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Phospho-furanose lactonase (EC 3.1.1.25)

 PFLAC_MYCS5             Reviewed;         353 AA.
Q4A724;
12-APR-2017, integrated into UniProtKB/Swiss-Prot.
13-SEP-2005, sequence version 1.
25-OCT-2017, entry version 71.
RecName: Full=Phospho-furanose lactonase {ECO:0000303|PubMed:24955762};
EC=3.1.1.25 {ECO:0000269|PubMed:24955762};
OrderedLocusNames=MS53_0025 {ECO:0000312|EMBL:AAZ43447.1};
Mycoplasma synoviae (strain 53).
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
NCBI_TaxID=262723;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=53 {ECO:0000312|EMBL:AAZ43447.1,
ECO:0000312|Proteomes:UP000000549};
PubMed=16077101; DOI=10.1128/JB.187.16.5568-5577.2005;
Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L.,
Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R.,
Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R.,
Brigido M.M., Brocchi M., Burity H.A., Camargo A.A., Camargo S.S.,
Carepo M.S., Carraro D.M., de Mattos Cascardo J.C., Castro L.A.,
Cavalcanti G., Chemale G., Collevatti R.G., Cunha C.W.,
Dallagiovanna B., Dambros B.P., Dellagostin O.A., Falcao C.,
Fantinatti-Garboggini F., Felipe M.S.S., Fiorentin L., Franco G.R.,
Freitas N.S.A., Frias D., Grangeiro T.B., Grisard E.C.,
Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A., Laurino J.P.,
Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F., Manfio G.P.,
Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B., Moreira M.A.M.,
Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C.,
Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M.,
Pereira-Ferrari L., Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M.,
Santos F.R., Schmitt R., Schneider M.P.C., Schrank A., Schrank I.S.,
Schuck A.F., Seuanez H.N., Silva D.W., Silva R., Silva S.C.,
Soares C.M.A., Souza K.R.L., Souza R.C., Staats C.C., Steffens M.B.R.,
Teixeira S.M.R., Urmenyi T.P., Vainstein M.H., Zuccherato L.W.,
Simpson A.J.G., Zaha A.;
"Swine and poultry pathogens: the complete genome sequences of two
strains of Mycoplasma hyopneumoniae and a strain of Mycoplasma
synoviae.";
J. Bacteriol. 187:5568-5577(2005).
[2]
X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 2-353 IN COMPLEX WITH 2 ZINC
IONS AND SUBSTRATE ANALOG, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, CARBAMYLATION AT LYS-153,
MUTAGENESIS OF LYS-29; GLU-34 AND HIS-100, AND SUBSTRATE SPECIFICITY.
PubMed=24955762; DOI=10.1021/bi500595c;
Korczynska M., Xiang D.F., Zhang Z., Xu C., Narindoshvili T.,
Kamat S.S., Williams H.J., Chang S.S., Kolb P., Hillerich B.,
Sauder J.M., Burley S.K., Almo S.C., Swaminathan S., Shoichet B.K.,
Raushel F.M.;
"Functional annotation and structural characterization of a novel
lactonase hydrolyzing D-xylono-1,4-lactone-5-phosphate and L-arabino-
1,4-lactone-5-phosphate.";
Biochemistry 53:4727-4738(2014).
-!- FUNCTION: Catalyzes the hydrolysis of D-xylono-1,4-lactone-5-
phosphate and L-arabino-1,4-lactone-5-phosphate. Also able to
hydroyze carboxy 1,4-lactones. {ECO:0000269|PubMed:24955762}.
-!- CATALYTIC ACTIVITY: A 1,4-lactone + H(2)O = a 4-hydroxyacid.
{ECO:0000269|PubMed:24955762}.
-!- CATALYTIC ACTIVITY: D-xylono-1,4-lactone-5-phosphate + H(2)O = 5-
phospho-D-xylonate. {ECO:0000269|PubMed:24955762}.
-!- CATALYTIC ACTIVITY: L-arabino-1,4-lactone-5-phosphate + H(2)O = 5-
phospho-L-arabinonate. {ECO:0000269|PubMed:24955762}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:24955762};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000269|PubMed:24955762};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.3 mM for D-arabino-1,4-lactone-5-phosphate
{ECO:0000269|PubMed:24955762};
KM=0.5 mM for D-xylono-1,4-lactone-5-phosphate
{ECO:0000269|PubMed:24955762};
Note=kcat is 23.4 sec(-1) with D-xylono-1,4-lactone-5-phosphate
as substrate. kcat is 6.7 sec(-1) with D-arabino-1,4-lactone-5-
phosphate as substrate. {ECO:0000269|PubMed:24955762};
-!- SIMILARITY: Belongs to the metallo-dependent hydrolases
superfamily. Phosphotriesterase family. {ECO:0000255|PROSITE-
ProRule:PRU00679}.
-----------------------------------------------------------------------
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EMBL; AE017245; AAZ43447.1; -; Genomic_DNA.
RefSeq; WP_011283191.1; NC_007294.1.
PDB; 3MSR; X-ray; 2.16 A; A=2-353.
