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Conserved domains on  [gi|515648679|ref|WP_017081279|]
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mannose-6-phosphate isomerase, class I [Vibrio splendidus]

Protein Classification

cupin domain-containing protein( domain architecture ID 1562428)

cupin domain-containing protein, part of a functionally diverse superfamily with the active site generally located at the center of a conserved domain forming a beta-barrel fold

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
19-404 7.00e-164

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


The actual alignment was detected with superfamily member PRK15131:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 389  Bit Score: 465.21  E-value: 7.00e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  19 MTNVIQNYAWGSPSSFSQLFGIDNQSGEPQAEIWMGAHPNGCSMVTD-NGQQTTLSNLISKNLNLFLSEKIASRFGELPY 97
Cdd:PRK15131   4 MINSVQNYAWGSKTALTELYGIANPDNQPMAELWMGAHPKSSSRVQDaNGDIVSLRDVIESDKSALLGEAVAKRFGELPF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  98 LFKVLAAEKALSVQVHPNKQQAESGYALEEQQGIPMTAGNRNYKDANHKPELVYALTDYTAMNGFRSISEILEHFHYLDI 177
Cdd:PRK15131  84 LFKVLCAAQPLSIQVHPNKRAAEIGFAKENAAGIPLDAAERNYKDPNHKPELVFALTPFLAMNAFREFSEIVSLLQPVAG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 178 --PELHSMVndlqgdQTPNG--LASFFASLLSLQGEQKGMALTMLlmKAKL---SDTPvFQLISELEEQYPDDVGLFAPL 250
Cdd:PRK15131 164 ahPAIAHFL------QQPDAerLSELFASLLNMQGEEKSRALAVL--KSALnsqQGEP-WQTIRLISEFYPDDSGLFSPL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 251 LLNVITLKPGQAMYLDAETPHAYIKGTGLEVMANSDNVLRAGLTPKYMDINELVSCTQFNEKPADRLLLSPIEQGDVMEY 330
Cdd:PRK15131 235 LLNVVKLNPGEAMFLFAETPHAYLQGVALEVMANSDNVLRAGLTPKYIDIPELVANVKFEAKPANQLLTQPVKQGAELDF 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515648679 331 QIPVEDFKFSIVQNSHQRQ-ITTEGAEILLPLDESMVLTHQcGETCVIEKGQSVFIPAYAESYKLDCVGRVARAY 404
Cdd:PRK15131 315 PIPVDDFAFSLHDLSDQPTtLSQQSAAILFCVEGEAVLWKG-EQQLTLKPGESAFIAANESPVTVSGHGRLARVY 388
 
Name Accession Description Interval E-value
PRK15131 PRK15131
mannose-6-phosphate isomerase; Provisional
19-404 7.00e-164

mannose-6-phosphate isomerase; Provisional


Pssm-ID: 185085 [Multi-domain]  Cd Length: 389  Bit Score: 465.21  E-value: 7.00e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  19 MTNVIQNYAWGSPSSFSQLFGIDNQSGEPQAEIWMGAHPNGCSMVTD-NGQQTTLSNLISKNLNLFLSEKIASRFGELPY 97
Cdd:PRK15131   4 MINSVQNYAWGSKTALTELYGIANPDNQPMAELWMGAHPKSSSRVQDaNGDIVSLRDVIESDKSALLGEAVAKRFGELPF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  98 LFKVLAAEKALSVQVHPNKQQAESGYALEEQQGIPMTAGNRNYKDANHKPELVYALTDYTAMNGFRSISEILEHFHYLDI 177
Cdd:PRK15131  84 LFKVLCAAQPLSIQVHPNKRAAEIGFAKENAAGIPLDAAERNYKDPNHKPELVFALTPFLAMNAFREFSEIVSLLQPVAG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 178 --PELHSMVndlqgdQTPNG--LASFFASLLSLQGEQKGMALTMLlmKAKL---SDTPvFQLISELEEQYPDDVGLFAPL 250
Cdd:PRK15131 164 ahPAIAHFL------QQPDAerLSELFASLLNMQGEEKSRALAVL--KSALnsqQGEP-WQTIRLISEFYPDDSGLFSPL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 251 LLNVITLKPGQAMYLDAETPHAYIKGTGLEVMANSDNVLRAGLTPKYMDINELVSCTQFNEKPADRLLLSPIEQGDVMEY 330
Cdd:PRK15131 235 LLNVVKLNPGEAMFLFAETPHAYLQGVALEVMANSDNVLRAGLTPKYIDIPELVANVKFEAKPANQLLTQPVKQGAELDF 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515648679 331 QIPVEDFKFSIVQNSHQRQ-ITTEGAEILLPLDESMVLTHQcGETCVIEKGQSVFIPAYAESYKLDCVGRVARAY 404
Cdd:PRK15131 315 PIPVDDFAFSLHDLSDQPTtLSQQSAAILFCVEGEAVLWKG-EQQLTLKPGESAFIAANESPVTVSGHGRLARVY 388
cupin_PMI_type_I_N cd07011
type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This ...
19-309 3.08e-111

