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CAZyme Information: MGYG000001748_00480

You are here: Home > Sequence: MGYG000001748_00480

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 CAG-56 sp900762665
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-56; CAG-56 sp900762665
CAZyme ID MGYG000001748_00480
CAZy Family GH127
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
2715 302186.85 4.5707
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001748 4218051 MAG Sweden Europe
Gene Location Start: 183147;  End: 191294  Strand: +

Full Sequence      Download help

MKKRIISFLL  SITMIAGACF  PSMPPVHAAA  STQQVQQVQE  TGNLNYFSNQ  GKLNENAFVQ60
LPMGAVEAKD  WLKQQLYLQK  NGLTGAIHDQ  YSLYGPDNGW  RGGKGDGWEK  GAYYLRGLTS120
LAWVLGDEEL  KGKAMEWIDF  ILDSQRENGF  MGPVNDGDGS  SDNWDWWPRM  VILQVIRDYY180
EATEQEGKPD  ERVLPFFEKY  FRYQLQRLPG  KPLNSWAASR  GGDNIEVLLW  YYNRVYDESD240
PTATDWIIDL  ASVLASQTKS  QDSGLDWNAV  FNDTTVREHV  VNTTQAMKTP  AVLSQLPGHE300
GDVNSLKQGI  FNMGLDHGRV  DNLANADEGA  RENYPYRGAE  LCSVVESLLS  NEMSIRITGE360
SWLGDQIEQT  AYNNLPAGYA  PDYTGHNYFQ  AQNQVLGTHG  NHEFDCDHGD  DSAYGALTGF420
ECCFPNMHMG  WPKFVQSMWM  ATKDNGLAVV  AYGPNQVTAK  VADGKTAVFE  EVTDYPFKDT480
IALNYSGDTA  KFPLKLRLPA  WCEKPEVTIN  GVTADLSVQE  KGFAVLNREW  KPGDQVSVTF540
PMKVRTSTWF  NNSQAVEYGP  LIFAVKVEED  WRIGTDDAAK  EIQYDPVGEF  DRKEVYPASD600
WNYGLVLNEA  DPEGSFEITA  EDEISLQPFI  LDNAPITMKV  KGQLIPQWKL  KGNVVPEPPY660
SPIAPDESLQ  REIELVPYGC  TRIRITQIPV  IGEPCSDGVT  ERTLEDAQIY  EENGTRVTEF720
DNIVMPFAED  YTLRISYEGS  GSMEMNINQK  YSESVRFDGS  GTMTAENLCE  IVPGTNRYFH780
FGYGKYNNIR  FFGKDVTITK  LEILPVDLFT  QPEIYSAVIS  KDGTSVTLNT  NIDRADGFYT840
VHYGTESGNY  TRTAENFFDK  KAVLTGLTPG  EDYYFQISML  VNGVEKVTEE  VKAVAAKEQP900
LSFKDDFSDP  AASKKQWTLY  DPKNVVTFEE  GKMSVGSSDN  IKAMTGEQQW  KDYAVVARLT960
GTGKAERDFG  IILRASDIGD  GSDGYKGYYV  GINAIAEGLN  IGYADGGWNG  IAAPGGITYE1020
EGKTYELKTI  IAGERLAVYV  DGVKLYDELI  SNMRSGDRPV  PLYESGSAGV  RSWNQSFDVN1080
SFEVREISQE  EYAELGIENH  LFEDDFSSAE  NSRTKWTVYD  PDGAVEFTDG  GLKVGNSKNL1140
