PFLAC_MYCAP
ID PFLAC_MYCAP Reviewed; 353 AA.
AC A5IZ80;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=MAG6390 {ECO:0000312|EMBL:CAL59339.1};
OS Mycoplasmopsis agalactiae (strain NCTC 10123 / CIP 59.7 / PG2) (Mycoplasma
OS agalactiae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=347257;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10123 / CIP 59.7 / PG2 {ECO:0000312|Proteomes:UP000007065};
RX PubMed=17511520; DOI=10.1371/journal.pgen.0030075;
RA Sirand-Pugnet P., Lartigue C., Marenda M., Jacob D., Barre A., Barbe V.,
RA Schenowitz C., Mangenot S., Couloux A., Segurens B., de Daruvar A.,
RA Blanchard A., Citti C.;
RT "Being pathogenic, plastic, and sexual while living with a nearly minimal
RT bacterial genome.";
RL PLoS Genet. 3:744-758(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP 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:0000305|PubMed:24955762};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q4A724};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.9 mM for D-xylono-1,4-lactone-5-phosphate
CC {ECO:0000269|PubMed:24955762};
CC KM=0.66 mM for L-arabino-1,4-lactone-5-phosphate
CC {ECO:0000269|PubMed:24955762};
CC Note=kcat is 51 sec(-1) with D-xylono-1,4-lactone-5-phosphate as
CC substrate. kcat is 8.7 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; CU179680; CAL59339.1; -; Genomic_DNA.
DR RefSeq; WP_011949793.1; NC_009497.1.
DR AlphaFoldDB; A5IZ80; -.
DR SMR; A5IZ80; -.
DR STRING; 347257.MAG6390; -.
DR EnsemblBacteria; CAL59339; CAL59339; MAG6390.
DR KEGG; maa:MAG6390; -.
DR HOGENOM; CLU_054760_1_1_14; -.
DR OMA; MVKCGFI; -.
DR BRENDA; 3.1.1.104; 16315.
DR Proteomes; UP000007065; 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 CDD; cd00530; PTE; 1.
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 Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..353
FT /note="Phospho-furanose lactonase"
FT /id="PRO_0000439669"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q4A724"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q4A724"
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:0000250|UniProtKB:Q4A724"
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:0000250|UniProtKB:Q4A724"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q4A724"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q4A724"
FT BINDING 244..245
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4A724"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q4A724"
FT BINDING 275..278
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4A724"
FT MOD_RES 153
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:Q4A724"
SQ SEQUENCE 353 AA; 39497 MW; F2BC44FD690C590D CRC64;
MAKDKFVRTV LGDVPAESIG ITDCHDHLIK NGGPEMHEHP DFLMIDVEAA KKEVQEYVDH
GGKTIVTMDP PNVGRDVYRM LEIAEAFKGK ANIVMSTGFH KAAFYDKYSS WLACVPTDDI
VKMMVAEVEE GMDEYNYNGP VVKRSKAKAG IIKAGTGYAA IDRLELKALE VAARTSITTG
CPILVHTQLG TMALEVAQHL IGFGANPRKI QLSHLNKNPD RYYYEKIIKE TGVTICFDGP
DRVKYYPDSL LADHIKYLVD KGLQKHITLS LDAGRILYQR NYGLTKGKET FGLSYLFERF
IPLLKQVGVS QEAIDDILIN NPREILAFDE PRVYDASKVS SEVVQLKKDL KLL