PDB; 3OVG; X-ray; 2.06 A; A/B/C/D/E/F=2-353.
PDBsum; 3MSR; -.
PDBsum; 3OVG; -.
ProteinModelPortal; Q4A724; -.
SMR; Q4A724; -.
STRING; 262723.MS53_0025; -.
EnsemblBacteria; AAZ43447; AAZ43447; MS53_0025.
KEGG; msy:MS53_0025; -.
eggNOG; ENOG41080QX; Bacteria.
eggNOG; COG1735; LUCA.
HOGENOM; HOG000081700; -.
KO; K07048; -.
OMA; PFQIIRV; -.
OrthoDB; POG091H0FI6; -.
BioCyc; MSYN262723:GH37-30-MONOMER; -.
EvolutionaryTrace; Q4A724; -.
Proteomes; UP000000549; Chromosome.
GO; GO:0050490; F:1,4-lactonase activity; IDA:CACAO.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0009056; P:catabolic process; IEA:InterPro.
InterPro; IPR032466; Metal_Hydrolase.
InterPro; IPR001559; Phosphotriesterase.
PANTHER; PTHR10819; PTHR10819; 2.
Pfam; PF02126; PTE; 1.
PIRSF; PIRSF016839; PhP; 1.
SUPFAM; SSF51556; SSF51556; 1.
PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Hydrolase; Metal-binding;
Reference proteome; Zinc.
CHAIN 1 353 Phospho-furanose lactonase.
/FTId=PRO_0000439668.
REGION 244 245 Substrate binding. {ECO:0000244|PDB:3MSR,
ECO:0000244|PDB:3OVG,
ECO:0000269|PubMed:24955762}.
REGION 275 278 Substrate binding. {ECO:0000244|PDB:3MSR,
ECO:0000244|PDB:3OVG,
ECO:0000269|PubMed:24955762}.
METAL 24 24 Zinc 1. {ECO:0000244|PDB:3OVG,
ECO:0000269|PubMed:24955762}.
METAL 26 26 Zinc 1. {ECO:0000244|PDB:3OVG,
ECO:0000269|PubMed:24955762}.
METAL 153 153 Zinc 1; via carbamate group.
{ECO:0000244|PDB:3OVG,
ECO:0000269|PubMed:24955762}.
METAL 153 153 Zinc 2; via carbamate group.
{ECO:0000244|PDB:3OVG,
ECO:0000269|PubMed:24955762}.
METAL 186 186 Zinc 2. {ECO:0000244|PDB:3OVG,
ECO:0000269|PubMed:24955762}.
METAL 214 214 Zinc 2. {ECO:0000244|PDB:3OVG,
ECO:0000269|PubMed:24955762}.
METAL 272 272 Zinc 1. {ECO:0000244|PDB:3OVG,
ECO:0000269|PubMed:24955762}.
MOD_RES 153 153 N6-carboxylysine. {ECO:0000244|PDB:3OVG,
ECO:0000269|PubMed:24955762}.
MUTAGEN 29 29 K->A: 3- and 20-fold decrease of the
affinity and catalytic efficiency for D-
xylono-1,4-lactone-5-phosphate,
respectively. 2- and 15-fold decrease of
the affinity and catalytic efficiency for
D-arabino-1,4-lactone-5-phosphate,
respectively.
{ECO:0000269|PubMed:24955762}.
MUTAGEN 34 34 E->Q: 20-fold decrease of the catalytic
efficiency for D-xylono-1,4-lactone-5-
phosphate, but almost the same affinity
compared to the wild-type. 6- and 11-fold
decrease of the affinity and catalytic
efficiency for D-arabino-1,4-lactone-5-
phosphate, respectively.
{ECO:0000269|PubMed:24955762}.
MUTAGEN 100 100 H->N: 4- and 5-fold decrease of the
catalytic efficiency and affinity for D-
xylono-1,4-lactone-5-phosphate,
respectively. Same catalytic efficeincy
for D-arabino-1,4-lactone-5-phosphate
compared to the wild-type, but 2-fold
decrease of the affinity.
{ECO:0000269|PubMed:24955762}.
STRAND 5 8 {ECO:0000244|PDB:3OVG}.
STRAND 11 14 {ECO:0000244|PDB:3OVG}.
HELIX 15 17 {ECO:0000244|PDB:3OVG}.
STRAND 20 25 {ECO:0000244|PDB:3OVG}.
HELIX 33 37 {ECO:0000244|PDB:3OVG}.
HELIX 39 41 {ECO:0000244|PDB:3OVG}.
HELIX 46 58 {ECO:0000244|PDB:3OVG}.
STRAND 61 66 {ECO:0000244|PDB:3OVG}.
TURN 70 73 {ECO:0000244|PDB:3OVG}.
HELIX 76 86 {ECO:0000244|PDB:3OVG}.
HELIX 87 89 {ECO:0000244|PDB:3OVG}.
STRAND 92 98 {ECO:0000244|PDB:3OVG}.
HELIX 102 104 {ECO:0000244|PDB:3OVG}.
