2FUE,3F9R,2I55,2AMY,4BND


Conserved Protein Domain Family
HAD_PMM

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cd02585: HAD_PMM 
Click on image for an interactive view with Cn3D
phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis thaliana PMM
PMM catalyzes the interconversion of mannose-6-phosphate (M6P) to mannose-1-phosphate (M1P); the conversion of M6P to M1P is an essential step in mannose activation and the biosynthesis of glycoconjugates in all eukaryotes. M1P is the substrate for the synthesis of GDP-mannose, which is an intermediate for protein glycosylation, protein sorting and secretion, and maintaining a functional endomembrane system in eukaryotic cells. Proteins in this family contains a conserved phosphorylated motif DxDx(T/V) shared with some other phosphotransferases. This family contains two human homologs, PMM1 and PMM2; PMM2 deficiency causes congenital disorder of glycosylation type I-a, also known as Jaeken syndrome. PMM1 can also act as glucose-1,6-bisphosphatase in the brain after stimulation with inosine monophosphate; PMM2 on the other hand, is insensitive to IMP and demonstrates low glucose-1,6-bisphosphatase activity. Arabidopsis thaliana PMM converted M1P into M6P and glucose-1-phosphate into glucose-6-phosphate, with the latter reaction being less efficient. Arabidopsis thaliana and Nicotiana benthamian PPMs are involved in ascorbic acid biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.
Statistics
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PSSM-Id: 319784
View PSSM: cd02585
Aligned: 22 rows
Threshold Bit Score: 274.923
Threshold Setting Gi: 311064130
Created: 25-Jun-2004
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 24 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1           #####    #                          ###   #                                 
2FUE_A       15 LCLFDVDGTLTPARqkidpEVAAFLQKLRsr---vQIGVVGGSDYCKIAEQLGdgde--viekFDYVFAENGTVQYKH-- 87
4BND_B        5 ILSFDIDNTLNEPKmpifpEMAELLATLSqk---yIIAPISGQKYDQFLIQIInnlpesanldNFHLFVAQGTQYYAHka 81
gi 41688600   5 MLIFDMDGTLTDPVqvinnDVKDILRRCKrk--nfEIAVVSGSKYEKIKGQLNdgf----ideFDYVFSENGTQVYVK-- 76
gi 46226758  16 LFLFDLDGTLTLPRk---pIMEDMVMTLKnakskvKIGVVSGSDYSKICEQLQnne----lacSHYIFSENGVVFHDE-- 86
gi 19173562   8 IFLFDVDGTLSESRakmpeKMGKMLESLRrk---vRIGFVGGSDLAKQKEQVGdni----leiFDYGFPENGVSFYKN-- 78
gi 12585299  12 LLLFDVDGTLTMPRsvvtpEFEEFFYSRVkp--raTIGIVGGSDLEKMFEQLNgrki---lneFDFIFPENGLVQIEG-- 84
gi 83767130  21 ICLFDVDGTLTPARrtispEMLQLLSQLRhk---cAIGTVGGSDLAKQQEQLGtsstk-vsslFDFCFAENGLTAIRL-- 94
gi 47156906   8 IFLFDVDGTLTRSRqkiepKMKETLQRLKkv---vYTAFVGGSDLQKQEEQIGddc----ldlFDFGFPENGVSFYRG-- 78
gi 74856304   8 ICLFDVDGTLTKPRnvitpEMKDFLAGLRtk---vELGVVGGSDINKIKEQLGenc----ineFHYLFAENGLLSFKD-- 78
