ID A0A0X8HHK3_9GAMM Unreviewed; 231 AA.
AC A0A0X8HHK3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aminopyrimidine aminohydrolase {ECO:0000256|PIRNR:PIRNR003170};
DE EC=3.5.99.2 {ECO:0000256|PIRNR:PIRNR003170};
GN Name=tenA_2 {ECO:0000313|EMBL:AMD02758.1};
GN ORFNames=LOKO_03718 {ECO:0000313|EMBL:AMD02758.1};
OS Halomonas chromatireducens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=507626 {ECO:0000313|EMBL:AMD02758.1, ECO:0000313|Proteomes:UP000063387};
RN [1] {ECO:0000313|EMBL:AMD02758.1, ECO:0000313|Proteomes:UP000063387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD02758.1,
RC ECO:0000313|Proteomes:UP000063387};
RX PubMed=26988058;
RA Sharko F.S., Shapovalova A.A., Tsygankova S.V., Komova A.V.,
RA Boulygina E.S., Teslyuk A.B., Gotovtsev P.M., Namsaraev Z.B.,
RA Khijniak T.V., Nedoluzhko A.V., Vasilov R.G.;
RT "Draft Genome Sequence of 'Halomonas chromatireducens' Strain AGD 8-3, a
RT Haloalkaliphilic Chromate- and Selenite-Reducing Gammaproteobacterium.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|EMBL:AMD02758.1, ECO:0000313|Proteomes:UP000063387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD02758.1,
RC ECO:0000313|Proteomes:UP000063387};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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; CP014226; AMD02758.1; -; Genomic_DNA.
DR RefSeq; WP_066452110.1; NZ_CP014226.1.
DR AlphaFoldDB; A0A0X8HHK3; -.
DR STRING; 507626.LOKO_03718; -.
DR KEGG; hco:LOKO_03718; -.
DR PATRIC; fig|507626.3.peg.3719; -.
DR OrthoDB; 3711545at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000063387; 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, ECO:0000313|EMBL:AMD02758.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000063387};
KW Thiamine biosynthesis {ECO:0000256|PIRNR:PIRNR003170}.
FT DOMAIN 29..225
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 60
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; 26195 MW; 8FC81952D4DC5F01 CRC64;
MTTRSDWNAW AASRESARIT DWLREISEPD WSATVNHPLF DALAEGRLVG GDFAAYMVQD
YGFVDPFTAL IGHAIGHAPS MADRVVLGQF MGMLTSDENS TFQRTFDAFE VPASLREAPD
YLPQTLAFRE LLHDTGQGGD YAEILTVLVV TEWVYLEWAL RVTRVDGLHP LMGEWIDLHD
NPAFQEFVAW LRQRLDEEAA ALDDTAFARM AERFRDTVAK ERAFHDAVQP R
//
