ID A0A261FGW7_9BIFI Unreviewed; 910 AA.
AC A0A261FGW7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ORFNames=BTIS_0761 {ECO:0000313|EMBL:OZG58392.1};
OS Bifidobacterium tissieri.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1630162 {ECO:0000313|EMBL:OZG58392.1, ECO:0000313|Proteomes:UP000216444};
RN [1] {ECO:0000313|EMBL:OZG58392.1, ECO:0000313|Proteomes:UP000216444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100201 {ECO:0000313|EMBL:OZG58392.1,
RC ECO:0000313|Proteomes:UP000216444};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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:0000256|ARBA:ARBA00003175, ECO:0000256|HAMAP-Rule:MF_00089}.
CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole
CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine
CC pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
CC {ECO:0000256|ARBA:ARBA00003814}.
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:0000256|HAMAP-Rule:MF_00089};
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 coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|HAMAP-Rule:MF_00089};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948, ECO:0000256|HAMAP-Rule:MF_00089}.
CC -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000256|HAMAP-
CC Rule:MF_00089}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZG58392.1}.
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DR EMBL; MWWV01000004; OZG58392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261FGW7; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000216444; 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 CDD; cd00564; TMP_TenI; 1.
DR Gene3D; 6.10.250.620; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.20.20.540; Radical SAM ThiC family, central domain; 1.
DR HAMAP; MF_00089; ThiC; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR InterPro; IPR037509; ThiC.
DR InterPro; IPR038521; ThiC/Bza_core_dom.
DR InterPro; IPR002817; ThiC/BzaA/B.
DR NCBIfam; TIGR00190; thiC; 1.
DR PANTHER; PTHR30557:SF1; PHOSPHOMETHYLPYRIMIDINE SYNTHASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR30557; THIAMINE BIOSYNTHESIS PROTEIN THIC; 1.
DR Pfam; PF01964; ThiC_Rad_SAM; 1.
DR Pfam; PF02581; TMP-TENI; 1.
DR SFLD; SFLDF00407; phosphomethylpyrimidine_syntha; 1.
DR SFLD; SFLDG01114; phosphomethylpyrimidine_syntha; 1.
DR SFLD; SFLDS00113; Radical_SAM_Phosphomethylpyrim; 1.
DR SUPFAM; SSF51391; Thiamin phosphate synthase; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00089};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00089};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00089};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00089};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00089}; Reference proteome {ECO:0000313|Proteomes:UP000216444};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00089};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_00089};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00089}.
FT DOMAIN 25..223
FT /note="Thiamine phosphate synthase/TenI"
FT /evidence="ECO:0000259|Pfam:PF02581"
FT REGION 249..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 480
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089"
FT BINDING 509
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089"
FT BINDING 538
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089"
FT BINDING 574
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089"
FT BINDING 594..596
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089"
FT BINDING 635..638
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089"
FT BINDING 674
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089"
FT BINDING 678
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089"
FT BINDING 701
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089"
FT BINDING 742
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089"
FT BINDING 822
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089"
FT BINDING 825
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089"
FT BINDING 830
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089"
SQ SEQUENCE 910 AA; 99429 MW; 8F8FF53C25062E75 CRC64;
MQNPAQSQRF PYVSMRDGFD LSASLVVGPQ DIANSVITDV VDDALRGGVT FIRVSARHVT
ARDLAGLAQD VAQIIEDNDK SDSVALVLDG RADVVWQCRN KGIKVDGVHL GPNDVEPREA
RELLGDDAII GLSAEIEGLV PILNEIPEGC IDYIAATPFH MATPELEAAS AADEHGTLLT
VDRVNTMATA CVYPVAVGGG VTVDDIATLA GTKAAGWFVT KAITEASDPQ AATQAMVDAW
KSVRGDARHG YAKRDEKPAA ETSAEPAAEK KFTNAKDAKA AAKLTKQQRV DIAARDSKQR
DKAHIRKTKT VHFENQHGTY DLEVPYTEIK LSDTPGVGPN PPFIDYSTEG PKCDPKEGLQ
PLRLAWIKDR GDVEEYEGRR RNLADDGKRA MKRGKATKEW RGRRHNPMKA KDHPVTQMWY
ARHGIITPEM KFVAERENCD VELVRSELAS GHAVMPCNIN HPEAEPMIIG EKFLTKLNAN
MGNSAVTSSI DEEVEKLTWA TKWGADTVMD LSTGNDIHTT REWILRNSPV PIGTVPMYQA
LEKVEDDASK LSWELFRDTV IEQCEQGVDY MTIHAGVLLR FVPLTANRVT GIVSRGGSIM
AEWCLQHHQE SFLYTHFDEL CDIFAKYDVA FSLGDGLRPG SLADANDAAQ LAELMTLGEL
TQRAWAKDVQ VMIEGPGHIP FDTVRMNIEL EKAVCSGAPF YTLGPLTTDT APGYDHITSA
IGGVEIARYG TAMLCYVTPK EHLGLPNKDD VKQGVIAYKI ACHAADIAKH HPHAQDRDLA
ISKARFEFRW LDQFNLAYDP DTAIAFHDET LPAEPAKMAH FCSMCGPKFC SMAISQNIRK
KFGNAAQQEQ LVQDTISGKV PAVDVAAQAV ADSGVRSGAA MSAEDIAAGM DQMSEKFRAQ
GGKLYAKASE
//
