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CAZyme Information: MGYG000000854_00012

You are here: Home > Sequence: MGYG000000854_00012

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 Paraprevotella sp900548345
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella sp900548345
CAZyme ID MGYG000000854_00012
CAZy Family GH27
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1257 MGYG000000854_1|CGC1 136408.49 4.5173
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000854 2733305 MAG China Asia
Gene Location Start: 21950;  End: 25723  Strand: -

Full Sequence      Download help

MKKMLLCAVA  GMMSLTAGAQ  TGKELPFQKW  ALTPPMGWNS  WDCFGPTVVE  DEVKANADYM60
AAKLADYGWE  YVIVDIRWFV  ENDKAGGYNQ  TNPIYVYDEY  GRYTPALNRF  PSAANGVGFK120
ALADYVHQKG  LKFGIHLMRG  LPKVAAEKKL  PVKGTNGITC  DMIANNDSAC  TWLRDNYKVD180
YTKPGAQEYY  NSCFELYASW  GVDYVKIDDL  SRPYHTAEIE  MIRKAIDGCG  RPIVLSLSPG240
ETPIDKMEHV  KTHANMWRTV  DDFWDNWSQL  NYQFQVCAKW  APYIAPGTWP  DADMLPLGKI300
SIRGERGAER  WTNFTTDEQY  TMMNLWTIFK  SPLMFGGDLP  QNDEATDALL  TNRDVLYMHH360
YSANNRQLSR  EDSRIIWAAD  DPANGDKFVA  LFNTGGTGYV  NTKNALYRSG  TISYLTTGYA420
TDIDVEIPEG  SRQLALVATD  GGDGYDCDHA  DWINPTVTLK  DGTKIDLTTQ  TYLRGTCGWG480
SVHVNQNLNG  GSLSIDGNTF  SKGFAVHANS  ILLFSLPENA  VRFTAHAGID  NTGSDQGSKS540
SVEFLVFNED  ATMREEKTDQ  WSGGNVTLKV  DPGKQVACSD  YISRKSIAQQ  ELEANIAGAQ600
KLYLVVTNGG  DGLAYDHANW  VNPVLVGEDG  KETSLTTIAW  DANPVNGWEA  PKLNKNNDGG660
TLKLGGVSYD  KGFGVNAPSQ  LAFTLPEGHN  YQTLKVLVGY  DSGVENASEG  VTMEFRIFTE720
SPEPDNATAV  PLDLAQLGFG  ADQPCRITEM  WTGREEGVFK  NADFAPVLRE  HASGLYRVAA780
TERAAGATVS  IEVPSGELTS  AEAFDIKMTV  SGGASEGAYV  QLLCDGKVIG  TLPVEADGTA840
TYVCSDLYGG  DHVLKAKYSG  TQSVASAESE  EVRITVTGAA  EDLTQLQKRL  QNLIEDAQKV900
NPLQVAGANR  GPLADAIEAA  QPVEEKTKAQ  LEAAITALQE  ALDAARLTMS  SMSALRAAID960
ETTVFLNAIS  ESPAKTSLVA  VIEECEGVYA  GVSSTKADVD  AAREKLTVQV  SETKKTAQPA1020
EGSKFDMTEF  LVNPSFEQQT  TGWRTANKVS  GWESFSTWGD  RPAADGSNFV  SVAYENITSI1080
DLYQVVNGLP  AGIYELEASL  RNTDGTSFLK  DQHVYAQVGT  DVYDSEKLTQ  VSGENNNDWY1140
RFTVSGIALG  EGGQLRLGVR  SSGNGTGRVG  WFQADDFRLY  YHGVSPDAVH  TAVAGVEGVD1200
VTLCAGGVRI  CSSVECMLPV  YSLGGSLVRT  ISVQVGTQDV  SLPQGQYVLN  GKVVVIK1257

Enzyme Prediction      help

EC 3.2.1.88

CAZyme Signature Domains help

Created with Snap621251882513143774395025656286917548178799421005106811311194189397GH27472625CBM51
Family Start End Evalue family coverage
GH27 189 397 6.6e-58 0.851528384279476
CBM51 472 625 6.4e-26 0.9402985074626866

CDD Domains      download full data without filtering help

Created with Snap62125188251314377439502565628691754817879942100510681131119434356GH2728374PLN0289934367PLN0323133356Melibiase_25397PLN02808
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14792 GH27 6.95e-101 34 356 1 266
glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
PLN02899 PLN02899 4.16e-83 28 374 25 391
alpha-galactosidase
PLN03231 PLN03231 6.86e-72 34 367 1 354
putative alpha-galactosidase; Provisional
pfam16499 Melibiase_2 2.70e-39 33 356 1 279
Alpha galactosidase A.
PLN02808 PLN02808 5.62e-38 5 397 1 332
alpha-galactosidase

CAZyme Hits      help

Created with Snap62125188251314377439502565628691754817879942100510681131119427558APU68995.1|CBM51|GH273547QIL77713.1|CBM51|GH2724547QDA61431.1|CBM51|GH271547QJX48209.1|CBM51|GH2716549QNE38644.1|CBM51|GH27
Hit ID E-Value Query Start Query End Hit Start Hit End
APU68995.1 1.19e-234 27 558 36 566
QIL77713.1 4.06e-213 3 547 6 546
QDA61431.1 2.42e-209 24 547 28 548
QJX48209.1 1.54e-207 1 547 1 548
QNE38644.1 4.95e-207 16 549 20 550

PDB Hits      download full data without filtering help

Created with Snap621251882513143774395025656286917548178799421005106811311194293934NX0_A293934NXK_A313933CC1_A333931UAS_A333916F4C_B
Hit ID E-Value Query Start Query End Hit Start Hit End Description
4NX0_A 1.05e-135 29 393 20 387
Crystalstructure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_B Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_C Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_D Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_E Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_F Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_G Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_H Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
4NXK_A 1.54e-134 29 393 20 387
Crystalstructure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_B Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_C Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_D Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_E Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_F Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_G Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_H Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NZF_A Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_B Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_C Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_D Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_E Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_F Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_G Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_H Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus]
3CC1_A 3.43e-126 31 393 9 374
ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]
1UAS_A 2.97e-30 33 393 8 305
ChainA, alpha-galactosidase [Oryza sativa]
6F4C_B 4.46e-26 33 391 8 301
Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana]

Swiss-Prot Hits      download full data without filtering help

Created with Snap62125188251314377439502565628691754817879942100510681131119431378sp|Q8RX86|AGAL2_ARATH33378sp|P14749|AGAL_CYATE33393sp|Q9FXT4|AGAL_ORYSJ31393sp|Q8VXZ7|AGAL3_ARATH32396sp|Q9FT97|AGAL1_ARATH
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8RX86 1.39e-31 31 378 37 322
Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1
P14749 2.46e-31 33 378 55 338
Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1
Q9FXT4 4.32e-29 33 393 63 360
Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1
Q8VXZ7 4.39e-29 31 393 70 371
Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1
Q9FT97 1.71e-28 32 396 52 352
Alpha-galactosidase 1 OS=Arabidopsis thaliana OX=3702 GN=AGAL1 PE=2 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
0.000356 0.998912 0.000198 0.000201 0.000169 0.000151

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000854_00012.