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: 326.04  E-value: 3.08e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  19 MTNVIQNYAWGSPSSFSQLF--GIDNQSGEPQAEIWMGAHpngcsmvtdngqqttlsnlisknlnlflsekiasrfgeLP 96
Cdd:cd07011    1 LKNAVQNYAWGSKGAISLLArgGGKIPEGKPYAELWMGTH--------------------------------------LP 42
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  97 YLFKVLAAEKALSVQVHPNKQQAESGYALEeqqgipmtagNRNYKDANHKPELVYALTDYTAMNGFRSISEILEHFHYLD 176
Cdd:cd07011   43 FLFKVLSAAKPLSIQAHPDKEQAEKLFARE----------PENYKDPNHKPEMAIALTPFEALCGFRPLEEILALLERVP 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 177 iPELHSMVNDLQGDQTPNGLASFFASLLSLQGEQKgmALTMLL-----MKAKLSDTPVFQLISELEEQYPDDVGLFAPLL 251
Cdd:cd07011  113 -PELRELLGQEDAEQSKEGLKALFSALLTLDSDEE--ALAALVarlraRPKSEELDEAEELVLRLAEQYPGDPGVFAALL 189
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515648679 252 LNVITLKPGQAMYLDAETPHAYIKGTGLEVMANSDNVLRAGLTPKYMDINELVSCTQF 309
Cdd:cd07011  190 LNLVTLKPGEAIFLPAGEPHAYLSGDGVECMANSDNVVRAGLTPKHVDVDELLRMLDY 247
manA TIGR00218
mannose-6-phosphate isomerase, class I; The names phosphomannose isomerase and ...
13-395 2.42e-51

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: 174.16  E-value: 2.42e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679   13 QRFFYPMTNviqNYAWGSpSSFSQLFGiDNQSGEPQAEIWMG-AHPNGCSMVTDN-GQQTTLSNLISKNLNLFlSEKIAS 90
Cdd:TIGR00218   1 PLFIFPVFK---ERDWGG-TALADLFG-YSIPSQQTGECWAGsAHPKGPSTVLNGpYKGVSLIDLWEKHRELL-GRADGD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679   91 RFgelPYLFKVLAAEKALSVQVHPNKqqaesgyaleeqqgipmtagnrnykdanhkpelvyaltdytamngfrsiseile 170
Cdd:TIGR00218  75 RF---PFLFKVLDAAKPLSIQVHPDD------------------------------------------------------ 97
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  171 hfhylDIPELHsmvndlqgdqtPNG-LASFFASLLSLQGEqkgmALTMLLMKAKlsdtpvfqlISELEEQYPDDVGLFAp 249
Cdd:TIGR00218  98 -----KYAEIH-----------EEGeLGKTECWYIIDCDE----AAEIIKGHLK---------NSKEELWTMIEDGLFK- 147
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  250 LLLNVITLKPGQAMYLDAETPHAYIKGTGLEVMANSDNVLRAGLTPKYMDINELVSCTQFNEKPADRLLLSPIEQGDVME 329
Cdd:TIGR00218 148 LLLNRIKLKPGDFFYVPSGTPHAYKGGLVLEVMQNSDNVYRAGDTDKYLDIEKLVEVLTFPHVPEFHLKGQPQKNGAEIV 227
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515648679  330 YQIPVEDFKFSIVQ-NSHQRQITTEGAEILLPLDESMVLTHQcGETCVIEKGQSVFIPAYAESYKLD 395
Cdd:TIGR00218 228 FMVPTEYFSVYKWDiSGKAEFIQQQSALILSVLEGSGRIKSG-GKTLPLKKGESFFIPAHLGPFTIE 293
PMI_typeI_cat pfam20511
Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain ...
17-163 2.21e-43

