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CAZyme Information: MGYG000000621_00898

You are here: Home > Sequence: MGYG000000621_00898

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; Lachnospirales; Lachnospiraceae; Acetatifactor;
CAZyme ID MGYG000000621_00898
CAZy Family GH32
CAZyme Description 5-dehydro-2-deoxygluconokinase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
772 MGYG000000621_18|CGC1 87317.53 4.6742
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000621 3027354 MAG Madagascar Africa
Gene Location Start: 13314;  End: 15632  Strand: -

Full Sequence      Download help

MREIVRPSLH  FTPQKGWIND  PNGLVFFKGQ  YHLFYQYNPY  HDNWDSMHWG  HAVSRDLIHW60
EELEPALVPD  MPYDNDKNGG  CFSGSVVVHD  DQLFLFYTGR  TEDETGIFET  QNLAVSKDGI120
HFVKAEENPL  IKEVPEKGGR  DFRDPKVFFA  QGKWRMICGG  STGRIEHPDS  CGRIYLFSST180
DLYHWTYSGI  LYEAEPGEGR  MFECPDAFCL  DDVWFLTTSP  MYEKDSVTTL  YLSGQVDFDK240
CEFHKEISGT  LDLGTHYYAA  QTYPVLNGEI  RSVAWLGGWL  WMPWIRDFGP  EEGYRGILDV300
SRVWYLDDNR  RLCAKVADTV  KSEMKVFSRT  LENHWTGENI  PPQSQPVMVE  LKGKLPGDGE360
LLCIDLYDTD  RHTVTICFDS  SNKEMTVNYN  RADRASRYGI  RTISCEMMEK  ETDIDILIDG420
NAFTLLWEHG  LYRYTGKLYP  QGNIGVDIKC  RAKQHYDITS  LGEILIDFTG  KKESERQTLS480
YTQNPGGAPA  NVVVAAQRLG  AQTAFIGKIG  EDFLGDFLKE  TLDKCGVSTE  GLISDADYFT540
TLAFVKLADN  GERNFAFARK  PGADIGLKGE  EVRKDIICQS  RILHVGSLSL  TDEISRNAEF600
IALKAAKNNG  TIISYDPNYR  AGLWDSQEEA  CKWMRSILEY  ADIVKVSEEE  IELLTGYTDV660
RKAAESITEY  GAKIVLITLG  EKGSFVYLQD  QQEAYVPGYS  SKVVDTTGAG  DSFMGGFLYK720
ICESGKRIEE  YSLQEMIECV  RFGNAVASLC  VEREGAIPAM  PVMEEVIKRI  NS772

Enzyme Prediction      help

No EC number prediction in MGYG000000621_00898.

CAZyme Signature Domains help

Created with Snap387711515419323127030834738642446350154057961765669473310313GH32
Family Start End Evalue family coverage
GH32 10 313 7.3e-89 0.9863481228668942

CDD Domains      download full data without filtering help

Created with Snap387711515419323127030834738642446350154057961765669473316306GH32_FFase458757bac_FRK10310Glyco_hydro_32N10419Glyco_3216280GH32_BfrA-like
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd08996 GH32_FFase 5.25e-116 16 306 1 281
Glycosyl hydrolase family 32, beta-fructosidases. Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd01167 bac_FRK 2.26e-102 458 757 2 295
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
pfam00251 Glyco_hydro_32N 2.83e-100 10 310 1 301
Glycosyl hydrolases family 32 N-terminal domain. This domain corresponds to the N-terminal domain of glycosyl hydrolase family 32 which forms a five bladed beta propeller structure.
smart00640 Glyco_32 4.56e-97 10 419 1 426
Glycosyl hydrolases family 32.
cd18625 GH32_BfrA-like 1.21e-92 16 280 1 264
glycoside hydrolase family 32 protein such as Thermotoga maritima invertase (BfrA or Tm1414). This subfamily of glycosyl hydrolase family GH32 includes beta-fructosidase (invertase, EC 3.2.1.26) that cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase. These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits      help

Created with Snap38771151541932312703083473864244635015405796176566947331772QNM02729.1|GH325312QNM03128.1|GH325430ADB10727.1|GH325430BAQ28033.1|GH325430VEG24706.1|GH32
Hit ID E-Value Query Start Query End Hit Start Hit End
QNM02729.1 0.0 1 772 1 772
QNM03128.1 3.64e-90 5 312 9 318
ADB10727.1 8.13e-89 5 430 6 431
BAQ28033.1 1.36e-88 5 430 24 449
VEG24706.1 1.57e-88 5 430 29 454

PDB Hits      download full data without filtering help

Created with Snap387711515419323127030834738642446350154057961765669473343551UYP_A43551W2T_A74407VCO_A63027BWB_A63027BWC_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
1UYP_A 1.91e-64 4 355 1 334
Thethree-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_B The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_C The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_D The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_E The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_F The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8]
1W2T_A 5.09e-64 4 355 1 334
beta-fructosidasefrom Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_B beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_C beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_D beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_E beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_F beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8]
7VCO_A 6.99e-60 7 440 27 459
ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
7BWB_A 2.42e-59 6 302 49 336
Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori]
7BWC_A 3.18e-58 6 302 49 336
Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori]

Swiss-Prot Hits      download full data without filtering help

Created with Snap3877115154193231270308347386424463501540579617656694733458772sp|O82616|SCRK5_ARATH458772sp|A2WXV8|SCRK1_ORYSI458766sp|Q9M1B9|SCRK4_ARATH458772sp|Q0JGZ6|SCRK1_ORYSJ458767sp|Q42896|SCRK2_SOLLC
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O82616 3.54e-70 458 772 7 321
Probable fructokinase-5 OS=Arabidopsis thaliana OX=3702 GN=At4g10260 PE=2 SV=1
A2WXV8 3.64e-66 458 772 8 322
Fructokinase-1 OS=Oryza sativa subsp. indica OX=39946 GN=FRK1 PE=1 SV=1
Q9M1B9 3.98e-66 458 766 11 319
Probable fructokinase-4 OS=Arabidopsis thaliana OX=3702 GN=At3g59480 PE=2 SV=1
Q0JGZ6 9.81e-66 458 772 8 322
Fructokinase-1 OS=Oryza sativa subsp. japonica OX=39947 GN=FRK1 PE=1 SV=2
Q42896 1.58e-65 458 767 12 321
Fructokinase-2 OS=Solanum lycopersicum OX=4081 GN=FRK2 PE=2 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000078 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000621_00898.