TENA_STAAR
ID TENA_STAAR Reviewed; 229 AA.
AC Q6GEY1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Aminopyrimidine aminohydrolase {ECO:0000250|UniProtKB:P25052};
DE EC=3.5.99.2 {ECO:0000269|PubMed:24311574};
DE AltName: Full=Thiaminase II {ECO:0000303|PubMed:21206023};
GN Name=tenA {ECO:0000303|PubMed:21206023}; OrderedLocusNames=SAR2183;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
RN [2]
RP CRYSTALLIZATION.
RC STRAIN=ATCC 25923 / DSM 1104 / Seattle 1945 / FO 14462 / JCM 2413;
RX PubMed=21206023; DOI=10.1107/s1744309110043174;
RA Begum A., Drebes J., Perbandt M., Wrenger C., Betzel C.;
RT "Purification, crystallization and preliminary X-ray diffraction analysis
RT of the thiaminase type II from Staphylococcus aureus.";
RL Acta Crystallogr. F 67:51-53(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF ASP-111 AND
RP LYS-115.
RC STRAIN=ATCC 25923 / DSM 1104 / Seattle 1945 / FO 14462 / JCM 2413;
RX PubMed=24311574; DOI=10.1107/s0907444913021550;
RA Begum A., Drebes J., Kikhney A., Mueller I.B., Perbandt M., Svergun D.,
RA Wrenger C., Betzel C.;
RT "Staphylococcus aureus thiaminase II: oligomerization warrants proteolytic
RT protection against serine proteases.";
RL Acta Crystallogr. D 69:2320-2329(2013).
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) (By similarity). Is also able to catalyze the
CC hydrolytic cleavage of thiamine; however, this thiaminase activity may
CC not be physiologically relevant. Therefore, is probably involved in the
CC regeneration of the thiamine pyrimidine from thiamine degraded products
CC present in the environment, rather than in thiamine degradation.
CC {ECO:0000250|UniProtKB:P25052, ECO:0000269|PubMed:24311574,
CC ECO:0000305}.
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:0000250|UniProtKB:P25052};
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:0000269|PubMed:24311574};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.40 mM for thiamine {ECO:0000269|PubMed:24311574};
CC Note=kcat is 4.07 msec(-1) for the hydrolysis of thiamine.
CC {ECO:0000269|PubMed:24311574};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000250|UniProtKB:P25052}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:24311574}.
CC -!- SIMILARITY: Belongs to the TenA family. {ECO:0000305}.
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DR EMBL; BX571856; CAG41163.1; -; Genomic_DNA.
DR RefSeq; WP_000396068.1; NC_002952.2.
DR PDB; 4FN6; X-ray; 2.69 A; A/B/C/D=1-229.
DR PDBsum; 4FN6; -.
DR AlphaFoldDB; Q6GEY1; -.
DR SASBDB; Q6GEY1; -.
DR SMR; Q6GEY1; -.
DR KEGG; sar:SAR2183; -.
DR HOGENOM; CLU_077537_3_1_9; -.
DR OMA; SAHHYIR; -.
DR OrthoDB; 1537025at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0050334; F:thiaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.910.10; -; 1.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR004305; Thiaminase-2/PQQC.
DR InterPro; IPR027574; Thiaminase_II.
DR Pfam; PF03070; TENA_THI-4; 1.
DR SUPFAM; SSF48613; SSF48613; 1.
DR TIGRFAMs; TIGR04306; salvage_TenA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Thiamine biosynthesis.
FT CHAIN 1..229
FT /note="Aminopyrimidine aminohydrolase"
FT /id="PRO_0000293607"
FT ACT_SITE 137
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT ACT_SITE 208
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT SITE 47
FT /note="Increases nucleophilicity of active site Cys"
FT /evidence="ECO:0000250|UniProtKB:P25052"
FT MUTAGEN 111
FT /note="D->A: Affects the oligomeric state since the mutant
FT is a monomer that is much more susceptible to serine
FT protease degradation, but has nearly no effect on kinetic
FT parameters; when associated with A-115."
FT /evidence="ECO:0000269|PubMed:24311574"
FT MUTAGEN 115
FT /note="K->A: Affects the oligomeric state since the mutant
FT is a monomer that is much more susceptible to serine
FT protease degradation, but has nearly no effect on kinetic
FT parameters; when associated with A-111."
FT /evidence="ECO:0000269|PubMed:24311574"
FT HELIX 3..20
FT /evidence="ECO:0007829|PDB:4FN6"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:4FN6"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:4FN6"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:4FN6"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:4FN6"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:4FN6"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:4FN6"
FT HELIX 108..123
FT /evidence="ECO:0007829|PDB:4FN6"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:4FN6"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:4FN6"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:4FN6"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:4FN6"
FT HELIX 172..186
FT /evidence="ECO:0007829|PDB:4FN6"
FT HELIX 191..216
FT /evidence="ECO:0007829|PDB:4FN6"
SQ SEQUENCE 229 AA; 26841 MW; 79AA54FF5298A8C7 CRC64;
MEFSQKLYQA AKPIINDIYE DDFIQKMLLG NIQADALRHY LQADAAYLKE FTNLYALLIP
KMNSMNDVKF LVEQIEFMVE GEVLAHDILA QIVGESYEEI IKTKVWPPSG DHYIKHMYFQ
AHSRENAIYT IAAMAPCPYI YAELAKRSQS DHKLNREKDT AKWFDFYSTE MDDIINVFES
LMNKLAESMS DKELEQVKQV FLESCIHERR FFNMAMTLEQ WEFGGKVND
