2B5D,3N98,1XW8,2I5I,1QWU


Conserved Protein Domain Family
GH38-57_N_LamB_YdjC_SF
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cd10785: GH38-57_N_LamB_YdjC_SF 
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Catalytic domain of glycoside hydrolase (GH) families 38 and 57, lactam utilization protein LamB/YcsF family proteins, YdjC-family proteins, and similar proteins.
The superfamily possesses strong sequence similarities across a wide range of all three kingdoms of life. It mainly includes four families, glycoside hydrolases family 38 (GH38), heat stable retaining glycoside hydrolases family 57 (GH57), lactam utilization protein LamB/YcsF family, and YdjC-family. The GH38 family corresponds to class II alpha-mannosidases (alphaMII, EC 3.2.1.24), which contain intermediate Golgi alpha-mannosidases II, acidic lysosomal alpha-mannosidases, animal sperm and epididymal alpha -mannosidases, neutral ER/cytosolic alpha-mannosidases, and some putative prokaryotic alpha-mannosidases. AlphaMII possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyzes the degradation of N-linked oligosaccharides by employing a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. GH57 is a purely prokaryotic family with the majority of thermostable enzymes from extremophiles (many of them are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57 cleaves alpha-glycosidic bond by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation. Although the exact molecular function of LamB/YcsF family and YdjC-family remains unclear, they show high sequence and structure homology to the members of GH38 and GH57. Their catalytic domains adopt a similar parallel 7-stranded beta/alpha barrel, which is remotely related to catalytic NodB homology domain of the carbohydrate esterase 4 superfamily.
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Statistics
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PSSM-Id: 212097
Aligned: 5 rows
Threshold Bit Score: 123.137
Created: 24-May-2011
Updated: 2-Oct-2020
Structure
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Sequence Alignment
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2B5D_X    6 LIFLH.[26].TYIPLLMMF.[ 7].LTMSITP.[76].KLEIVTC.[13].PEVVNAQITVGVKNYEK.[4].HPRGIW 182  Thermotoga maritima MSB8
3N98_A    6 TFVLH.[25].TYIPLLMEF.[11].IVINVTP.[72].YVEVITS.[12].DEAIRAQIANGVATYEK.[4].KPKGIW 180  Thermococcus kodakarensis
1XW8_A    4 DLNAD.[ 6].SDAELLTLV      SSANIAC.[20].GVAIGAH.[17].PETVYAQTLYQIGALAT.[7].VXRHVK 104  Escherichia coli
2I5I_A    8 IINAD.[ 7].VTQGIIEAH.[ 5].TSTTALP.[17].TLAIGVH.[38].LEEVYNEWDAQIISFXK.[3].RPDHID 128  Enterococcus faecalis V583
1QWU_A   84 FVVPH.[21].ILSNALRHL.[ 5].MKFIWAE.[26].QLEFVTG.[11].WRNVLLQLTEGQTWLKQ.[4].TPTASW 201  fruit fly


2B5D_X  183 LAE.[ 5].GLDLYLAQ.[3].EYFFV.[24].GVFAF.[108].IVAPFD.[12].FFLKRF 367  Thermotoga maritima MSB8
3N98_A  181 LPE.[20].GIEKFLEE.[3].RYFFV.[35].NVAVF.[ 89].IVAPYD.[12].KWLGRV 372  Thermococcus kodakarensis
1XW8_A  105 PHG.[14].AIARAVYA.[4].LILVG.[13].GLTTR.[ 56].QTVCLH.[ 7].AFARRL 231  Escherichia coli
2I5I_A  129 SHH.[11].VALALARK.[2].LPLRN.[15].DVRTP.[ 31].FEINCH.[22].EILTSQ 242  Enterococcus faecalis V583
1QWU_A  202 AID.[ 6].TMPYILQK.[3].KNMLI.[31].ALFTH.[ 71].LLIPLG.[15].VNYERL 360  fruit fly
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