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Conserved domains on  [gi|1088501618|gb|OHD32073|]
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mannose-6-phosphate isomerase, class I [Spirochaetes bacterium GWC2_52_13]

Protein Classification

class I mannose-6-phosphate isomerase( domain architecture ID 14401446)

mannose-6-phosphate isomerase, class I, catalyzes the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P), the first committed step in the synthesis of mannosylated glycoproteins

CATH:  2.60.120.10
EC:  5.3.1.8
Gene Ontology:  GO:0004476|GO:0009298|GO:0008270
SCOP:  3001825

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cupin_PMI_type_I_N cd07011
type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This ...
6-306 3.16e-91

type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This subfamily contains type I phosphomannose isomerase (PMI; E.C. 5.3.1.8; also known as mannose-6-phosphate isomerase) found in eukaryotes and some bacteria such as Salmonella enterica. PMI catalyzes the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P), the first committed step in the synthesis of mannosylated glycoproteins. The active site, located within the N-terminal jelly roll-like beta-barrel cupin fold, contains a single essential zinc atom and forms a deep, open cavity large enough to contain M6P or F6P. PMI type I also has a C-terminal beta-barrel fold which has diverged considerably from the N-terminal domain and is not included here. This subfamily contains an alpha helical domain that is found in eukaryotic and some prokaryotic PMIs but is not present in their archaeal counterparts. F6P is a substrate for glycolysis and gluconeogenesis, while M6P is a substrate for production of activated mannose donor guanosine 5'-diphosphate D-mannose, an important precursor of mannosylated biomolecules such as glycoproteins, bacterial exopolysaccharides and fungal cell wall components. PMI is also essential for survival, virulence and possibly pathogenicity of some bacteria and protozoan parasites, as well as for cell wall integrity of certain yeasts. Thus, PMI is a potential target against fungal infections causing serious illness or death.


:

Pssm-ID: 380414 [Multi-domain]  Cd Length: 247  Bit Score: 274.81  E-value: 3.16e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618   6 ITPKVQPYPWGDDSFIPSL---LGKKPDGKPQAELWFGTHpggesalpdseplgdflrdhdkeflgeeqvkrhgkeLPFL 82
Cdd:cd07011     1 LKNAVQNYAWGSKGAISLLargGGKIPEGKPYAELWMGTH------------------------------------LPFL 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618  83 LKVLAIAQPLSLQVHPSAEQALHGYTEElPRhvdipqdqwNYKDGRQKAEVLYALTPVTAMCGFLPIAKLSANLLRLLPy 162
Cdd:cd07011    45 FKVLSAAKPLSIQAHPDKEQAEKLFARE-PE---------NYKDPNHKPEMAIALTPFEALCGFRPLEEILALLERVPP- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 163 qfpLVFPFLQEPEEKDEARLLQRFFTTLYTLE--QEQRKLLLTEFKENLELLQEDSytvDGNWltpggIARLClESYPDD 240
Cdd:cd07011   114 ---ELRELLGQEDAEQSKEGLKALFSALLTLDsdEEALAALVARLRARPKSEELDE---AEEL-----VLRLA-EQYPGD 181
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1088501618 241 PGVFAPFFLHVLHLKPGEAVYLEPRTLHAYVRGHGIELMSNSDNVLRGGLTNKKVDVPELLQTLAF 306
Cdd:cd07011   182 PGVFAALLLNLVTLKPGEAIFLPAGEPHAYLSGDGVECMANSDNVVRAGLTPKHVDVDELLRMLDY 247
 
