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cd05197: GH4_glycoside_hydrolases 
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Glycoside Hydrases Family 4
Glycoside hydrolases cleave glycosidic bonds to release smaller sugars from oligo- or polysaccharides. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by GH4 glycoside hydrolases. Other organisms (such as archaea and Thermotoga maritima) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. GH4 family members include 6-phospho-beta-glucosidases, 6-phospho-alpha-glucosidases, alpha-glucosidases/alpha-glucuronidases (only from Thermotoga), and alpha-galactosidases. They require two cofactors, NAD+ and a divalent metal (Mn2+, Ni2+, Mg2+), for activity. Some also require reducing conditions. GH4 glycoside hydrolases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.
Statistics
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PSSM-Id: 133425
View PSSM: cd05197
Aligned: 4 rows
Threshold Bit Score: 587.953
Threshold Setting Gi: 31615790
Created: 6-Dec-2005
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
Hierarchy
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Display:
 
Conserved site includes 15 residues -Click on image for an interactive view with Cn3D
Feature 1:NAD binding site [chemical binding site]
Evidence:

cd05197 is part of a hierarchy of related CD models.
Use the graphical representation to navigate this hierarchy.
cd05197 is a member of the superfamily cl17195.
cd00300:LDH_likecd00650:LDH_MDH_likecd00704:MDHcd01336:MDH_cytoplasmic_cytosoliccd01337:MDH_glyoxysomal_mitochondrialcd01338:MDH_choloroplast_likecd01339:LDH-like_MDHcd05197:GH4_glycoside_hydrolasescd05290:LDH_3cd05291:HicDH_likecd05292:LDH_2cd05293:LDH_1cd05294:LDH-like_MDH_nadpcd05295:MDH_likecd05296:GH4_P_beta_glucosidasecd05297:GH4_alpha_glucosidase_galactosidasecd05298:GH4_GlvA_pagL_like1OBB B1670390571500206591573642411609016171542500311VJT A20690110015643200160902319206901539126465608159041403119720416179056014026146156741863171059913671536581542523851162489261538896353912990892113321573713422069009172121907611846879256908427118725381140261412069005531462965741503841151609342841538907674691511815381621182946675399334558871261439157601462977332069002111608809791609387661U8X X18143856391401713364097210630474597984271609147575696384391224797150019792196247958212696968148378269890965083752590815001961421063199921062854516094430013943939816414976182417461116621044211094021184676941529642358449449829828296148271527721631675083915411996049516384044715450790615141176154496200518572771677553701UP7 A1UP4 H157362914206901232160931904134098175212211171567413701624471331503918842051532318241806328899408375266471544995801S6Y A1500188482106270661683332921561347523099728520787872506168167756326146321930289015501499082841674648231OBB B1670390571500206591573642411609016171542500311VJT A20690110015643200160902319206901539126465608159041403119720416179056014026146156741863171059913671536581542523851162489261538896353912990892113321573713422069009172121907611846879256908427118725381140261412069005531462965741503841151609342841538907674691511815381621182946675399334558871261439157601462977332069002111608809791609387661U8X X18143856391401713364097210630474597984271609147575696384391224797150019792196247958212696968148378269890965083752590815001961421063199921062854516094430013943939816414976182417461116621044211094021184676941529642358449449829828296148271527721631675083915411996049516384044715450790615141176154496200518572771677553701UP7 A1UP4 H157362914206901232160931904134098175212211171567413701624471331503918842051532318241806328899408375266471544995801S6Y A150018848210627066168333292156134752309972852078787250616816775632614632193028901550149908284167464823
cd05197 Sequence Cluster
cd05197 Sequence Cluster
Sub-family Hierarchy
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 cd05197 Branch
 Whole Hierarchy
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CD Hierarchy
