ID D2B053_STRRD Unreviewed; 231 AA.
AC D2B053;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Aminopyrimidine aminohydrolase {ECO:0000256|PIRNR:PIRNR003170};
DE EC=3.5.99.2 {ECO:0000256|PIRNR:PIRNR003170};
GN OrderedLocusNames=Sros_6338 {ECO:0000313|EMBL:ACZ89059.1};
OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS 9100).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ89059.1, ECO:0000313|Proteomes:UP000002029};
RN [1] {ECO:0000313|EMBL:ACZ89059.1, ECO:0000313|Proteomes:UP000002029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC {ECO:0000313|Proteomes:UP000002029};
RX PubMed=21304675; DOI=10.4056/sigs.631049;
RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptosporangium roseum type strain (NI
RT 9100).";
RL Stand. Genomic Sci. 2:29-37(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; CP001814; ACZ89059.1; -; Genomic_DNA.
DR RefSeq; WP_012892794.1; NC_013595.1.
DR AlphaFoldDB; D2B053; -.
DR STRING; 479432.Sros_6338; -.
DR KEGG; sro:Sros_6338; -.
DR eggNOG; COG0819; Bacteria.
DR HOGENOM; CLU_077537_0_1_11; -.
DR OrthoDB; 3711545at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000002029; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000002029};
KW Thiamine biosynthesis {ECO:0000256|PIRNR:PIRNR003170}.
FT DOMAIN 28..229
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
FT ACT_SITE 221
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR003170-1"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003170-2"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003170-2"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003170-2"
SQ SEQUENCE 231 AA; 25791 MW; 3CA9C64DBFA04414 CRC64;
MDLVPYDEWR ASAVDPAFSE WLRSLSEPEW TAVVNHPFAA SITRGDVADD DMRRYLIQDF
QFVDSFTALL GAAVASADNF ESRVPFGRFL GETATTEEKT YFHRALAALG ATPADLASPP
LEPVTADFRA LMDEARTSLD YPLVLAVLSV AEWSYLGWAS LAGEPSPDNF VHREWIELHE
GPVFRAWVGF LRGELDRLGP GLTSEGQLRV LDFFRRAVRL ELRFFDMAAG A
//
