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CAZyme Information: MGYG000003909_01003

You are here: Home > Sequence: MGYG000003909_01003

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Butyricicoccaceae; Agathobaculum;
CAZyme ID MGYG000003909_01003
CAZy Family GH97
CAZyme Description 3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
2449 MGYG000003909_36|CGC1 262323.67 3.8462
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003909 2340068 MAG China Asia
Gene Location Start: 1484;  End: 8833  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003909_01003.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH97 734 1333 3.5e-137 0.9809825673534073

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam14508 GH97_N 7.38e-56 741 984 1 235
Glycosyl-hydrolase 97 N-terminal. This N-terminal domain of glycosyl-hydrolase-97 contributes part of the active site pocket. It is also important for contact with the catalytic and C-terminal domains of the whole.
pfam10566 Glyco_hydro_97 5.02e-51 993 1237 1 278
Glycoside hydrolase 97. This domain is the catalytic region of the bacterial glycosyl-hydrolase family 97. This central part of the GH97 family protein sequences represents a typical and complete (beta/alpha)8-barrel or catalytic TIM-barrel type domain. The N- and C-terminal parts of the sequences, mainly consisting of beta-strands, form two additional non-catalytic domains. In all known glycosidases with the (beta-alpha)8-barrel fold, the amino acid residues at the active site are located on the C-termini of the beta-strands.
pfam14509 GH97_C 3.03e-25 1240 1334 1 97
Glycosyl-hydrolase 97 C-terminal, oligomerization. Glycosyl-hydrolase-97 is made up of three tightly linked and highly conserved globular domains. The C-terminal domain is found to be necessary for oligomerization of the whole molecule in order to create the active-site pocket and the Ca++-binding site.
cd00839 MPP_PAPs 1.26e-10 1744 2032 5 296
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain. Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
pfam00149 Metallophos 2.11e-10 1744 1935 1 191
Calcineurin-like phosphoesterase. This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNL45026.1 0.0 113 2443 28 2499
BCI59828.1 4.08e-112 1645 2057 976 1401
QNE39615.1 4.78e-112 739 1336 31 621
QNK61828.1 6.69e-107 734 1335 36 629
AGA29066.1 4.08e-105 738 1335 32 633

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3A24_A 1.05e-47 741 1333 6 640
Crystalstructure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron],3A24_B Crystal structure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron]
5E1Q_A 1.01e-46 741 1333 20 654
Mutant(D415G) GH97 alpha-galactosidase in complex with Gal-Lac [Bacteroides thetaiotaomicron VPI-5482],5E1Q_B Mutant (D415G) GH97 alpha-galactosidase in complex with Gal-Lac [Bacteroides thetaiotaomicron VPI-5482]
3WFA_A 4.29e-38 738 1335 4 705
Catalyticrole of the calcium ion in GH97 inverting glycoside hydrolase [Bacteroides thetaiotaomicron],3WFA_B Catalytic role of the calcium ion in GH97 inverting glycoside hydrolase [Bacteroides thetaiotaomicron]
2JKA_A 4.32e-38 738 1335 13 714
Nativestructure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],2JKA_B Native structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],2JKE_A Structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron in complex with deoxynojirimycin [Bacteroides thetaiotaomicron VPI-5482],2JKE_B Structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron in complex with deoxynojirimycin [Bacteroides thetaiotaomicron VPI-5482],2JKP_A Structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron in complex with castanospermine [Bacteroides thetaiotaomicron VPI-5482],2JKP_B Structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron in complex with castanospermine [Bacteroides thetaiotaomicron VPI-5482]
2D73_A 4.72e-38 738 1335 24 725
CrystalStructure Analysis of SusB [Bacteroides thetaiotaomicron VPI-5482],2D73_B Crystal Structure Analysis of SusB [Bacteroides thetaiotaomicron VPI-5482],2ZQ0_A Crystal structure of SusB complexed with acarbose [Bacteroides thetaiotaomicron],2ZQ0_B Crystal structure of SusB complexed with acarbose [Bacteroides thetaiotaomicron]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
D7CFN7 5.93e-50 756 1329 57 616
Probable retaining alpha-galactosidase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 GN=SBI_01652 PE=3 SV=1
Q8A6L0 7.50e-48 734 1333 20 661
Retaining alpha-galactosidase OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=BT_1871 PE=1 SV=1
G8JZS4 2.58e-37 738 1335 24 725
Glucan 1,4-alpha-glucosidase SusB OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=susB PE=1 SV=1
C6CRV0 1.51e-15 2271 2447 1283 1461
Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
P19424 1.07e-12 2254 2441 24 210
Endoglucanase OS=Bacillus sp. (strain KSM-635) OX=1415 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000264 0.999041 0.000183 0.000176 0.000164 0.000144

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003909_01003.