gi 15672552   4 ILSFDIDNTLNEPKmpifpEMAELLATLSqk---yIIAPISGQKYDQFLIQIInnlpesanldNFHLFVAQGTQYYAH-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                        #    #     #      #            
2FUE_A       88 GRLLSKQtiqnhLGEELLQDLINFCLSYXALLRLPk-----KRGTFIEFRNGXLNISPIGRSCTLEER-IEFSELDKKEK 161
4BND_B       82 GEWKQVFny--aLTDEQANAIMGALEKAAKELGHWdesvllPGDEINENRESMIAYSAIGQKAGVEAKqAWDPDMTKRNE 159
gi 41688600  77 NVLVKSLditeaIPETKLRKMVEFCLRYIADLDIPt-----KRGTFIEHRKSLINICPPGRNCSMVDR-RRFVEYDSIHH 150
gi 46226758  87 GVKVSSEsiskhLGEDNIKRFVNFCLRYIADLDIPi-----KRGTFIEYRTGMLNISPIGRNCSYDER-LEFFELDKKNG 160
gi 19173562  79 GTLESQEkiidvLGEEFYKEFANFVLRYLSDIDLPi-----KRGNFIEYRNSMINISPIGRNCSREER-MKFFELDKKEK 152
gi 12585299  85 GKEVGKQniimhLGEETVKRFINFVLRYLSELDVPi-----KRGTFIEFRNGMMNVCPIGRQCTREER-NMFAEYDIEHK 158
gi 83767130  95 GRFLASNsfiawIGEEKYQKLANFCLKYIADLQLPk-----KRGTFVEFRNGMINVSPVGRNASVDER-IEFEAYDKQHN 168
gi 47156906  79 RELVSQEsiiefMGEELHRELVEFTMRYIADLDIPv-----KRGTFLELRRSMINISPIGRNCSQDER-MMFFSLDKERG 152
gi 74856304  79 GSLLATQdikkfLGEENIKKFINFVLHYIADLDIPi-----KRGTFVEFRNGMINISPIGRNCSQQER-EEFEKYDLEHK 152
gi 15672552  79 KDGEWKQvfnyaLTDEQANAIMGALEKAAKELGHWdesvlaPGDEINENRESMIAYSAIGQKAGVEAKqAWDPDMTKRNE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                #### #       #                        ##      ##       
2FUE_A      162 IReKFVEALktef--agkgLRFSRGGXISFDVFPeGWDKRYCLDSLDqds------fdtIHFFGNEtspGGNDFEIFADp 233
4BND_B      160 IA-KLASQYap-------eFEFEVAGTTTINGFVpGQNKEFGMNHLMeelnv---tkeeILYFGDMtqpGGNDYPVVQM- 227
gi 41688600 151 VRqKLIQVLksqfdsddcpLSFVAGGQISIDVYPkAWSKSIALSHIGkc--------dvIHFFGDNtreGGNDFEIYNHp 222
gi 46226758 161 IReKFIQDLskef--sdldLQYSIGGQISIDVFPqGWDKRYCLRHVEnkf-------deIHFFGDKtypGGNDHEIYNDk 231
gi 19173562 153 FReKMVTAMrdrf--kdscLVFSIGGQISIDCFPkGWDKTYCLRHIKkeg------venVYFFGDMtmeGGNDYEIYNHk 224
gi 12585299 159 VReKMIKDLkqef--advdLTYSIGGQISFDVFPhGWDKTYCLRHIEahyk-----fkeIHFFGDKtepGGNDYEIYSDp 231
gi 83767130 169 IRkSFVEALktef--pdynLSYSIGGQISFDVFPaGWDKTYCLRHIEaekdisgikyktIHFFGDKsfpGGNDYEIYTDs 246
gi 47156906 153 IRkEMVRELerrf--gergMHFCIGGQISIDCFPkGWDKTYCLRHLRdf--------ntIVFFGDKtekGGNDYEILTDe 222
gi 74856304 153 IRpTMVSILkekf--qslgLQYSIGGQISFDVFPiGWDKTYCLRHLPedk------yktIYFFGDKtfvGGNDYEIANDp 224
gi 15672552 159 IA-KLASQYap-------eFEFEVAGTTTINGFVpGQNKEFGMNHLMeelnv---tkeeILYFGDMtqpGGNDYPVVQMg 227
                       250       260
                ....*....|....*....|.
Feature 1                            
2FUE_A      234 -RTVGHSVvsPQDTVQRCREI 253
4BND_B      228 -GIETITVrdWKETAAILKAI 247
gi 41688600 223 -DVIGHTVtgYKDLVNQLEEL 242
gi 46226758 232 -RVIGHNVinPNDTIQQLSRL 251
gi 19173562 225 -DVHGISVgnPDDTYRKVDQA 244
gi 12585299 232 -RTISHRVytPKDTQRILTEI 251
gi 83767130 247 -RTIGHAVkdPDDTMKQLKEI 266
gi 47156906 223 -RTVSVSVscPEDTIQKIDEM 242
gi 74856304 225 rITKSFTVtsPTDTKNFLSEL 245
gi 15672552 228 iETITVRD--WKETAAILKAI 246

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