Name Accession Description Interval E-value
cupin_PMI_type_I_N cd07011
type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This ...
6-306 3.16e-91

type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This subfamily contains type I phosphomannose isomerase (PMI; E.C. 5.3.1.8; also known as mannose-6-phosphate isomerase) found in eukaryotes and some bacteria such as Salmonella enterica. PMI catalyzes the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P), the first committed step in the synthesis of mannosylated glycoproteins. The active site, located within the N-terminal jelly roll-like beta-barrel cupin fold, contains a single essential zinc atom and forms a deep, open cavity large enough to contain M6P or F6P. PMI type I also has a C-terminal beta-barrel fold which has diverged considerably from the N-terminal domain and is not included here. This subfamily contains an alpha helical domain that is found in eukaryotic and some prokaryotic PMIs but is not present in their archaeal counterparts. F6P is a substrate for glycolysis and gluconeogenesis, while M6P is a substrate for production of activated mannose donor guanosine 5'-diphosphate D-mannose, an important precursor of mannosylated biomolecules such as glycoproteins, bacterial exopolysaccharides and fungal cell wall components. PMI is also essential for survival, virulence and possibly pathogenicity of some bacteria and protozoan parasites, as well as for cell wall integrity of certain yeasts. Thus, PMI is a potential target against fungal infections causing serious illness or death.


Pssm-ID: 380414 [Multi-domain]  Cd Length: 247  Bit Score: 274.81  E-value: 3.16e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618   6 ITPKVQPYPWGDDSFIPSL---LGKKPDGKPQAELWFGTHpggesalpdseplgdflrdhdkeflgeeqvkrhgkeLPFL 82
Cdd:cd07011     1 LKNAVQNYAWGSKGAISLLargGGKIPEGKPYAELWMGTH------------------------------------LPFL 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618  83 LKVLAIAQPLSLQVHPSAEQALHGYTEElPRhvdipqdqwNYKDGRQKAEVLYALTPVTAMCGFLPIAKLSANLLRLLPy 162
Cdd:cd07011    45 FKVLSAAKPLSIQAHPDKEQAEKLFARE-PE---------NYKDPNHKPEMAIALTPFEALCGFRPLEEILALLERVPP- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 163 qfpLVFPFLQEPEEKDEARLLQRFFTTLYTLE--QEQRKLLLTEFKENLELLQEDSytvDGNWltpggIARLClESYPDD 240
Cdd:cd07011   114 ---ELRELLGQEDAEQSKEGLKALFSALLTLDsdEEALAALVARLRARPKSEELDE---AEEL-----VLRLA-EQYPGD 181
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1088501618 241 PGVFAPFFLHVLHLKPGEAVYLEPRTLHAYVRGHGIELMSNSDNVLRGGLTNKKVDVPELLQTLAF 306
Cdd:cd07011   182 PGVFAALLLNLVTLKPGEAIFLPAGEPHAYLSGDGVECMANSDNVVRAGLTPKHVDVDELLRMLDY 247
PRK15131 PRK15131
mannose-6-phosphate isomerase; Provisional
3-400 1.50e-83

mannose-6-phosphate isomerase; Provisional


Pssm-ID: 185085 [Multi-domain]  Cd Length: 389  Bit Score: 260.29  E-value: 1.50e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618   3 MVKITPKVQPYPWGDDSFIPSLLG-KKPDGKPQAELWFGTHPGGESALPDSEPLGDFLRDH---DKE-FLGEEQVKRHGk 77
Cdd:PRK15131    1 MQKMINSVQNYAWGSKTALTELYGiANPDNQPMAELWMGAHPKSSSRVQDANGDIVSLRDViesDKSaLLGEAVAKRFG- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618  78 ELPFLLKVLAIAQPLSLQVHPSAEQALHGYTEElpRHVDIPQD--QWNYKDGRQKAEVLYALTPVTAMCGFLPIAKLsAN 155
Cdd:PRK15131   80 ELPFLFKVLCAAQPLSIQVHPNKRAAEIGFAKE--NAAGIPLDaaERNYKDPNHKPELVFALTPFLAMNAFREFSEI-VS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 156 LLRLLPYQFPLVFPFLQEPEEKDEARLlqrfFTTLYTLEQEQRKLLLTEFKENLELLQEDSytvdgnWLTPGGIArlclE 235
Cdd:PRK15131  157 LLQPVAGAHPAIAHFLQQPDAERLSEL----FASLLNMQGEEKSRALAVLKSALNSQQGEP------WQTIRLIS----E 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 236 SYPDDPGVFAPFFLHVLHLKPGEAVYLEPRTLHAYVRGHGIELMSNSDNVLRGGLTNKKVDVPELLQTLAFKAYNAG-LC 314
Cdd:PRK15131  223 FYPDDSGLFSPLLLNVVKLNPGEAMFLFAETPHAYLQGVALEVMANSDNVLRAGLTPKYIDIPELVANVKFEAKPANqLL 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 315 PQIRDTNNRLNILAPTDDFLLGVYE-RGTYHVGNRFSIEFLLCSEGTAEVVKDNQTHKLAQGE-CLVVASsvDSyRITVK 392
Cdd:PRK15131  303 TQPVKQGAELDFPIPVDDFAFSLHDlSDQPTTLSQQSAAILFCVEGEAVLWKGEQQLTLKPGEsAFIAAN--ES-PVTVS 379

