PFLAC_MYCS5
ID PFLAC_MYCS5 Reviewed; 353 AA.
AC Q4A724;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Phospho-furanose lactonase {ECO:0000303|PubMed:24955762};
DE EC=3.1.1.104 {ECO:0000269|PubMed:24955762};
DE EC=3.1.1.25 {ECO:0000269|PubMed:24955762};
GN OrderedLocusNames=MS53_0025 {ECO:0000312|EMBL:AAZ43447.1};
OS Mycoplasmopsis synoviae (strain 53) (Mycoplasma synoviae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=262723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=53 {ECO:0000312|EMBL:AAZ43447.1, ECO:0000312|Proteomes:UP000000549};
RX PubMed=16077101; DOI=10.1128/jb.187.16.5568-5577.2005;
RA Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L.,
RA Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R.,
RA Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M.,
RA Brocchi M., Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S.,
RA Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G.,
RA Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S.,
RA Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B.,
RA Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B.,
RA Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C.,
RA Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L.,
RA Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R.,
RA Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C.,
RA Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P.,
RA Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.;
RT "Swine and poultry pathogens: the complete genome sequences of two strains
RT of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL J. Bacteriol. 187:5568-5577(2005).
RN [2] {ECO:0007744|PDB:3MSR, ECO:0007744|PDB:3OVG}
RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 2-353 IN COMPLEX WITH 2 ZINC IONS
RP AND SUBSTRATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, CARBOXYLATION AT LYS-153, MUTAGENESIS OF LYS-29;
RP GLU-34 AND HIS-100, AND SUBSTRATE SPECIFICITY.
RX PubMed=24955762; DOI=10.1021/bi500595c;
RA Korczynska M., Xiang D.F., Zhang Z., Xu C., Narindoshvili T., Kamat S.S.,
RA Williams H.J., Chang S.S., Kolb P., Hillerich B., Sauder J.M., Burley S.K.,
RA Almo S.C., Swaminathan S., Shoichet B.K., Raushel F.M.;
RT "Functional annotation and structural characterization of a novel lactonase
RT hydrolyzing D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-
RT phosphate.";
RL Biochemistry 53:4727-4738(2014).
CC -!- FUNCTION: Catalyzes the hydrolysis of D-xylono-1,4-lactone-5-phosphate
CC and L-arabino-1,4-lactone-5-phosphate. Also able to hydrolyze carboxy
CC 1,4-lactones. {ECO:0000269|PubMed:24955762}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,4-lactone + H2O = a 4-hydroxyacid + H(+);
CC Xref=Rhea:RHEA:12745, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37581, ChEBI:CHEBI:136596; EC=3.1.1.25;
CC Evidence={ECO:0000269|PubMed:24955762};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylono-1,4-lactone 5-phosphate + H2O = 5-phospho-D-xylonate
CC + H(+); Xref=Rhea:RHEA:52644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:136749, ChEBI:CHEBI:136751; EC=3.1.1.104;
CC Evidence={ECO:0000269|PubMed:24955762};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arabino-1,4-lactone 5-phosphate = 5-phospho-L-
CC arabinonate + H(+); Xref=Rhea:RHEA:52648, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136753, ChEBI:CHEBI:136756;
CC EC=3.1.1.104; Evidence={ECO:0000269|PubMed:24955762};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:24955762};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:24955762};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for D-xylono-1,4-lactone-5-phosphate
CC {ECO:0000269|PubMed:24955762};
CC KM=0.3 mM for L-arabino-1,4-lactone-5-phosphate
CC {ECO:0000269|PubMed:24955762};
CC Note=kcat is 23.4 sec(-1) with D-xylono-1,4-lactone-5-phosphate as
CC substrate. kcat is 6.7 sec(-1) with L-arabino-1,4-lactone-5-phosphate
CC as substrate. {ECO:0000269|PubMed:24955762};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.
