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Protein

Phospho-furanose lactonase

Gene

MS53_0025

Organism
Mycoplasma synoviae (strain 53)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

A 1,4-lactone + H2O = a 4-hydroxyacid.1 Publication
D-xylono-1,4-lactone-5-phosphate + H2O = 5-phospho-D-xylonate.1 Publication
L-arabino-1,4-lactone-5-phosphate + H2O = 5-phospho-L-arabinonate.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

Kineticsi

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.1 Publication
  1. KM=0.3 mM for D-arabino-1,4-lactone-5-phosphate1 Publication
  2. KM=0.5 mM for D-xylono-1,4-lactone-5-phosphate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi24Zinc 1Combined sources1 Publication1
    Metal bindingi26Zinc 1Combined sources1 Publication1
    Metal bindingi153Zinc 1; via carbamate groupCombined sources1 Publication1
    Metal bindingi153Zinc 2; via carbamate groupCombined sources1 Publication1
    Metal bindingi186Zinc 2Combined sources1 Publication1
    Metal bindingi214Zinc 2Combined sources1 Publication1
    Metal bindingi272Zinc 1Combined sources1 Publication1

    GO - Molecular functioni

    • 1,4-lactonase activity Source: CACAO
    • zinc ion binding Source: InterPro

    GO - Biological processi

    Keywordsi

    Molecular functionHydrolase
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMSYN262723:GH37-30-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phospho-furanose lactonase1 Publication (EC:3.1.1.251 Publication)
    Gene namesi
    Ordered Locus Names:MS53_0025Imported
    OrganismiMycoplasma synoviae (strain 53)
    Taxonomic identifieri262723 [NCBI]
    Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
    Proteomesi
    • UP000000549 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi29K → 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. 1 Publication1
    Mutagenesisi34E → 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. 1 Publication1
    Mutagenesisi100H → 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. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004396681 – 353Phospho-furanose lactonaseAdd BLAST353

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei153N6-carboxylysineCombined sources1 Publication1

    Interactioni

    Protein-protein interaction databases

    STRINGi262723.MS53_0025.

    Structurei

    Secondary structure

    1353
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 8Combined sources4
    Beta strandi11 – 14Combined sources4
    Helixi15 – 17Combined sources3
    Beta strandi20 – 25Combined sources6
    Helixi33 – 37Combined sources5
    Helixi39 – 41Combined sources3
    Helixi46 – 58Combined sources13
    Beta strandi61 – 66Combined sources6
    Turni70 – 73Combined sources4
    Helixi76 – 86Combined sources11
    Helixi87 – 89Combined sources3
    Beta strandi92 – 98Combined sources7
    Helixi102 – 104Combined sources3
    Turni107 – 109Combined sources3
    Helixi111 – 114Combined sources4
    Helixi117 – 129Combined sources13
    Turni134 – 137Combined sources4
    Beta strandi138 – 140Combined sources3
    Beta strandi151 – 158Combined sources8
    Beta strandi160 – 162Combined sources3
    Helixi163 – 179Combined sources17
    Beta strandi183 – 188Combined sources6
    Helixi193 – 203Combined sources11
    Helixi207 – 209Combined sources3
    Beta strandi210 – 213Combined sources4
    Helixi215 – 217Combined sources3
    Helixi221 – 231Combined sources11
    Beta strandi234 – 237Combined sources4
    Turni243 – 245Combined sources3
    Helixi248 – 260Combined sources13
    Helixi264 – 266Combined sources3
    Beta strandi267 – 269Combined sources3
    Helixi276 – 278Combined sources3
    Helixi280 – 285Combined sources6
    Helixi294 – 298Combined sources5
    Helixi300 – 307Combined sources8
    Helixi311 – 318Combined sources8
    Helixi320 – 325Combined sources6
    Helixi336 – 338Combined sources3
    Helixi341 – 349Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3MSRX-ray2.16A2-353[»]
    3OVGX-ray2.06A/B/C/D/E/F2-353[»]
    ProteinModelPortaliQ4A724.
    SMRiQ4A724.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ4A724.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni244 – 245Substrate bindingCombined sources1 Publication2
    Regioni275 – 278Substrate bindingCombined sources1 Publication4

    Sequence similaritiesi

    Belongs to the metallo-dependent hydrolases superfamily. Phosphotriesterase family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG41080QX. Bacteria.
    COG1735. LUCA.
    HOGENOMiHOG000081700.
    KOiK07048.
    OMAiPFQIIRV.
    OrthoDBiPOG091H0FI6.

    Family and domain databases

    InterProiView protein in InterPro
    IPR032466. Metal_Hydrolase.
    IPR001559. Phosphotriesterase.
    PANTHERiPTHR10819. PTHR10819. 2 hits.
    PfamiView protein in Pfam
    PF02126. PTE. 1 hit.
    PIRSFiPIRSF016839. PhP. 1 hit.
    SUPFAMiSSF51556. SSF51556. 1 hit.
    PROSITEiView protein in PROSITE
    PS51347. PHOSPHOTRIESTERASE_2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q4A724-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MENKFARTVL GDIPVEKLGI TDCHDHFIKN GGPEVEEHID FLMLNVDASI
    60 70 80 90 100
    KEFKEFIDRG GSTIVTMDPP NVGRDVLKTL EIANAVKNLG GNVIMSTGFH
    110 120 130 140 150
    KAKFYDKYSS WLAVVPTEEI VKMCVAEIEE GMDEYNYNGP VVKRSKAKAG
    160 170 180 190 200
    IIKAGTGYGA IDRLELKALE VAARTSILTG CPILVHTQLG TMALEVAKHL
    210 220 230 240 250
    IGFGANPDKI QISHLNKNPD KYYYEKVIKE TGVTLCFDGP DRVKYYPDSL
    260 270 280 290 300
    LAENIKYLVD KGLQKHITLS LDAGRILYQR NYGLTKGKQT FGLAYLFDRF
    310 320 330 340 350
    LPLLKQVGVS KEAIFDILVN NPKRVLAFDE KRNFDPLKVS KEVLELKKEL

    NLN
    Length:353
    Mass (Da):39,499
    Last modified:September 13, 2005 - v1
    Checksum:i5F6004A8271CFAAB
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE017245 Genomic DNA. Translation: AAZ43447.1.
    RefSeqiWP_011283191.1. NC_007294.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ43447; AAZ43447; MS53_0025.
    KEGGimsy:MS53_0025.

    Similar proteinsi

    Entry informationi

    Entry nameiPFLAC_MYCS5
    AccessioniPrimary (citable) accession number: Q4A724
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 12, 2017
    Last sequence update: September 13, 2005
    Last modified: October 25, 2017
    This is version 71 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families