                  ....*...
gi 1088501618 393 GKVFSASV 400
Cdd:PRK15131  380 GHGRLARV 387
manA TIGR00218
mannose-6-phosphate isomerase, class I; The names phosphomannose isomerase and ...
5-393 6.35e-37

mannose-6-phosphate isomerase, class I; The names phosphomannose isomerase and mannose-6-phosphate isomerase are synonomous. This family contains two rather deeply branched groups. One group contains an experimentally determined phosphomannose isomerase of Streptococcus mutans as well as three uncharacterized paralogous proteins of Bacillus subtilis, all at more than 50 % identity to each other, plus a more distant homolog from Archaeoglobus fulgidus. The other group contains members from E. coli, budding yeast, Borrelia burgdorferi, etc. [Energy metabolism, Sugars]


Pssm-ID: 272966 [Multi-domain]  Cd Length: 302  Bit Score: 136.02  E-value: 6.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618   5 KITPKVQPYPWGDdSFIPSLLGKKPDGKPQAELW-FGTHPGGES----ALPDSEPLGDFLRDHdKEFLGEEQvkrhGKEL 79
Cdd:TIGR00218   3 FIFPVFKERDWGG-TALADLFGYSIPSQQTGECWaGSAHPKGPStvlnGPYKGVSLIDLWEKH-RELLGRAD----GDRF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618  80 PFLLKVLAIAQPLSLQVHPSAEQAlhgyteelprhvdipqdqwnykdgrqkaevlyaltpvtamcGFLPIAKLSANLLRL 159
Cdd:TIGR00218  77 PFLFKVLDAAKPLSIQVHPDDKYA-----------------------------------------EIHEEGELGKTECWY 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 160 LPYQfplvfpflqepeeKDEARLLQrffttlytleqEQRKLLLTEFKENLEllqedsytvDGNWLTpggiarlclesypd 239
Cdd:TIGR00218 116 IIDC-------------DEAAEIIK-----------GHLKNSKEELWTMIE---------DGLFKL-------------- 148
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 240 dpgvfapfFLHVLHLKPGEAVYLEPRTLHAYVRGHGIELMSNSDNVLRGGLTNKKVDVPELLQTLAFKAYNAG-LCPQIR 318
Cdd:TIGR00218 149 --------LLNRIKLKPGDFFYVPSGTPHAYKGGLVLEVMQNSDNVYRAGDTDKYLDIEKLVEVLTFPHVPEFhLKGQPQ 220
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1088501618 319 DTNNRLNILAPTDDFLLGVYE-RGTYHVGNRFSIEFLLCSEGTAEVVKDNQTHKLAQGECLVVASSVDSYriTVKG 393
Cdd:TIGR00218 221 KNGAEIVFMVPTEYFSVYKWDiSGKAEFIQQQSALILSVLEGSGRIKSGGKTLPLKKGESFFIPAHLGPF--TIEG 294
PMI_typeI_cat pfam20511
Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain ...
3-149 1.01e-26

Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8) which contains a zinc-binding site. It is composed of beta-strands connected by long loops in a jelly roll conformation.