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: 148.10  E-value: 2.21e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679   17 YPMTNVIQNYAWG---SPSSFSQLFGIDNQS---GEPQAEIWMGAHPNGCSMVTDNgqqtTLSNLISKNLNLFLSEKIAS 90
Cdd:pfam20511   2 FRLQCGVQNYAWGkigSNSALAKLFAYSIPSideDKPYAELWMGTHPKGPSKVLNG----QLRDVTLDELSAELGELFGK 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515648679   91 RFG-ELPYLFKVLAAEKALSVQVHPNKQQAEsgyaleeqqgIPMTAGNRNYKDANHKPELVYALTDYTAMNGFR 163
Cdd:pfam20511  78 RFGgNLPFLFKVLSVEKPLSIQVHPDKELGE----------ILHAADPKNYPDDNHKPELAIALTPFEGLCGFR 141
ManA COG1482
Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism];
17-394 4.17e-15

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


Pssm-ID: 441091 [Multi-domain]  Cd Length: 324  Bit Score: 75.59  E-value: 4.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  17 YP--MTNVIQNYAWGSpSSFSQLFGIDNQSGEPqAEIWMG-AHPNGCSMVTdNGQQ--TTLSNLISKNLNLFLSEKIASR 91
Cdd:COG1482    3 YPlrFKPIFKEKIWGG-RRLKEVFGKDLPEGKI-GESWEIsAHPNGVSVVA-NGPLagKTLDELVEEHPEELLGEKVYAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  92 FG-ELPYLFKVLAAEKALSVQVHPNKQqaesgYALEeqqgipmtagnrNYKDANHKPELVYaltdytamngfrsiseILe 170
Cdd:COG1482   80 FGdEFPLLIKFLDAKDDLSVQVHPDDE-----YAKE------------HEGGSYGKTEMWY----------------IL- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 171 hfhyldipelhsmvndlqgDQTPNglasffASLLSlqGEQKGMaltmllmkaklsdTPVfQLISELEEQYPDDvglfapl 250
Cdd:COG1482  126 -------------------DAEPG------AEIYL--GFKEGV-------------TKE-EFREALENGDIED------- 157
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 251 LLNVITLKPGQAMYLDAETPHAYikGTG---LEVMANSDNV------LRAGLTPKY--MDINELVSCTQFNEKPADRLLL 319
Cdd:COG1482  158 LLNRVPVKKGDFFLIPAGTVHAI--GAGilvLEIQQTSDITyrvydyDRLDLDGKPreLHIEKALDVIDFERKPDEVVQP 235
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515648679 320 SPIEQGDVMEYQIPVEDFkFSIVQ---NSHQRQITTEGAEILLPLDESMVLTHQcGETCVIEKGQSVFIPAYAESYKL 394
Cdd:COG1482  236 TVVEEEGNREERLVECPY-FTVERlelDGEVTLDTEDSFHILSVVEGEGTIESD-GEPYELKKGETFLLPAAVGEYTI 311
 
