ID A0A4Q8R9F6_9BRAD Unreviewed; 1060 AA. AC A0A4Q8R9F6; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 27-MAR-2024, entry version 16. DE RecName: Full=Thiamine pyrimidine synthase {ECO:0000256|ARBA:ARBA00033171}; GN ORFNames=CWO89_04385 {ECO:0000313|EMBL:TAI67180.1}; OS Bradyrhizobium sp. Leo170. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Bradyrhizobium. OX NCBI_TaxID=1571199 {ECO:0000313|EMBL:TAI67180.1, ECO:0000313|Proteomes:UP000292824}; RN [1] {ECO:0000313|EMBL:TAI67180.1, ECO:0000313|Proteomes:UP000292824} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leo170 {ECO:0000313|EMBL:TAI67180.1, RC ECO:0000313|Proteomes:UP000292824}; RA Avontuur J.R., Beukes C.W., Chan W.Y., Coetzee M.P., Palmer M., Shapiro N., RA Blom J., Stepkowski T., Venter S.N., Steenkamp E.T.; RT "Genome-informed Bradyrhizobium taxonomy: where to from here?"; RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 Fe(3+) + 4 H2O + L-histidyl-[4-amino-5-hydroxymethyl-2- CC methylpyrimidine phosphate synthase] + N(6)-(pyridoxal phosphate)-L- CC lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] CC = (2S)-2-amino-5-hydroxy-4-oxopentanoyl-[4-amino-5-hydroxymethyl-2- CC methylpyrimidine phosphate synthase] + 3-oxopropanoate + 4-amino-2- CC methyl-5-(phosphooxymethyl)pyrimidine + 2 Fe(2+) + 2 H(+) + L-lysyl- CC [4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase]; CC Xref=Rhea:RHEA:65756, Rhea:RHEA-COMP:16892, Rhea:RHEA-COMP:16893, CC Rhea:RHEA-COMP:16894, Rhea:RHEA-COMP:16895, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:29979, ChEBI:CHEBI:33190, CC ChEBI:CHEBI:58354, ChEBI:CHEBI:143915, ChEBI:CHEBI:157692; CC Evidence={ECO:0000256|ARBA:ARBA00023967}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65757; CC Evidence={ECO:0000256|ARBA:ARBA00023967}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000256|ARBA:ARBA00004948}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SIMILARITY: Belongs to the NMT1/THI5 family. CC {ECO:0000256|ARBA:ARBA00009406}. 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:TAI67180.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; PSRR01000012; TAI67180.1; -; Genomic_DNA. DR AlphaFoldDB; A0A4Q8R9F6; -. DR OrthoDB; 9789782at2; -. DR Proteomes; UP000292824; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR CDD; cd07302; CHD; 1. DR Gene3D; 6.10.340.10; -; 1. DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1. DR Gene3D; 3.30.450.20; PAS domain; 1. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2. DR InterPro; IPR001054; A/G_cyclase. DR InterPro; IPR027939; NMT1/THI5. DR InterPro; IPR029787; Nucleotide_cyclase. DR InterPro; IPR015168; SsuA/THI5. DR PANTHER; PTHR31528; 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE PHOSPHATE SYNTHASE THI11-RELATED; 1. DR PANTHER; PTHR31528:SF1; 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE PHOSPHATE SYNTHASE THI11-RELATED; 1. DR Pfam; PF00211; Guanylate_cyc; 1. DR Pfam; PF09084; NMT1; 1. DR SMART; SM00044; CYCc; 1. DR SUPFAM; SSF55073; Nucleotide cyclase; 1. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1. DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1. PE 3: Inferred from homology; KW Iron {ECO:0000256|ARBA:ARBA00023004}; Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}; KW Reference proteome {ECO:0000313|Proteomes:UP000292824}; KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 342..359 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 371..396 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 713..731 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 813..945 FT /note="Guanylate cyclase" FT /evidence="ECO:0000259|PROSITE:PS50125" SQ SEQUENCE 1060 AA; 117240 MW; 0FB421FE828300D8 CRC64; MSAGLDMSAP QMLRHGRDVL FALCLMAGLV FGRVTPALAL EQVSLQLKWK HQFQFAGYYA AVEQGFYRDN GLDVSVREGG PGIDAGLEVA KGAADFGVCT TSVLVNSAER ANNVVLAVIF QHSAAIILVL HRAGIHAVSE LKGHALMDAP GSDDIAAMLK HEGVSYADLP RITHSGNPRD LLSGRADAMV AYSTNEPYLF EEYGTPYMAF SPRAYGFDFY GDNLCTSRRQ IVEHPERAAA FRAASLKGWA YALAHKEEIA DLIRRKYSAQ KSQKALLFEA TRTELLIEPH LTAIGHQSTA RWNAIARAYV DLGMLREAKL AEGLIYASDD ETWRSQMRDP RVWAFLAVVV AILLGRILYR RIARAVGALR LSAAMSGLFV LLSIPALIFI LAYNYWQNSA TINATLNDVV AKTRRASMDD ARSLINPVAA TLELLASFAA EDPEAFKKEE SRELLFKALT SAPQIDAVYV SLEDGYHRVV TRIDDDRRRS DPKIPATANW HSAYIDSFSG SPRRVRHRTF YDTWPHVVGN YDLPTIEDIR TLAGYQAAKD SRALIIEGPR PNPDTGFPVI ILRVPVVKDD AFVGCASANI TLNVLSQFLT SHRASPHSTT VIANPTEGTI IAYPDPKKGV RLENDRLEMA RLDTIDDGNV REAHRLQSDT NRDDFLFRSP QGGEEISASF ARVPGSFGKP WEVITLTPTD DFIGTLKRTN KQMVALIVAL TGIELLLIYF FSRRLSRPIE CVSRDLRSVE DLTFSYGVAT PSKIKEIKEL QAAVKLFETS LRSFSSFVPM GIVRNLIKTG TPLTLGVEQR FMTMLFTDLK DFSTLSEQMA PNDLLAQLSH YFEVVSQAIA EESGTVDKFI GDGIMAFWGA PVHRDDDVLR GCCGAMRATR RMEQLNADWS KQGRPSLHLR VGLHCAEVLV GNVGSSERLS YTVMGDGVNV AARLEGINKN FGTTICISDS VVEAVGPEIV ARPIRKVQVK GRKREFMIYE LLGIRASDDP ELKARDNATR LCDLTWEASL HFERSEFDQA ARRYEDILTA FPDDPVAKSL LAMCSAKASA //