Pssm-ID: 466660 [Multi-domain]  Cd Length: 143  Bit Score: 104.19  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618   3 MVKITPKVQPYPWGD--------DSF---IPSLlgkkPDGKPQAELWFGTHPGGESALPDSePLGDFLRDHDKEFLGEEQ 71
Cdd:pfam20511   1 LFRLQCGVQNYAWGKigsnsalaKLFaysIPSI----DEDKPYAELWMGTHPKGPSKVLNG-QLRDVTLDELSAELGELF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618  72 VKRHGKELPFLLKVLAIAQPLSLQVHPSAEQA--LHGyteelprhvdipQDQWNYKDGRQKAEVLYALTPVTAMCGFLPI 149
Cdd:pfam20511  76 GKRFGGNLPFLFKVLSVEKPLSIQVHPDKELGeiLHA------------ADPKNYPDDNHKPELAIALTPFEGLCGFRPL 143
ManA COG1482
Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism];
1-402 2.69e-17

Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism];


Pssm-ID: 441091 [Multi-domain]  Cd Length: 324  Bit Score: 82.14  E-value: 2.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618   1 MNMVKITPKVQPYPWGDDSfIPSLLGKKPDGKPQAELW-FGTHPGGESALPDSE----PLGDFLRDHDKEFLGEEQVKRH 75
Cdd:COG1482     2 MYPLRFKPIFKEKIWGGRR-LKEVFGKDLPEGKIGESWeISAHPNGVSVVANGPlagkTLDELVEEHPEELLGEKVYARF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618  76 GKELPFLLKVLAIAQPLSLQVHPSAEQALHGYTEELPrhvdipqdqwnykdgrqKAEVLYALtpvtamcgflpiaklsan 155
Cdd:COG1482    81 GDEFPLLIKFLDAKDDLSVQVHPDDEYAKEHEGGSYG-----------------KTEMWYIL------------------ 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 156 llrllpyqfplvfpflqepEEKDEARLlqrffttLYTLEQEQRKlllTEFKENLEllqedsytvDGNWltpggiarlclE 235
Cdd:COG1482   126 -------------------DAEPGAEI-------YLGFKEGVTK---EEFREALE---------NGDI-----------E 156
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 236 SYpddpgvfapffLHVLHLKPGEAVYLEPRTLHAYvrGHGI---ELMSNSDNV------LRGGLTNKK--VDVPELLQTL 304
Cdd:COG1482   157 DL-----------LNRVPVKKGDFFLIPAGTVHAI--GAGIlvlEIQQTSDITyrvydyDRLDLDGKPreLHIEKALDVI 223
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 305 AFKAYNAGLCP--QIRDTNNRLNILAPTDDF---LLGVYERGTYHVGNRFSIefLLCSEGTAEVVKDNQTHKLAQGECLV 379
Cdd:COG1482   224 DFERKPDEVVQptVVEEEGNREERLVECPYFtveRLELDGEVTLDTEDSFHI--LSVVEGEGTIESDGEPYELKKGETFL 301
                         410       420
                  ....*....|....*....|...
gi 1088501618 380 VASSVDSYRITVKGKVFSASVPG 402
Cdd:COG1482   302 LPAAVGEYTIRGEAKLLKSYVPD 324
 
Name Accession Description Interval E-value
cupin_PMI_type_I_N cd07011
type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This ...
6-306 3.16e-91

type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This subfamily contains type I phosphomannose isomerase (PMI; E.C. 5.3.1.8; also known as mannose-6-phosphate isomerase) found in eukaryotes and some bacteria such as Salmonella enterica. PMI catalyzes the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P), the first committed step in the synthesis of mannosylated glycoproteins. The active site, located within the N-terminal jelly roll-like beta-barrel cupin fold, contains a single essential zinc atom and forms a deep, open cavity large enough to contain M6P or F6P. PMI type I also has a C-terminal beta-barrel fold which has diverged considerably from the N-terminal domain and is not included here. This subfamily contains an alpha helical domain that is found in eukaryotic and some prokaryotic PMIs but is not present in their archaeal counterparts. F6P is a substrate for glycolysis and gluconeogenesis, while M6P is a substrate for production of activated mannose donor guanosine 5'-diphosphate D-mannose, an important precursor of mannosylated biomolecules such as glycoproteins, bacterial exopolysaccharides and fungal cell wall components. PMI is also essential for survival, virulence and possibly pathogenicity of some bacteria and protozoan parasites, as well as for cell wall integrity of certain yeasts. Thus, PMI is a potential target against fungal infections causing serious illness or death.


