(data stored in SCRATCH zone)

SWISSPROT: Q5LWK6_RUEPO

ID   Q5LWK6_RUEPO            Unreviewed;       214 AA.
AC   Q5LWK6;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=Aminopyrimidine aminohydrolase {ECO:0000256|RuleBase:RU363093};
DE            EC=3.5.99.2 {ECO:0000256|RuleBase:RU363093};
GN   OrderedLocusNames=SPO0051 {ECO:0000313|EMBL:AAV93382.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93382.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93382.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93382.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Catalyzes an amino-pyrimidine hydrolysis reaction at the
CC       C5' of the pyrimidine moiety of thiamine compounds, a reaction
CC       that is part of a thiamine salvage pathway.
CC       {ECO:0000256|RuleBase:RU363093}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-
CC         5-hydroxymethyl-2-methylpyrimidine + NH4(+);
CC         Xref=Rhea:RHEA:31799, ChEBI:CHEBI:15377, ChEBI:CHEBI:16892,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:63416; EC=3.5.99.2;
CC         Evidence={ECO:0000256|RuleBase:RU363093};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + thiamine = 4-amino-5-hydroxymethyl-2-
CC         methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole + H(+);
CC         Xref=Rhea:RHEA:17509, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16892, ChEBI:CHEBI:17957, ChEBI:CHEBI:18385;
CC         EC=3.5.99.2; Evidence={ECO:0000256|RuleBase:RU363093};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|RuleBase:RU363093}.
CC   -!- SIMILARITY: Belongs to the TenA family.
CC       {ECO:0000256|RuleBase:RU363093}.
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DR   EMBL; CP000031; AAV93382.1; -; Genomic_DNA.
DR   STRING; 246200.SPO0051; -.
DR   EnsemblBacteria; AAV93382; AAV93382; SPO0051.
DR   KEGG; sil:SPO0051; -.
DR   eggNOG; ENOG4105ETU; Bacteria.
DR   eggNOG; COG0819; LUCA.
DR   HOGENOM; HOG000225158; -.
DR   KO; K03707; -.
DR   OMA; CISHPFV; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001023; 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   3: Inferred from homology;
DR   PRODOM; Q5LWK6.
DR   SWISS-2DPAGE; Q5LWK6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Hydrolase {ECO:0000256|RuleBase:RU363093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Thiamine biosynthesis {ECO:0000256|RuleBase:RU363093}.
FT   DOMAIN        8    212       TENA_THI-4. {ECO:0000259|Pfam:PF03070}.
SQ   SEQUENCE   214 AA;  23634 MW;  7BF30E89D9D999B8 CRC64;
     MRAAAGQPWR DYTRHAFVEG MKDGSLARDA FVHYLRQDYV FLIHFARAWA LAVVKGETHA
     EMLAAVGTVN TLVVEEMQLH VGVCEAAGIS KDALFATPER PENLAYTRFV LEAGYSGDLA
     DLLAALAPCV MGYGEIGARL ATEATSEAYK DWIDTYAGPE YQAACKAVGE LMDQALTRRI
     GADFEASPRW ERLCRTFRTA TELEVGFWQM GLTP
//

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