ID C6B9Q0_RHILS Unreviewed; 215 AA.
AC C6B9Q0;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Aminopyrimidine aminohydrolase {ECO:0000256|PIRNR:PIRNR003170};
DE EC=3.5.99.2 {ECO:0000256|PIRNR:PIRNR003170};
GN OrderedLocusNames=Rleg_6167 {ECO:0000313|EMBL:ACS60922.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OG Plasmid pR132504 {ECO:0000313|EMBL:ACS60922.1,
OG ECO:0000313|Proteomes:UP000002256}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS60922.1, ECO:0000313|Proteomes:UP000002256};
RN [1] {ECO:0000313|EMBL:ACS60922.1, ECO:0000313|Proteomes:UP000002256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1325 {ECO:0000313|EMBL:ACS60922.1,
RC ECO:0000313|Proteomes:UP000002256};
RC PLASMID=Plasmid pR132504 {ECO:0000313|Proteomes:UP000002256};
RX PubMed=21304718;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Copeland A., Nolan M., Han C., Brettin T., Land M., Ovchinikova G.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv. trifolii strain
RT WSM1325, an effective microsymbiont of annual Mediterranean clovers.";
RL Stand. Genomic Sci. 2:347-356(2010).
CC -!- FUNCTION: Catalyzes an amino-pyrimidine hydrolysis reaction at the C5'
CC of the pyrimidine moiety of thiamine compounds, a reaction that is part
CC of a thiamine salvage pathway. Thus, catalyzes the conversion of 4-
CC amino-5-aminomethyl-2-methylpyrimidine to 4-amino-5-hydroxymethyl-2-
CC methylpyrimidine (HMP). {ECO:0000256|PIRNR:PIRNR003170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-
CC hydroxymethyl-2-methylpyrimidine + NH4(+); Xref=Rhea:RHEA:31799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16892, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:63416; EC=3.5.99.2;
CC Evidence={ECO:0000256|PIRNR:PIRNR003170};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + thiamine = 4-amino-5-hydroxymethyl-2-methylpyrimidine +
CC 5-(2-hydroxyethyl)-4-methylthiazole + H(+); Xref=Rhea:RHEA:17509,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC ChEBI:CHEBI:17957, ChEBI:CHEBI:18385; EC=3.5.99.2;
CC Evidence={ECO:0000256|PIRNR:PIRNR003170};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|PIRNR:PIRNR003170}.
CC -!- SIMILARITY: Belongs to the TenA family.
CC {ECO:0000256|PIRNR:PIRNR003170}.
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DR EMBL; CP001626; ACS60922.1; -; Genomic_DNA.
DR RefSeq; WP_012760067.1; NC_012852.1.
DR AlphaFoldDB; C6B9Q0; -.
DR KEGG; rlg:Rleg_6167; -.
DR HOGENOM; CLU_077537_0_1_5; -.
DR OrthoDB; 3711545at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000002256; Plasmid pR132504.
DR GO; GO:0050334; F:thiaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd19358; TenA_E_Spr0628-like; 1.
DR Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR026285; TenA_E.
DR InterPro; IPR004305; Thiaminase-2/PQQC.
DR PANTHER; PTHR43198; BIFUNCTIONAL TH2 PROTEIN; 1.
DR PANTHER; PTHR43198:SF2; BIFUNCTIONAL TH2 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF03070; TENA_THI-4; 1.
DR PIRSF; PIRSF003170; Pet18p; 1.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR003170};
KW Plasmid {ECO:0000313|EMBL:ACS60922.1};
KW Thiamine biosynthesis {ECO:0000256|PIRNR:PIRNR003170}.
FT DOMAIN 21..211
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
FT ACT_SITE 206
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR003170-1"
SQ SEQUENCE 215 AA; 24204 MW; 376E7CE0AD10601C CRC64;
MAAESLSARI LRENDAVLGA MLNHRFVEDV KNDRLSKEAF ERYLVYEGAF VDSAISIFAY
AAATANTMTQ KRWLIAVLDA LANEQIAYFE RTFAGRGIDT SSFDTGIAEV EAFRAGMLEI
ARQGGFLDTV AAMFAAEWMY WTWSKEAANR PISDPLLKEW VDLHVDPNFA AQAQWLKNEL
DMAGETLEED EKARLSAIFG RAMQLEIDFH DAPYL
//