Pssm-ID: 380414 [Multi-domain]  Cd Length: 247  Bit Score: 274.81  E-value: 3.16e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618   6 ITPKVQPYPWGDDSFIPSL---LGKKPDGKPQAELWFGTHpggesalpdseplgdflrdhdkeflgeeqvkrhgkeLPFL 82
Cdd:cd07011     1 LKNAVQNYAWGSKGAISLLargGGKIPEGKPYAELWMGTH------------------------------------LPFL 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618  83 LKVLAIAQPLSLQVHPSAEQALHGYTEElPRhvdipqdqwNYKDGRQKAEVLYALTPVTAMCGFLPIAKLSANLLRLLPy 162
Cdd:cd07011    45 FKVLSAAKPLSIQAHPDKEQAEKLFARE-PE---------NYKDPNHKPEMAIALTPFEALCGFRPLEEILALLERVPP- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 163 qfpLVFPFLQEPEEKDEARLLQRFFTTLYTLE--QEQRKLLLTEFKENLELLQEDSytvDGNWltpggIARLClESYPDD 240
Cdd:cd07011   114 ---ELRELLGQEDAEQSKEGLKALFSALLTLDsdEEALAALVARLRARPKSEELDE---AEEL-----VLRLA-EQYPGD 181
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1088501618 241 PGVFAPFFLHVLHLKPGEAVYLEPRTLHAYVRGHGIELMSNSDNVLRGGLTNKKVDVPELLQTLAF 306
Cdd:cd07011   182 PGVFAALLLNLVTLKPGEAIFLPAGEPHAYLSGDGVECMANSDNVVRAGLTPKHVDVDELLRMLDY 247
PRK15131 PRK15131
mannose-6-phosphate isomerase; Provisional
3-400 1.50e-83

mannose-6-phosphate isomerase; Provisional


Pssm-ID: 185085 [Multi-domain]  Cd Length: 389  Bit Score: 260.29  E-value: 1.50e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618   3 MVKITPKVQPYPWGDDSFIPSLLG-KKPDGKPQAELWFGTHPGGESALPDSEPLGDFLRDH---DKE-FLGEEQVKRHGk 77
Cdd:PRK15131    1 MQKMINSVQNYAWGSKTALTELYGiANPDNQPMAELWMGAHPKSSSRVQDANGDIVSLRDViesDKSaLLGEAVAKRFG- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618  78 ELPFLLKVLAIAQPLSLQVHPSAEQALHGYTEElpRHVDIPQD--QWNYKDGRQKAEVLYALTPVTAMCGFLPIAKLsAN 155
Cdd:PRK15131   80 ELPFLFKVLCAAQPLSIQVHPNKRAAEIGFAKE--NAAGIPLDaaERNYKDPNHKPELVFALTPFLAMNAFREFSEI-VS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 156 LLRLLPYQFPLVFPFLQEPEEKDEARLlqrfFTTLYTLEQEQRKLLLTEFKENLELLQEDSytvdgnWLTPGGIArlclE 235
Cdd:PRK15131  157 LLQPVAGAHPAIAHFLQQPDAERLSEL----FASLLNMQGEEKSRALAVLKSALNSQQGEP------WQTIRLIS----E 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 236 SYPDDPGVFAPFFLHVLHLKPGEAVYLEPRTLHAYVRGHGIELMSNSDNVLRGGLTNKKVDVPELLQTLAFKAYNAG-LC 314
Cdd:PRK15131  223 FYPDDSGLFSPLLLNVVKLNPGEAMFLFAETPHAYLQGVALEVMANSDNVLRAGLTPKYIDIPELVANVKFEAKPANqLL 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 315 PQIRDTNNRLNILAPTDDFLLGVYE-RGTYHVGNRFSIEFLLCSEGTAEVVKDNQTHKLAQGE-CLVVASsvDSyRITVK 392
Cdd:PRK15131  303 TQPVKQGAELDFPIPVDDFAFSLHDlSDQPTTLSQQSAAILFCVEGEAVLWKGEQQLTLKPGEsAFIAAN--ES-PVTVS 379