TURN 107 109 {ECO:0000244|PDB:3OVG}.
HELIX 111 114 {ECO:0000244|PDB:3OVG}.
HELIX 117 129 {ECO:0000244|PDB:3OVG}.
TURN 134 137 {ECO:0000244|PDB:3OVG}.
STRAND 138 140 {ECO:0000244|PDB:3OVG}.
STRAND 151 158 {ECO:0000244|PDB:3OVG}.
STRAND 160 162 {ECO:0000244|PDB:3OVG}.
HELIX 163 179 {ECO:0000244|PDB:3OVG}.
STRAND 183 188 {ECO:0000244|PDB:3OVG}.
HELIX 193 203 {ECO:0000244|PDB:3OVG}.
HELIX 207 209 {ECO:0000244|PDB:3OVG}.
STRAND 210 213 {ECO:0000244|PDB:3OVG}.
HELIX 215 217 {ECO:0000244|PDB:3OVG}.
HELIX 221 231 {ECO:0000244|PDB:3OVG}.
STRAND 234 237 {ECO:0000244|PDB:3OVG}.
TURN 243 245 {ECO:0000244|PDB:3OVG}.
HELIX 248 260 {ECO:0000244|PDB:3OVG}.
HELIX 264 266 {ECO:0000244|PDB:3OVG}.
STRAND 267 269 {ECO:0000244|PDB:3OVG}.
HELIX 276 278 {ECO:0000244|PDB:3OVG}.
HELIX 280 285 {ECO:0000244|PDB:3OVG}.
HELIX 294 298 {ECO:0000244|PDB:3OVG}.
HELIX 300 307 {ECO:0000244|PDB:3OVG}.
HELIX 311 318 {ECO:0000244|PDB:3OVG}.
HELIX 320 325 {ECO:0000244|PDB:3OVG}.
HELIX 336 338 {ECO:0000244|PDB:3OVG}.
HELIX 341 349 {ECO:0000244|PDB:3OVG}.
SEQUENCE 353 AA; 39499 MW; 5F6004A8271CFAAB CRC64;
MENKFARTVL GDIPVEKLGI TDCHDHFIKN GGPEVEEHID FLMLNVDASI KEFKEFIDRG
GSTIVTMDPP NVGRDVLKTL EIANAVKNLG GNVIMSTGFH KAKFYDKYSS WLAVVPTEEI
VKMCVAEIEE GMDEYNYNGP VVKRSKAKAG IIKAGTGYGA IDRLELKALE VAARTSILTG
CPILVHTQLG TMALEVAKHL IGFGANPDKI QISHLNKNPD KYYYEKVIKE TGVTLCFDGP
DRVKYYPDSL LAENIKYLVD KGLQKHITLS LDAGRILYQR NYGLTKGKQT FGLAYLFDRF
LPLLKQVGVS KEAIFDILVN NPKRVLAFDE KRNFDPLKVS KEVLELKKEL NLN


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Phospho-AB3D283 Phospho antibody Polyclonal: Anti-Phospho BMX (Phospho Site: 566Y); Human, Mouse; Specificity: Anti-Phospho BMX (Phospho Site: 566Y); Application: IHC 0.1mg
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Phospho-AB1F053 Phospho antibody Polyclonal: Anti-Phospho RAD51 (phospho site: 310 T); Human, Mouse; Specificity: Anti-Phospho RAD51 (phospho site: 310 T); Application: IHC 0.1mg
S516 Phospho-AB3L121 Phospho antibody Polyclonal: Anti-Phospho HRX (Phospho Site: 516S); Human; Specificity: Anti-Phospho HRX (Phospho Site: 516S); Application: IHC 0.1mg
Phospho-AB1J174 Phospho antibody Polyclonal: Anti-Phospho AXL (Phospho tyrosine at 698_702_703); Human, Mouse, Rat; Specificity: Anti-Phospho AXL (Phospho tyrosine at 698_702_703); Application: IHC 0.1mg
T223 Phospho-AB3J231 Phospho antibody Polyclonal: Anti-Phospho STN1 (Phospho Site: 223T); Baker's Yeast (Saccharomyces cerevisiae); Specificity: Anti-Phospho STN1 (Phospho Site: 223T); Application: IHC 0.1mg
Phospho-AB2I184 Phospho antibody Polyclonal: Anti-Phospho CESA1 (Phospho Site: 162S); Plant Thale cress (Arabidopsis thaliana); Specificity: Anti-Phospho CESA1 (Phospho Site: 162S); Application: IHC 0.1mg
Phospho-AB1L053 Phospho antibody Polyclonal: Anti-Phospho BMH2 ( Phospho Site 189S); Baker's yeast (Saccharomyces cerevisiae); Specificity: Anti-Phospho BMH2 ( Phospho Site 189S); Application: IHC 0.1mg
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Phospho-AB1F067 Phospho antibody Polyclonal: Anti-Phospho PRKDC (Phospho Site: 2056 S); Human, mouse ; Specificity: Anti-Phospho PRKDC (Phospho Site: 2056 S); Application: IHC 0.1mg


 

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