KIMAGTGEEE  WENYAVETKL  KGPQNPQRDF  GVMFRCTDVT  EEGADSYFGY  YVGIDAIGGG1200
LNVGYANGGW  NDIEKVRAFQ  YEPGKVYDLK  ILVCGNQFKV  YVDGQQYYEF  TDDKFPYGSV1260
GLRSWNQPFE  AGYFKVRRLT  AEEEGQFDQK  TDPNVPEEVV  PQFSDDFEDT  AASAEKWRLC1320
GDKSRMKFEA  GKLSMGSSDN  VKAVAGDENW  KDYVAEVSVA  LDAKGEQNAG  LMYRVTGVEE1380
NGSDGYNGYY  YGIGNNRDGT  GYFIIGYADG  DWHQTMRKNL  PAFEAGTEYV  LKAVVYGDRI1440
ALYLDDQMIT  RFVDARYASG  MIGLRSYDKA  FTADNVTVRS  LTDADKAGFD  GMSRYIEETF1500
GAYKTIQLKF  PKFSSSKNYK  IIYGTEPGNY  TNEVYNLNHW  KSGSRSDKQG  LTLPENDQAY1560
YLKLIALDGK  EETTVSDEVM  VHTGDKPDLS  EELEKLSVVL  KDAEQTSQDG  MTEESSERLN1620
WAIAYAKEVA  GAPDRNLMEV  RLAKNSLLVG  KNELEEDTNA  EVLPVKVKLE  AENAQLAGVA1680
KLVERGDASG  GYKVGMIDNQ  DATVTYTLKA  PKDGSYRIEL  ATGSGADQPN  ASHMYYVNGQ1740
KDQAKIVTYQ  PNGWDNWSLY  PVEVELKKGE  NTFTVTHSGR  ENSFSELDYI  IFYTSNPKVD1800
KITLDGEALE  GFERDTLTYQ  IKVQDLEKLP  KVAAELSPDA  AEEFEVTVIQ  GREASVTLTH1860
KKDKTFTLTY  QVRFYDDRAF  DSSIVNFGAD  PYVTYQDGYY  YYCRVLQDKA  IYVSKAKELN1920
RIAATEPQLV  YTPAAGEPNR  ELWAPEMHYM  NGKWYIYYTA  GAGADHRMYV  LESKTGDALG1980
EYEFKGKLAP  ETDRWAIDQT  VLEYGGKLYA  VWSGWEGTTN  VSQRIYIAEM  SDPLTITGER2040
AELSRPEYSW  ELDGTPTINE  GAQIAVSPEG  VVNIIYSASG  SWTDNYCLGR  LTLRGENPMN2100
PEDWEKGTES  VFHKSAPSTY  STGHACFTKS  PDGTEDYIVY  HATRGAGQGW  NGRGVRTQMF2160
TWNEDGTPHF  GTALAYDGKV  NMPSGTETAK  RSRYEAEEGT  LLGGAAVEET  YNSSGKKKVT2220
GLRSDGDGVS  FTVEAQTAGI  YHLYLGAATK  EEGAGLELQV  NGAQSVKKNV  LPFNAASGGG2280
LCPDNWIGYE  FSVTLAKGEN  NIDVRKMDGQ  PMPDLDYLDM  ELEEEIKADK  TELQEVYDLH2340
KGKQETDYTP  KSWKAFGEAL  DQAKTLLEDE  HADQSQVDLA  VKALVEAARK  LVRKDGQVTE2400
EDLQEAVKKA  EEAREAAEEA  KKLAEQAQAE  AKKQKEEAEA  AKKAALEAQK  RAEEMADASK2460
EEREKAQAEA  EEARKQAEAA  EKLVKEAEKA  VQAAEKARKA  AEEAAEVSSR  EAEAVRAELT2520
AAKEEIEKAR  EEAQKAREEA  DRLRRAAEAS  AKEAEEALKA  LQEKQKEQET  VNSVKVGEIY2580
PSGNLKYLVT  SVSEKTVSVT  GASRKNLKAI  TVPASITIEG  DTYRVTAISK  NAFFRYKRLQ2640
KITIGKNVTS  IGSKAFYRDA  KLKTIVVRAE  KLVKIGKNAW  KGIYKKAVIR  TPQKKKKAYA2700
KLLKKSGIAK  TVKIK2715