                  ....*...
gi 1088501618 393 GKVFSASV 400
Cdd:PRK15131  380 GHGRLARV 387
PLN02288 PLN02288
mannose-6-phosphate isomerase
3-307 2.41e-57

mannose-6-phosphate isomerase


Pssm-ID: 215162 [Multi-domain]  Cd Length: 394  Bit Score: 192.58  E-value: 2.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618   3 MVKITPKVQPYPWG---DDSFIPSL----LGKKPD-GKPQAELWFGTHPGGESAL----PDSEPLGDFLRDHdKEFLGEE 70
Cdd:PLN02288    1 MLRLRCAVQNYDWGrigSESEVARLaaanSGSDVDpDKPYAELWMGTHPSGPSFVvatgKGSVLLKEWIAEN-PAALGDR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618  71 QVKRHGKELPFLLKVLAIAQPLSLQVHPSAE--QALHgytEELPRhvdipqdqwNYKDGRQKAEVLYALTPVTAMCGFLP 148
Cdd:PLN02288   80 VVERWGGDLPFLFKVLSVAKALSIQAHPDKKlaEKLH---AEQPN---------VYKDDNHKPEMALALTEFEALCGFVT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 149 IAKLSANLlRLLPYQFPLVFP-----FLQEPEEKDEARL---LQRFFTTLYTLEQEQRKLLLTEFKENLELLQEDSYTVD 220
Cdd:PLN02288  148 IQELKAVL-RTVPELRELVGSeaadqLLALPEHDGEEDVksvLRSAFTALMTASKDVVTEAVSKLKARLHAESQARELTD 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 221 GNWLtpggIARLClESYPDDPGVFAPFFLHVLHLKPGEAVYLEPRTLHAYVRGHGIELMSNSDNVLRGGLTNKKVDVPEL 300
Cdd:PLN02288  227 KEEL----VLRLE-KQYPGDVGVLSAFFLNYVKLNPGEALYLGANEPHAYLSGECIECMATSDNVVRAGLTPKFRDVQTL 301

                  ....*..
gi 1088501618 301 LQTLAFK 307
Cdd:PLN02288  302 CSMLTYK 308
manA TIGR00218
mannose-6-phosphate isomerase, class I; The names phosphomannose isomerase and ...
5-393 6.35e-37

mannose-6-phosphate isomerase, class I; The names phosphomannose isomerase and mannose-6-phosphate isomerase are synonomous. This family contains two rather deeply branched groups. One group contains an experimentally determined phosphomannose isomerase of Streptococcus mutans as well as three uncharacterized paralogous proteins of Bacillus subtilis, all at more than 50 % identity to each other, plus a more distant homolog from Archaeoglobus fulgidus. The other group contains members from E. coli, budding yeast, Borrelia burgdorferi, etc. [Energy metabolism, Sugars]


