logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001535_01387

You are here: Home > Sequence: MGYG000001535_01387

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 Paenibacillus_A phocaensis
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A phocaensis
CAZyme ID MGYG000001535_01387
CAZy Family GH36
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
700 MGYG000001535_12|CGC6 79532.6 5.4471
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001535 5515101 Isolate not provided not provided
Gene Location Start: 301647;  End: 303749  Strand: -

Full Sequence      Download help

MSRIELQENG  LYLVIEVAQE  KEVRLLHFGA  SPLDETRIKE  GQKSGFRLME  LQLTGEDRAE60
YHGRTHRASY  PGLRMVYAGH  TNCRNELGRK  LEVTLRDPKT  GLEAVQHVQF  YDGVQTVRAW120
TELYNAGSAA  VSVEYVSSFA  LTGLDKEGGQ  DRDDKMTLSI  PHSGWQSELQ  WRTYRLPELG180
LSHLTDRSSK  RISCSNTGSW  SAAEHIPMAV  LENRETNSSL  FWQIEHNGSW  HWEIFDQVDQ240
LTLLLSGPTE  HDNHWWKSLL  PGERFVGVPV  AVGATKGGFE  AAIGQLTAYR  RRIRRPNADN300
RELRIIFNDY  MNCLWGSPTT  EKLLPLIDAA  ADAGCEYFCI  DAGWYAPGEW  WDGVGEWMPS360
SERFPEGIKY  VLDYIRSKGM  VPGLWLELEV  MGINSPKLAD  TDDSWFFLRH  GKRVMDRSRY420
QLDYRNPKVT  AHADEVIRRL  VEDYGVGYIK  MDYNINAGIG  TEASADSFGD  GLLQHNRAYL480
AWLDRIFARY  PELVIENCSS  GGMRMDYAML  SRHSIQSTSD  QENYVNYAAI  AAASPSAVTP540
EQSAVWSYPL  REGDDEEVVF  NMVNALLLRV  HQSGHLAELS  PRRRELVKEA  LDYYKSIRAD600
IPEALPFWPL  GLPKQQDEWV  SLGLRRPGSD  TMYLAVWRTR  GDITSQALPL  LALQGEEPDI660
RCAYPRDLDC  AWSWNAADGQ  LTVTLPPAPS  ARLFEIRRQR  700

Enzyme Prediction      help

No EC number prediction in MGYG000001535_01387.

CAZyme Signature Domains help

Created with Snap35701051401752102452803153503854204554905255605956306655659GH36
Family Start End Evalue family coverage
GH36 5 659 4.5e-97 0.9607558139534884

CDD Domains      download full data without filtering help

Created with Snap3570105140175210245280315350385420455490525560595630665305595GH36289510Melibiase319520GalA331470GH27332387Melibiase_2
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14791 GH36 2.43e-89 305 595 4 298
glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 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. GH36 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.
pfam02065 Melibiase 3.24e-30 289 510 27 250
Melibiase. Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27.
COG3345 GalA 4.35e-18 319 520 307 505
Alpha-galactosidase [Carbohydrate transport and metabolism].
cd14792 GH27 1.80e-10 331 470 33 140
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.
pfam16499 Melibiase_2 7.29e-06 332 387 45 98
Alpha galactosidase A.

CAZyme Hits      help

Created with Snap35701051401752102452803153503854204554905255605956306653695QMV41922.1|GH368697QJD85481.1|GH363696CQR54700.1|GH363696QQZ59050.1|GH364696AIQ17108.1|GH36
Hit ID E-Value Query Start Query End Hit Start Hit End
QMV41922.1 0.0 3 695 4 694
QJD85481.1 0.0 8 697 9 698
CQR54700.1 0.0 3 696 5 696
QQZ59050.1 0.0 3 696 5 696
AIQ17108.1 0.0 4 696 6 696

PDB Hits      download full data without filtering help

Created with Snap3570105140175210245280315350385420455490525560595630665915062XN0_A915062XN2_A2596594FNQ_A2375063MI6_A2016592YFN_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2XN0_A 7.05e-21 91 506 137 538
Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN0_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN1_A Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_C Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_D Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM]
2XN2_A 9.31e-21 91 506 137 538
Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM]
4FNQ_A 1.83e-18 259 659 284 687
Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
3MI6_A 6.88e-17 237 506 263 535
ChainA, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_B Chain B, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_C Chain C, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_D Chain D, Alpha-galactosidase [Levilactobacillus brevis ATCC 367]
2YFN_A 1.06e-15 201 659 224 679
galactosidasedomain of alpha-galactosidase-sucrose kinase, AgaSK [[Ruminococcus] gnavus E1],2YFO_A GALACTOSIDASE DOMAIN OF ALPHA-GALACTOSIDASE-SUCROSE KINASE, AGASK, in complex with galactose [[Ruminococcus] gnavus E1]

Swiss-Prot Hits      download full data without filtering help

Created with Snap357010514017521024528031535038542045549052556059563066591506sp|G1UB44|MELA_LACAC91509sp|P43467|AGAL1_PEDPE195510sp|P27756|AGAL_STRMU321512sp|P16551|RAFA_ECOLX201659sp|G4T4R7|AGASK_RUMGN
Hit ID E-Value Query Start Query End Hit Start Hit End Description
G1UB44 3.86e-20 91 506 137 538
Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1
P43467 6.75e-20 91 509 135 539
Alpha-galactosidase 1 OS=Pediococcus pentosaceus OX=1255 GN=agaR PE=3 SV=1
P27756 5.23e-17 195 510 213 531
Alpha-galactosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=aga PE=3 SV=3
P16551 1.09e-15 321 512 309 497
Alpha-galactosidase OS=Escherichia coli OX=562 GN=rafA PE=1 SV=1
G4T4R7 6.98e-15 201 659 224 679
Bifunctional alpha-galactosidase/sucrose kinase AgaSK OS=Ruminococcus gnavus OX=33038 GN=agaSK PE=1 SV=1

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
1.000047 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001535_01387.