Enzyme Prediction      help

No EC number prediction in MGYG000001748_00480.

CAZyme Signature Domains help

Created with Snap13527140754367881495010861221135714931629176419002036217223072443257918832168GH43339563GH12711141267CBM669291077CBM6616701790CBM35
Family Start End Evalue family coverage
GH43 1883 2168 8.5e-99 0.9863945578231292
GH127 339 563 3.2e-30 0.42366412213740456
CBM66 1114 1267 1.1e-21 0.9290322580645162
CBM66 929 1077 1.5e-17 0.8580645161290322
CBM35 1670 1790 3.6e-17 0.9663865546218487

CDD Domains      download full data without filtering help

Created with Snap13527140754367881495010861221135714931629176419002036217223072443257918892143GH43_LbAraf43-like18892142GH43_LbAraf43-like18892142GH43f_LbAraf43-like18892175COG3940106564Glyco_hydro_127
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd18820 GH43_LbAraf43-like 8.95e-127 1889 2143 1 258
Glycosyl hydrolase family 43 proteins similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans GbtXyl43B. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes enzymes with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase activities, similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans IT-08 beta-xylosidase / exo-xylanase (GbtXyl43B). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain 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.
cd08980 GH43_LbAraf43-like 3.05e-76 1889 2142 1 275
Glycosyl hydrolase family 43 proteins such as Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans GbtXyl43B. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase activities. In addition to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans IT-08 beta-xylosidase / exo-xylanase (GbtXyl43B). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) familiesGH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain 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.
cd18817 GH43f_LbAraf43-like 6.02e-63 1889 2142 1 261
Glycosyl hydrolase family 43 such as Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43. This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with alpha-L-arabinofuranosidase (EC 3.2.1.55) activity. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. Characterized enzymes belonging to this subgroup include Lactobacillus brevis (LbAraf43) and Weissella sp (WAraf43) which show activity with similar catalytic efficiency on 1,5-alpha-L-arabinooligosaccharides with a degree of polymerization (DP) of 2-3; size is limited by an extended loop at the entrance to the active site. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain 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.
COG3940 COG3940 1.93e-60 1889 2175 14 315
Beta-xylosidase, GH43 family [Carbohydrate transport and metabolism].
pfam07944 Glyco_hydro_127 6.82e-46 106 564 46 503
Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.

CAZyme Hits      help

Created with Snap13527140754367881495010861221135714931629176419002036217223072443257949696QJE95537.1|CBM6639710ALL07583.1|CBM6619694QPH39723.1|CBM6648710QNF30112.1|CBM3546710AMP98056.1|CBM66
Hit ID E-Value Query Start Query End Hit Start Hit End
QJE95537.1 1.07e-150 49 696 31 653
ALL07583.1 2.19e-143 39 710 21 676
QPH39723.1 1.42e-139 19 694 8 652
QNF30112.1 4.25e-138 48 710 30 676
AMP98056.1 4.41e-138 46 710 28 676

PDB Hits      download full data without filtering help

Created with Snap135271407543678814950108612211357149316291764190020362172230724432579188921795M8B_A188921833K1U_A187921753AKF_A188021715M8E_A3395664QJY_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
5M8B_A 7.56e-44 1889 2179 36 346
ChainA, Alpha-L-arabinofuranosidase II [Levilactobacillus brevis],5M8B_B Chain B, Alpha-L-arabinofuranosidase II [Levilactobacillus brevis]
3K1U_A 1.06e-42 1889 2183 18 327
Beta-xylosidase,family 43 glycosyl hydrolase from Clostridium acetobutylicum [Clostridium acetobutylicum]
3AKF_A 5.47e-42 1879 2175 10 317
Crystalstructure of exo-1,5-alpha-L-arabinofuranosidase [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKG_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-1,5-L-arabinofuranobiose [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKH_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-1,5-L-arabinofuranotriose [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKI_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-L-arabinofuranosyl azido [Streptomyces avermitilis MA-4680 = NBRC 14893]
5M8E_A 3.82e-35 1880 2171 25 336
Crystalstructure of a GH43 arabonofuranosidase from Weissella sp. strain 142 [Weissella cibaria],5M8E_B Crystal structure of a GH43 arabonofuranosidase from Weissella sp. strain 142 [Weissella cibaria]
4QJY_A 3.21e-14 339 566 332 562
Crystalstructure of native Ara127N, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QJY_B Crystal structure of native Ara127N, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus]

Swiss-Prot Hits      download full data without filtering help

Created with Snap13527140754367881495010861221135714931629176419002036217223072443257918792175sp|Q82P90|IABF_STRAW18802142sp|P82594|IABF_STRCX18792248sp|G4MMH2|ABFB_MAGO7
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q82P90 3.86e-41 1879 2175 36 343
Extracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=Araf43A PE=1 SV=1
P82594 5.78e-35 1880 2142 50 318
Extracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Streptomyces chartreusis OX=1969 PE=1 SV=1
G4MMH2 2.00e-31 1879 2248 40 415
Alpha-L-arabinofuranosidase B OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=abfB 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
0.000614 0.673987 0.324340 0.000480 0.000309 0.000225

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001748_00480.