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CAZyme Information: MGYG000002271_02971

You are here: Home > Sequence: MGYG000002271_02971

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 GCA-900066135 sp900066135
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; GCA-900066135; GCA-900066135 sp900066135
CAZyme ID MGYG000002271_02971
CAZy Family GH27
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
641 MGYG000002271_20|CGC1 72880.01 4.9636
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002271 3727782 Isolate China Asia
Gene Location Start: 27707;  End: 29632  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002271_02971.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 375 619 2.5e-16 0.9606986899563319

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14792 GH27 1.96e-14 247 549 2 265
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.
cd14791 GH36 1.94e-08 247 539 3 293
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCK01163.1 4.42e-249 10 639 19 683
AYQ71136.1 2.14e-136 11 638 30 678
QGQ94687.1 2.59e-121 93 639 110 669
ANE45666.1 6.06e-121 9 612 29 654
ACX66631.1 4.17e-120 121 639 152 681

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      help

has no Swissprot hit.

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
1.000044 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002271_02971.