Name Accession Description Interval E-value
PRK15131 PRK15131
mannose-6-phosphate isomerase; Provisional
19-404 7.00e-164

mannose-6-phosphate isomerase; Provisional


Pssm-ID: 185085 [Multi-domain]  Cd Length: 389  Bit Score: 465.21  E-value: 7.00e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  19 MTNVIQNYAWGSPSSFSQLFGIDNQSGEPQAEIWMGAHPNGCSMVTD-NGQQTTLSNLISKNLNLFLSEKIASRFGELPY 97
Cdd:PRK15131   4 MINSVQNYAWGSKTALTELYGIANPDNQPMAELWMGAHPKSSSRVQDaNGDIVSLRDVIESDKSALLGEAVAKRFGELPF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  98 LFKVLAAEKALSVQVHPNKQQAESGYALEEQQGIPMTAGNRNYKDANHKPELVYALTDYTAMNGFRSISEILEHFHYLDI 177
Cdd:PRK15131  84 LFKVLCAAQPLSIQVHPNKRAAEIGFAKENAAGIPLDAAERNYKDPNHKPELVFALTPFLAMNAFREFSEIVSLLQPVAG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 178 --PELHSMVndlqgdQTPNG--LASFFASLLSLQGEQKGMALTMLlmKAKL---SDTPvFQLISELEEQYPDDVGLFAPL 250
Cdd:PRK15131 164 ahPAIAHFL------QQPDAerLSELFASLLNMQGEEKSRALAVL--KSALnsqQGEP-WQTIRLISEFYPDDSGLFSPL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 251 LLNVITLKPGQAMYLDAETPHAYIKGTGLEVMANSDNVLRAGLTPKYMDINELVSCTQFNEKPADRLLLSPIEQGDVMEY 330
Cdd:PRK15131 235 LLNVVKLNPGEAMFLFAETPHAYLQGVALEVMANSDNVLRAGLTPKYIDIPELVANVKFEAKPANQLLTQPVKQGAELDF 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515648679 331 QIPVEDFKFSIVQNSHQRQ-ITTEGAEILLPLDESMVLTHQcGETCVIEKGQSVFIPAYAESYKLDCVGRVARAY 404
Cdd:PRK15131 315 PIPVDDFAFSLHDLSDQPTtLSQQSAAILFCVEGEAVLWKG-EQQLTLKPGESAFIAANESPVTVSGHGRLARVY 388
cupin_PMI_type_I_N cd07011
type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This ...
19-309 3.08e-111

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: 326.04  E-value: 3.08e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  19 MTNVIQNYAWGSPSSFSQLF--GIDNQSGEPQAEIWMGAHpngcsmvtdngqqttlsnlisknlnlflsekiasrfgeLP 96
Cdd:cd07011    1 LKNAVQNYAWGSKGAISLLArgGGKIPEGKPYAELWMGTH--------------------------------------LP 42
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  97 YLFKVLAAEKALSVQVHPNKQQAESGYALEeqqgipmtagNRNYKDANHKPELVYALTDYTAMNGFRSISEILEHFHYLD 176
Cdd:cd07011   43 FLFKVLSAAKPLSIQAHPDKEQAEKLFARE----------PENYKDPNHKPEMAIALTPFEALCGFRPLEEILALLERVP 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 177 iPELHSMVNDLQGDQTPNGLASFFASLLSLQGEQKgmALTMLL-----MKAKLSDTPVFQLISELEEQYPDDVGLFAPLL 251
Cdd:cd07011  113 -PELRELLGQEDAEQSKEGLKALFSALLTLDSDEE--ALAALVarlraRPKSEELDEAEELVLRLAEQYPGDPGVFAALL 189
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515648679 252 LNVITLKPGQAMYLDAETPHAYIKGTGLEVMANSDNVLRAGLTPKYMDINELVSCTQF 309
Cdd:cd07011  190 LNLVTLKPGEAIFLPAGEPHAYLSGDGVECMANSDNVVRAGLTPKHVDVDELLRMLDY 247
PLN02288 PLN02288
mannose-6-phosphate isomerase
23-390 3.65e-82

