1U0F,1DQR,1G98,1T10,2Q8N,2PGI,1ZZG,1GZD,1IAT,1IRI,1JLH


Conserved Protein Domain Family
SIS_PGI_2

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cd05016: SIS_PGI_2 
Click on image for an interactive view with Cn3D
Phosphoglucose isomerase (PGI) contains two SIS (Sugar ISomerase) domains. This classification is based on the alignment of the second SIS domain. PGI is a multifunctional enzyme which as an intracellular dimer catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. As an extracellular protein, PGI also has functions equivalent to neuroleukin (NLK), autocrine motility factor (AMF), and maturation factor (MF). Evidence suggests that PGI, NLK, AMF, and MF are closely related or identical. NLK is a neurotrophic growth factor that promotes regeneration and survival of neurons. The dimeric form of NLK has isomerase function, whereas its monomeric form carries out neurotrophic activity. AMF is a cytokine that stimulates cell migration and metastasis. MF mediates the differentiation of human myeloid leukemic HL-60 cells to terminal monocytic cells.
Statistics
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PSSM-Id: 240147
Aligned: 110 rows
Threshold Bit Score: 72.2469
Created: 11-Jun-2007
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
active sitedimer interface
Conserved site includes 2 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Structure:1U0F: Mus musculus Phosphoglucose isomerase binds Glucose 6-phosphate (G6P), contacts calculated at 3.5A
  • Structure:1U0F: Mus musculus Phosphoglucose isomerase binds inhibitor Erythrose 4-phosphate (E4P), contacts calculated at 3.5A
  • Structure:1T10: Leishmania mexicana Phosphoglucose isomerase binds Fructose-6-phosphate, contact calculated at 3.5A
  • Structure:1DQR: Oryctolagus cuniculus Phosphoglucose isomerase binds 6-phospho-D-gluconate, contact calculated at 3.5A
  • Structure:1G98: Oryctolagus cuniculus Phosphoglucose isomerase binds Arabinonate-5-phosphate, contact calculated at 3.5A
  • Comment:catalytic activity of PGI is dependent on dimer formation; a conserved histidine from chain B is required
  • Comment:phosphohexoses and inhibitors of both PGI enzymatic and cytokine activity share similar binding sites