Pssm-ID: 272966 [Multi-domain]  Cd Length: 302  Bit Score: 136.02  E-value: 6.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618   5 KITPKVQPYPWGDdSFIPSLLGKKPDGKPQAELW-FGTHPGGES----ALPDSEPLGDFLRDHdKEFLGEEQvkrhGKEL 79
Cdd:TIGR00218   3 FIFPVFKERDWGG-TALADLFGYSIPSQQTGECWaGSAHPKGPStvlnGPYKGVSLIDLWEKH-RELLGRAD----GDRF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618  80 PFLLKVLAIAQPLSLQVHPSAEQAlhgyteelprhvdipqdqwnykdgrqkaevlyaltpvtamcGFLPIAKLSANLLRL 159
Cdd:TIGR00218  77 PFLFKVLDAAKPLSIQVHPDDKYA-----------------------------------------EIHEEGELGKTECWY 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 160 LPYQfplvfpflqepeeKDEARLLQrffttlytleqEQRKLLLTEFKENLEllqedsytvDGNWLTpggiarlclesypd 239
Cdd:TIGR00218 116 IIDC-------------DEAAEIIK-----------GHLKNSKEELWTMIE---------DGLFKL-------------- 148
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 240 dpgvfapfFLHVLHLKPGEAVYLEPRTLHAYVRGHGIELMSNSDNVLRGGLTNKKVDVPELLQTLAFKAYNAG-LCPQIR 318
Cdd:TIGR00218 149 --------LLNRIKLKPGDFFYVPSGTPHAYKGGLVLEVMQNSDNVYRAGDTDKYLDIEKLVEVLTFPHVPEFhLKGQPQ 220
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1088501618 319 DTNNRLNILAPTDDFLLGVYE-RGTYHVGNRFSIEFLLCSEGTAEVVKDNQTHKLAQGECLVVASSVDSYriTVKG 393
Cdd:TIGR00218 221 KNGAEIVFMVPTEYFSVYKWDiSGKAEFIQQQSALILSVLEGSGRIKSGGKTLPLKKGESFFIPAHLGPF--TIEG 294
PMI_typeI_cat pfam20511
Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain ...
3-149 1.01e-26

Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8) which contains a zinc-binding site. It is composed of beta-strands connected by long loops in a jelly roll conformation.


Pssm-ID: 466660 [Multi-domain]  Cd Length: 143  Bit Score: 104.19  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618   3 MVKITPKVQPYPWGD--------DSF---IPSLlgkkPDGKPQAELWFGTHPGGESALPDSePLGDFLRDHDKEFLGEEQ 71
Cdd:pfam20511   1 LFRLQCGVQNYAWGKigsnsalaKLFaysIPSI----DEDKPYAELWMGTHPKGPSKVLNG-QLRDVTLDELSAELGELF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618  72 VKRHGKELPFLLKVLAIAQPLSLQVHPSAEQA--LHGyteelprhvdipQDQWNYKDGRQKAEVLYALTPVTAMCGFLPI 149
Cdd:pfam20511  76 GKRFGGNLPFLFKVLSVEKPLSIQVHPDKELGeiLHA------------ADPKNYPDDNHKPELAIALTPFEGLCGFRPL 143
ManA COG1482
Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism];
1-402 2.69e-17

Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism];