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                      10        20        30        40        50        60        70        80
              ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1             ##                          ##     #                                    
1S6Y_A      8 LKIATIGGGSS-YTPELVEGLIKRyhELPVGELWLVDIPegKEKLEIVGALAKRXVEkagvpiEIHLTLDRRRALDGADF 86
1U8X_X     29 FSIVIAGGGST-FTPGIVLXLLDHleEFPIRKLKLYDND--KERQDRIAGACDVFIRekapdiEFAATTDPEEAFTDVDF 105
1OBB_B      4 VKIGIIGAGSAvFSLRLVSDLCKTp-GLSGSTVTLMDID--EERLDAILTIAKKYVEevgadlKFEKTMNLDDVIIDADF 80
1UP7_A      3 MRIAVIGGGSS-YTPELVKGLLDIseDVRIDEVIFYDID--EEKQKIVVDFVKRLVKdr---fKVLISDTFEGAVVDAKY 76
                      90       100       110       120       130       140       150       160
              ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1        ###  ##                            #           #                   # #       
1S6Y_A     87 VTTQFRVGGLEARAKDERIPLKYGVIg------QETNGPGGLFKGLRTIpVILDIIRDXEELCpDAWLINFTNPAGXVTE 160
1U8X_X    106 VXAHIRVGKYAXRALDEQIPLKYGVVg------QETCGPGGIAYGXRSIgGVLEILDYXEKYSpDAWXLNYSNPAAIVAE 179
1OBB_B     81 VINTAMVGGHTYLEKVRQIGEKYGYYrgidaqeFNMVSDYYTFSNYNQLkYFVDIARKIEKLSpKAWYLQAANPIFEGTT 160
1UP7_A     77 VIFQFRPGGLKGRENDEGIPLKYGLIg------QETTGVGGFSAALRAFpIVEEYVDTVRKTS-NATIVNFTNPSGHITE 149
                     170       180       190       200       210       220       230       240
              ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                  #                                                                  
1S6Y_A    161 AVLRYtkqEKVVGLCNVPIGXRXGVAKLLgv-daDRVHIDFAGLNHXVFGLHVYLD-GVEVTEKVIDLVAHPDrsgvtxk 238
1U8X_X    180 ATRRLrpnSKILNICDXPVGIEDRXAQILglssrKEXKVRYYGLNHFGWWTSIQDQeGNDLXPKLKEHVSQYGyipktea 259
1OBB_B    161 LVTRTv-pIKAVGFXHGHYGVMEIVEKLGle--eEKVDWQVAGVNHGIWLNRFRYN-GGNAYPLLDKWIEEKSkdwkpen 236
1UP7_A    150 FVRNYleyEKFIGLCNVPINFIREIAEMFsa-rlEDVFLKYYGLNHLSFIEKVFVK-GEDVTEKVFENLKLKLsnipded 227
                     250       260       270       280       290       300       310       320
              ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                     
1S6Y_A    239 nivd-------lgwepdflkgLKVLPCPYHRYYFqtdkxlaee------------leaaktkgTRAEVVQQL-EKELFEL 298
1U8X_X    260 eaveaswndtfakardvqaadPDTLPNTYLQYYLfpddxvk----------------ksnpnhTRANEVXEGrEAFIFSQ 323
1OBB_B    237 pfndq-----lspaaidmyrfYGVMPIGDTVRNSswryhrdletkkkwygepwggadseigwkWYQDTLGKV-TEITKKV 310
1UP7_A    228 f-------------ptwfydsVRLIVNPYLRYYLmekkmfk----------------kistheLRAREVMKI-EKELFEK 277
                     330       340       350       360       370       380       390       400
              ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                     
1S6Y_A    299 YKdpnlaikp---------------------pqlekrggAYYSDAACSLISSIYNDKRDIQPVNTRNNGAIASISAESAV 357
1U8X_X    324 CDxitreqss----------------------enseikiDDHASYIVDLARAIAYNTGERXLLIVENNGAIANFDPTAXV 381
1OBB_B    311 AKfikenpsvrlsdlgsvlgkdlsekqfvlevekildpeRKSGEQHIPFIDALLNDNKARFVVNIPNKGIIHGIDDDVVV 390
1UP7_A    278 YRtaveipe-----------------------eltkrggSMYSTAAAHLIRDLETDEGKIHIVNTRNNGSIENLPDDYVL 334
                     410       420       430       440       450       460       470
              ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
Feature 1                                                                                  
1S6Y_A    358 EVNCVITKDGPKPIA-VGDl-PVAVRGLVQQIKSFERVAAEAAVtGDYQTALVAXTINPlVPSDTIAKQILDEXLEA 432
1U8X_X    382 EVPCIVGSNGPEPIT-VGTi-PQFQKGLXEQQVSVEKLTVEAWAeKSFQKLWQALILSKtVPNARVARLILEDLVEA 456
1OBB_B    391 EVPALVDKNGIHPEKiEPPlpDRVVKYYLRPRIMRMEMALEAFLtGDIRIIKELLYRDPrTKSDEQVEKVIEEILAL 467
1UP7_A    335 EIPCYVRSGRVHTLS-QGKg-DHFALSFIHAVKMYERLTIEAYLkRSKKLALKALLSHPlGPDVEDAKDLLEEILEA 409

Citing CDD
Marchler-Bauer A et al. (2013), "CDD: conserved domains and protein three-dimensional structure.", Nucleic Acids Res. 41(D1):D384-52.
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Click on image for an interactive view with Cn3D
Conserved site includes 15 residues -Click on image for an interactive view with Cn3D