mannose-6-phosphate isomerase


Pssm-ID: 215162 [Multi-domain]  Cd Length: 394  Bit Score: 256.91  E-value: 3.65e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  23 IQNYAWG---SPSSFSQLF----GIDNQSGEPQAEIWMGAHPNGCSMVT-DNGQQTTLSNLISKNLNLfLSEKIASRFG- 93
Cdd:PLN02288   8 VQNYDWGrigSESEVARLAaansGSDVDPDKPYAELWMGTHPSGPSFVVaTGKGSVLLKEWIAENPAA-LGDRVVERWGg 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  94 ELPYLFKVLAAEKALSVQVHPNKQQAEsgyALEEQQgiPmtagnRNYKDANHKPELVYALTDYTAMNGFRSISEILEHFH 173
Cdd:PLN02288  87 DLPFLFKVLSVAKALSIQAHPDKKLAE---KLHAEQ--P-----NVYKDDNHKPEMALALTEFEALCGFVTIQELKAVLR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 174 ylDIPELHSMVNDLQGDQ------------TPNGLASFFASLLSLQGEQKGMALTMllMKAKLSD-------TPVFQLIS 234
Cdd:PLN02288 157 --TVPELRELVGSEAADQllalpehdgeedVKSVLRSAFTALMTASKDVVTEAVSK--LKARLHAesqarelTDKEELVL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 235 ELEEQYPDDVGLFAPLLLNVITLKPGQAMYLDAETPHAYIKGTGLEVMANSDNVLRAGLTPKYMDINELVSCTQFNEKPA 314
Cdd:PLN02288 233 RLEKQYPGDVGVLSAFFLNYVKLNPGEALYLGANEPHAYLSGECIECMATSDNVVRAGLTPKFRDVQTLCSMLTYKQGFP 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 315 DRLLLSPIEQGdVMEYQIPVEDFkfsivqnshqrqittEGAEILLPLDESMVLTHQCG-------------------ETC 375
Cdd:PLN02288 313 EILTGVPVDPY-TTRYLPPFDEF---------------EVDHCDVPPGASVVFPAVPGpsvflviegegvlstgsseDGT 376
                        410
                 ....*....|....*
gi 515648679 376 VIEKGQSVFIPAYAE 390
Cdd:PLN02288 377 AAKRGDVFFVPAGTE 391
manA TIGR00218
mannose-6-phosphate isomerase, class I; The names phosphomannose isomerase and ...
13-395 2.42e-51

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: 174.16  E-value: 2.42e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679   13 QRFFYPMTNviqNYAWGSpSSFSQLFGiDNQSGEPQAEIWMG-AHPNGCSMVTDN-GQQTTLSNLISKNLNLFlSEKIAS 90
Cdd:TIGR00218   1 PLFIFPVFK---ERDWGG-TALADLFG-YSIPSQQTGECWAGsAHPKGPSTVLNGpYKGVSLIDLWEKHRELL-GRADGD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679   91 RFgelPYLFKVLAAEKALSVQVHPNKqqaesgyaleeqqgipmtagnrnykdanhkpelvyaltdytamngfrsiseile 170
Cdd:TIGR00218  75 RF---PFLFKVLDAAKPLSIQVHPDD------------------------------------------------------ 97
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  171 hfhylDIPELHsmvndlqgdqtPNG-LASFFASLLSLQGEqkgmALTMLLMKAKlsdtpvfqlISELEEQYPDDVGLFAp 249
Cdd:TIGR00218  98 -----KYAEIH-----------EEGeLGKTECWYIIDCDE----AAEIIKGHLK---------NSKEELWTMIEDGLFK- 147
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  250 LLLNVITLKPGQAMYLDAETPHAYIKGTGLEVMANSDNVLRAGLTPKYMDINELVSCTQFNEKPADRLLLSPIEQGDVME 329
Cdd:TIGR00218 148 LLLNRIKLKPGDFFYVPSGTPHAYKGGLVLEVMQNSDNVYRAGDTDKYLDIEKLVEVLTFPHVPEFHLKGQPQKNGAEIV 227
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515648679  330 YQIPVEDFKFSIVQ-NSHQRQITTEGAEILLPLDESMVLTHQcGETCVIEKGQSVFIPAYAESYKLD 395
Cdd:TIGR00218 228 FMVPTEYFSVYKWDiSGKAEFIQQQSALILSVLEGSGRIKSG-GKTLPLKKGESFFIPAHLGPFTIE 293
PMI_typeI_cat pfam20511
Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain ...
17-163 2.21e-43