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                            #   #                                                       
1U0F_A       334 ETHALLPYDqyMHRFAAYFQQGDMESNGKyitksgarvdhqtgpIVWGEpGTNGQHAFYQLIHQGtkmiPCDFLIpvqtq 413  house mouse
EDO73142     653 DKITIIASPg-IDTFGTWAEQLIAESTGK---------------EGVGI-IPVEGEPVGVPAVYGedrlFVYLRL----- 710  Methylobacteri...
NP_789360    251 AVEGKAAIAs-ESLIGNWIEQLLAESTGK---------------DLTGV-LPIVTNGDLSKVRLEgvsyFDVRLEdgs-- 311  Tropheryma whi...
NP_863888    348 SIRVMSVWSkaLESVGLWYDQLLAESNGKdgk----------gvTPLTTlNTRDLHSRHQQHQQGrndkVFNNVIvesqr 417  Rhodopirellula...
P47357       260 KIEVCIAYHslYEYLLLQHRQLFGESEGKndk----------slFPTFSiFTVDLHSMGQLYQEGekvfFETVIDvknpl 329  Mycoplasma gen...
NP_757854    260 YNEVFCVYEdaLRFFTEHLKQLFAESEGKegk----------glLPVNClFTTDLHSVGQFLQEGnqifFETCISiknpl 329  Mycoplasma pen...
Q9KX58       258 DVEIAITYEeqHEYLMLQHRQLFGESEGKsln----------slFPTYSvFTTDLHSMGQLYQDGkkifFETVFSfekan 327  Mycoplasma gal...
YP_810243    265 DVETIVGYEpqFRFLFEWWKQLMAESEGKdnk----------giYPTSAiFSTDLHSIGQYIQDGkkilFETILDitkpi 334  Oenococcus oen...
YP_001256458 258 DIELMCSYEpkLSFFIEWWKQLFAESEGKdnk----------glWVTGStFSTDLHSIGQIIQDGkkilFETILVskepl 327  Mycoplasma aga...
EDP24562     252 EIEYLVAHEfkLTYLQEWWKQLFAESEGKngk----------glYVESAiFTRDLHSFGQMIQDGnkitFETIIEvenlk 321  Peptostreptoco...
Feature 1                                                                                        
1U0F_A       414 h-----------------pirkgLHHKILLANFLAQTEalmkgklpeearkelqaagkspedlekllphkvfeGNRPTNS 476  house mouse
EDO73142     711 -----------------------ASQADARQDEAVKILe---------------------------------sEAQPVVR 734  Methylobacteri...
NP_789360    312 ---------------------rnSSENSSEKSIQSETEc----------------------------------ADKEFCA 336  Tropheryma whi...
NP_863888    418 tdslavghs-qrnqdtlndiaekTLPDIMAAAIKGTNDal-------------------------------haDGRPTTD 465  Rhodopirellula...
P47357       330 vninlppsd-fdnddeldflldkSLNEISDVAIDSVIKah-------------------------------yqANVSIIK 377  Mycoplasma gen...
NP_757854    330 ndvvinef--lkdedglgflngkKLDYINKVAASSTIDahh------------------------------idGKIDIIQ 377  Mycoplasma pen...
Q9KX58       328 knklklknsefnnddqldyltkkSVNQLNYVACEATKQah-------------------------------asAGVPIIE 376  Mycoplasma gal...
YP_810243    335 sdrvvpsa--ddntdnldyilnkPMKEVNEAALTATAQah-------------------------------tsAGVPNIL 381  Oenococcus oen...
YP_001256458 328 ydillske--kndddklnyldgkTVHKVNLSAFKGTLEahs------------------------------ktALVPNIV 375  Mycoplasma aga...
EDP24562     322 ndiiipli--eedfdklnylakkSLNDINKVAVTATRKah-------------------------------tdGDVPTVR 368  Peptostreptoco...
Feature 1                                                         
1U0F_A       477 IVftkltPFILGALIAMYEHKIFVQGIMWDINSFDQWGVELGKQLAKKI 525  house mouse
EDO73142     735 IDld--kAEQLPQEFFRFEIATAVAGAVLGINPFDQPDVEASKIETKKL 781  Methylobacterium populi BJ001
NP_789360    337 RI-----TAGLGEQFVLWEFATAVLGHILSINPFDQPDVEKAKEATRGI 380  Tropheryma whipplei TW08/27
NP_863888    466 IIlpqidTHVLGQLFQMLMIATVIEGRLLGINPYGQPGVEQYKTNMNKN 514  Rhodopirellula baltica SH 1
P47357       378 LTlkeqsAFMFGYFYFWLSVATVMSGSLLGHNVFNQPGVEVYKKLMFEK 426  Mycoplasma genitalium
NP_757854    378 INldnrnEESFGYLYSWFSKVVAMSGLLLKVNPFDQPGVEAYKSRMFTK 426  Mycoplasma penetrans HF-2
Q9KX58       377 IDvkensAYGFGYLYFWLCVATSVSALLLGHDPYNQPGVENYKQRMFKL 425  Mycoplasma gallisepticum
YP_810243    382 LQlddldEFNLGNLIYFFEAAVAVSGYLDGINPFDQPGVEIYKTNMFKI 430  Oenococcus oeni PSU-1
YP_001256458 376 IEiakldEYALGYLFQFFMRGLAISAYLLGVNPFDQPGVEIYKSNMFKI 424  Mycoplasma agalactiae PG2
EDP24562     369 IKvpkldAYNIGKLIYFFEMSCAISAYMLDVNPFDQPGVDNYKKNMYQL 417  Peptostreptococcus micros ATCC 33270

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