.
ProteinModelPortal; V6XXG4; -.
EnsemblBacteria; ESV33883; ESV33883; BLONG_1438.
PATRIC; fig|1322347.4.peg.1402; -.
UniPathway; UPA00060; UER00141.
Proteomes; UP000018321; Chromosome.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-UniRule.
GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd00564; TMP_TenI; 1.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_00089; ThiC; 1.
HAMAP; MF_00097; TMP_synthase; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR036206; ThiamineP_synth_sf.
InterPro; IPR022998; ThiamineP_synth_TenI.
InterPro; IPR002817; ThiC.
InterPro; IPR025747; ThiC-associated_dom.
InterPro; IPR034291; TMP_synthase.
PANTHER; PTHR30557; PTHR30557; 1.
Pfam; PF13667; ThiC-associated; 1.
Pfam; PF01964; ThiC_Rad_SAM; 1.
Pfam; PF02581; TMP-TENI; 1.
SFLD; SFLDF00407; phosphomethylpyrimidine_syntha; 1.
SUPFAM; SSF51391; SSF51391; 1.
TIGRFAMs; TIGR00190; thiC; 1.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00089,
ECO:0000256|SAAS:SAAS00923200};
Complete proteome {ECO:0000313|Proteomes:UP000018321};
Iron {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|SAAS:SAAS00923200};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00089,
ECO:0000256|SAAS:SAAS00923200};
Lyase {ECO:0000256|HAMAP-Rule:MF_00089,
ECO:0000256|SAAS:SAAS00923244};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00097,
ECO:0000256|SAAS:SAAS00709725};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00089,
ECO:0000256|SAAS:SAAS00923200};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00089,
ECO:0000256|SAAS:SAAS00923219};
Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00089,
ECO:0000256|SAAS:SAAS00709833};
Transferase {ECO:0000256|HAMAP-Rule:MF_00097,
ECO:0000256|SAAS:SAAS00709679, ECO:0000313|EMBL:ESV33883.1};
Zinc {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|SAAS:SAAS00923206}.
DOMAIN 19 219 TMP-TENI. {ECO:0000259|Pfam:PF02581}.
DOMAIN 327 381 ThiC-associated.
{ECO:0000259|Pfam:PF13667}.
REGION 48 52 HMP-PP binding. {ECO:0000256|HAMAP-
Rule:MF_00097}.
REGION 157 159 THZ-P binding. {ECO:0000256|HAMAP-
Rule:MF_00097}.
REGION 216 217 THZ-P binding. {ECO:0000256|HAMAP-
Rule:MF_00097}.
REGION 601 603 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00089}.
REGION 642 645 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00089}.
METAL 85 85 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00097}.
METAL 109 109 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00097}.
METAL 685 685 Zinc. {ECO:0000256|HAMAP-Rule:MF_00089}.
METAL 749 749 Zinc. {ECO:0000256|HAMAP-Rule:MF_00089}.
METAL 829 829 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00089}.
METAL 832 832 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00089}.
METAL 837 837 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00089}.
BINDING 84 84 HMP-PP. {ECO:0000256|HAMAP-
Rule:MF_00097}.
BINDING 128 128 HMP-PP. {ECO:0000256|HAMAP-
Rule:MF_00097}.
BINDING 160 160 HMP-PP. {ECO:0000256|HAMAP-
Rule:MF_00097}.
BINDING 196 196 THZ-P; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00097}.
BINDING 487 487 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00089}.
BINDING 516 516 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00089}.
BINDING 545 545 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00089}.
BINDING 581 581 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00089}.
BINDING 681 681 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00089}.
BINDING 708 708 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00089}.
SEQUENCE 917 AA; 100251 MW; 7802255376B69AA0 CRC64;
MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT
DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG
DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI
NTICVASEFP VVVGGGVTAA DMAMLAGTKA AGWFAVSAIA GAENPEEAAR TMVEGWKAVR
GDKKHGYAPR VVTHTPATDT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA
ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC
DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH
PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF
LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG
TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV
SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE
LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG
YDHITSAIGA TEIARYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH
AVDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA
ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LATAKANVDN GVVSANVLSP EEILAGMDAM
SEKYTAQGGK LYSTAQE


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