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: 148.10  E-value: 2.21e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679   17 YPMTNVIQNYAWG---SPSSFSQLFGIDNQS---GEPQAEIWMGAHPNGCSMVTDNgqqtTLSNLISKNLNLFLSEKIAS 90
Cdd:pfam20511   2 FRLQCGVQNYAWGkigSNSALAKLFAYSIPSideDKPYAELWMGTHPKGPSKVLNG----QLRDVTLDELSAELGELFGK 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515648679   91 RFG-ELPYLFKVLAAEKALSVQVHPNKQQAEsgyaleeqqgIPMTAGNRNYKDANHKPELVYALTDYTAMNGFR 163
Cdd:pfam20511  78 RFGgNLPFLFKVLSVEKPLSIQVHPDKELGE----------ILHAADPKNYPDDNHKPELAIALTPFEGLCGFR 141
ManA COG1482
Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism];
17-394 4.17e-15

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


Pssm-ID: 441091 [Multi-domain]  Cd Length: 324  Bit Score: 75.59  E-value: 4.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  17 YP--MTNVIQNYAWGSpSSFSQLFGIDNQSGEPqAEIWMG-AHPNGCSMVTdNGQQ--TTLSNLISKNLNLFLSEKIASR 91
Cdd:COG1482    3 YPlrFKPIFKEKIWGG-RRLKEVFGKDLPEGKI-GESWEIsAHPNGVSVVA-NGPLagKTLDELVEEHPEELLGEKVYAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679  92 FG-ELPYLFKVLAAEKALSVQVHPNKQqaesgYALEeqqgipmtagnrNYKDANHKPELVYaltdytamngfrsiseILe 170
Cdd:COG1482   80 FGdEFPLLIKFLDAKDDLSVQVHPDDE-----YAKE------------HEGGSYGKTEMWY----------------IL- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 171 hfhyldipelhsmvndlqgDQTPNglasffASLLSlqGEQKGMaltmllmkaklsdTPVfQLISELEEQYPDDvglfapl 250
Cdd:COG1482  126 -------------------DAEPG------AEIYL--GFKEGV-------------TKE-EFREALENGDIED------- 157
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648679 251 LLNVITLKPGQAMYLDAETPHAYikGTG---LEVMANSDNV------LRAGLTPKY--MDINELVSCTQFNEKPADRLLL 319
Cdd:COG1482  158 LLNRVPVKKGDFFLIPAGTVHAI--GAGilvLEIQQTSDITyrvydyDRLDLDGKPreLHIEKALDVIDFERKPDEVVQP 235
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515648679 320 SPIEQGDVMEYQIPVEDFkFSIVQ---NSHQRQITTEGAEILLPLDESMVLTHQcGETCVIEKGQSVFIPAYAESYKL 394
Cdd:COG1482  236 TVVEEEGNREERLVECPY-FTVERlelDGEVTLDTEDSFHILSVVEGEGTIESD-GEPYELKKGETFLLPAAVGEYTI 311
PMI_typeI_hel pfam20512
Phosphomannose isomerase type I, helical insertion domain; This entry represents the ...
188-252 9.48e-07

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: 46.69  E-value: 9.48e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515648679  188 QGDQTPNGLASFFASLLSLQGEQKGMALTMLLMKAKLSDTPVFQ------LISELEEQYPDDVGLFAPLLL 252
Cdd:pfam20512  18 EPDAEQKLLQKLFSSLMNSQKEKIKIQLAKLVERIQSQPSEFNKtdalpeLIQRLNEQYPGDIGLFAPLFL 88
cupin_PMI_type_I_N_bac cd07010
Phosphomannose isomerase in bacteria and archaea, N-terminal cupin domain; This subfamily ...
96-130 7.48e-03

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: 37.12  E-value: 7.48e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 515648679  96 PYLFKVLAAEKALSVQVHPNKQQA-----------ESGYALEEQQG 130
Cdd:cd07010   34 PLLVKLLDAAERLSVQVHPDDEYArkhenepfgktEAWYILDAEPG 79
 
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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