Pssm-ID: 441091 [Multi-domain]  Cd Length: 324  Bit Score: 82.14  E-value: 2.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618   1 MNMVKITPKVQPYPWGDDSfIPSLLGKKPDGKPQAELW-FGTHPGGESALPDSE----PLGDFLRDHDKEFLGEEQVKRH 75
Cdd:COG1482     2 MYPLRFKPIFKEKIWGGRR-LKEVFGKDLPEGKIGESWeISAHPNGVSVVANGPlagkTLDELVEEHPEELLGEKVYARF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618  76 GKELPFLLKVLAIAQPLSLQVHPSAEQALHGYTEELPrhvdipqdqwnykdgrqKAEVLYALtpvtamcgflpiaklsan 155
Cdd:COG1482    81 GDEFPLLIKFLDAKDDLSVQVHPDDEYAKEHEGGSYG-----------------KTEMWYIL------------------ 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 156 llrllpyqfplvfpflqepEEKDEARLlqrffttLYTLEQEQRKlllTEFKENLEllqedsytvDGNWltpggiarlclE 235
Cdd:COG1482   126 -------------------DAEPGAEI-------YLGFKEGVTK---EEFREALE---------NGDI-----------E 156
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 236 SYpddpgvfapffLHVLHLKPGEAVYLEPRTLHAYvrGHGI---ELMSNSDNV------LRGGLTNKK--VDVPELLQTL 304
Cdd:COG1482   157 DL-----------LNRVPVKKGDFFLIPAGTVHAI--GAGIlvlEIQQTSDITyrvydyDRLDLDGKPreLHIEKALDVI 223
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 305 AFKAYNAGLCP--QIRDTNNRLNILAPTDDF---LLGVYERGTYHVGNRFSIefLLCSEGTAEVVKDNQTHKLAQGECLV 379
Cdd:COG1482   224 DFERKPDEVVQptVVEEEGNREERLVECPYFtveRLELDGEVTLDTEDSFHI--LSVVEGEGTIESDGEPYELKKGETFL 301
                         410       420
                  ....*....|....*....|...
gi 1088501618 380 VASSVDSYRITVKGKVFSASVPG 402
Cdd:COG1482   302 LPAAVGEYTIRGEAKLLKSYVPD 324
cupin_PMI_type_I_N_bac cd07010
Phosphomannose isomerase in bacteria and archaea, N-terminal cupin domain; This subfamily ...
8-103 4.59e-04

Phosphomannose isomerase in bacteria and archaea, N-terminal cupin domain; This subfamily contains type I phosphomannose isomerase (PMI; E.C. 5.3.1.8; also known as mannose-6-phosphate isomerase) found in many bacteria (e.g. Bacillus subtilis) and archaea. PMI catalyzes the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P), the first committed step in the synthesis of mannosylated glycoproteins. The active site, located within the N-terminal jelly roll-like beta-barrel cupin fold, contains a single essential zinc atom and forms a deep, open cavity large enough to contain M6P or F6P. PMI type I also has a C-terminal beta-barrel fold which has diverged considerably from the N-terminal domain and is not included here. This subfamily does not contain an alpha helical domain that exists in eukaryotic and some prokaryotic PMIs. F6P is a substrate for glycolysis and gluconeogenesis, while M6P is a substrate for production of activated mannose donor guanosine 5'-diphosphate D-mannose, an important precursor of mannosylated biomolecules such as glycoproteins, bacterial exopolysaccharides and fungal cell wall components. PMI is also essential for survival, virulence and possibly pathogenicity of some bacteria and protozoan parasites, as well as for cell wall integrity of certain yeasts. Thus, PMI is a potential target against fungal infections causing serious illness or death.


Pssm-ID: 380413  Cd Length: 173  Bit Score: 40.59  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618   8 PKVQPYPWGDDSfIPSLLGKKPDGKPQAELWFGThpggesalpdseplgdflrdhdkeflgeeqvkrhgkelPFLLKVLA 87
Cdd:cd07010     1 PILKERVWGGRR-LKELFGKPPPDEPIGESWEVS--------------------------------------PLLVKLLD 41
                          90
                  ....*....|....*.
gi 1088501618  88 IAQPLSLQVHPSAEQA 103
Cdd:cd07010    42 AAERLSVQVHPDDEYA 57
PMI_typeI_hel pfam20512
Phosphomannose isomerase type I, helical insertion domain; This entry represents the ...
170-249 5.05e-04

Phosphomannose isomerase type I, helical insertion domain; This entry represents the alpha-helical insertion domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8), in which the helices are packed closely, connected by short turns and loops. This domain packs closely against the catalytic domain, interrupting it.


Pssm-ID: 466661 [Multi-domain]  Cd Length: 88  Bit Score: 38.60  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088501618 170 FLQEPEekDEARLLQRFFTTLYTLEQEQRKLLLTEFKENLELLQEDSYTVDgnwlTPGGIARLCLESYPDDPGVFAPFFL 249
Cdd:pfam20512  15 SLQEPD--AEQKLLQKLFSSLMNSQKEKIKIQLAKLVERIQSQPSEFNKTD----ALPELIQRLNEQYPGDIGLFAPLFL 88
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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