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DR EMBL; AE017245; AAZ43447.1; -; Genomic_DNA.
DR RefSeq; WP_011283191.1; NC_007294.1.
DR PDB; 3MSR; X-ray; 2.16 A; A=2-353.
DR PDB; 3OVG; X-ray; 2.06 A; A/B/C/D/E/F=2-353.
DR PDBsum; 3MSR; -.
DR PDBsum; 3OVG; -.
DR AlphaFoldDB; Q4A724; -.
DR SMR; Q4A724; -.
DR STRING; 262723.MS53_0025; -.
DR EnsemblBacteria; AAZ43447; AAZ43447; MS53_0025.
DR KEGG; msy:MS53_0025; -.
DR eggNOG; COG1735; Bacteria.
DR HOGENOM; CLU_054760_1_1_14; -.
DR OMA; MVKCGFI; -.
DR BRENDA; 3.1.1.104; 10311.
DR EvolutionaryTrace; Q4A724; -.
DR Proteomes; UP000000549; Chromosome.
DR GO; GO:0050490; F:1,4-lactonase activity; IDA:CACAO.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009056; P:catabolic process; IEA:InterPro.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001559; Phosphotriesterase.
DR PANTHER; PTHR10819; PTHR10819; 1.
DR Pfam; PF02126; PTE; 1.
DR PIRSF; PIRSF016839; PhP; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..353
FT /note="Phospho-furanose lactonase"
FT /id="PRO_0000439668"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24955762,
FT ECO:0007744|PDB:3OVG"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24955762,
FT ECO:0007744|PDB:3OVG"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000269|PubMed:24955762,
FT ECO:0007744|PDB:3OVG"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000269|PubMed:24955762,
FT ECO:0007744|PDB:3OVG"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24955762,
FT ECO:0007744|PDB:3OVG"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24955762,
FT ECO:0007744|PDB:3OVG"
FT BINDING 244..245
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24955762,
FT ECO:0007744|PDB:3MSR, ECO:0007744|PDB:3OVG"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24955762,
FT ECO:0007744|PDB:3OVG"
FT BINDING 275..278
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24955762,
FT ECO:0007744|PDB:3MSR, ECO:0007744|PDB:3OVG"
FT MOD_RES 153
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000269|PubMed:24955762,
FT ECO:0007744|PDB:3OVG"
FT MUTAGEN 29
FT /note="K->A: 3- and 20-fold decrease of the affinity and
FT catalytic efficiency for D-xylono-1,4-lactone-5-phosphate,
FT respectively. 2- and 15-fold decrease of the affinity and
FT catalytic efficiency for L-arabino-1,4-lactone-5-phosphate,
FT respectively."
FT /evidence="ECO:0000269|PubMed:24955762"
FT MUTAGEN 34
FT /note="E->Q: 20-fold decrease of the catalytic efficiency
FT for D-xylono-1,4-lactone-5-phosphate, but almost the same
FT affinity compared to the wild-type. 6- and 11-fold decrease
FT of the affinity and catalytic efficiency for L-arabino-1,4-
FT lactone-5-phosphate, respectively."
FT /evidence="ECO:0000269|PubMed:24955762"
FT MUTAGEN 100
FT /note="H->N: 4- and 5-fold decrease of the catalytic
FT efficiency and affinity for D-xylono-1,4-lactone-5-
FT phosphate, respectively. Same catalytic efficiency for L-
FT arabino-1,4-lactone-5-phosphate compared to the wild-type,
FT but 2-fold decrease of the affinity."
FT /evidence="ECO:0000269|PubMed:24955762"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3OVG"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3OVG"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:3OVG"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:3OVG"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3OVG"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3OVG"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:3OVG"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:3OVG"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3OVG"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:3OVG"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:3OVG"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3OVG"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:3OVG"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:3OVG"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3OVG"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 320..325
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:3OVG"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:3OVG"
SQ 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
