|
Name |
Accession |
Description |
Interval |
E-value |
| pgm |
TIGR01132 |
phosphoglucomutase, alpha-D-glucose phosphate-specific; This enzyme interconverts ... |
2-547 |
0e+00 |
|
phosphoglucomutase, alpha-D-glucose phosphate-specific; This enzyme interconverts alpha-D-glucose-1-P and alpha-D-glucose-6-P. [Energy metabolism, Sugars]
Pssm-ID: 273459 Cd Length: 543 Bit Score: 985.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 2 VANPRAGQPAQPEDLVDLPHLVTAYYSIEPDPDDLAQQVAFGTSGHRGSALTGTFNELHILAITQAIVEYRAAQGTTGPL 81
Cdd:TIGR01132 1 AIHPRAGQPAQQEDLINVAQLVAQYYVLQPEAGNAAHAVKFGTSGHRGSALRGTFNEPHILAIAQAIAEYRAAQGITGPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 82 FIGRDTHGLSEPAWVSALEVLAANQVVAVVDSRDRYTPTPAISHAILTYNRgRTEALADGIVVTPSHNPPSDGGIKYNPP 161
Cdd:TIGR01132 81 YIGKDTHALSEPAFISVLEVLAANGVEVIVQENNGFTPTPAVSHAILTHNK-KGEPLADGIVITPSHNPPEDGGIKYNPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 162 NGGPADTAATTAIAKRANEILLAR-SMVKRLPLARALR--TAQRHDYLGHYVDDLPNVVDIAAIREAGVRIGADPLGGAS 238
Cdd:TIGR01132 160 NGGPADTEATQAIEDRANALLANGlKGVKRLPLAQALAsgTVKAHDLVQPYVDGLADIVDMAAIQKAGLRLGVDPLGGSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 239 VDYWGEIAHRHGLDLTVVNPLVDATWRFMTLDTDGKIRMDCSSPDAMAGLIRtmfgNRERYQIATGNDADADRHGIVTPd 318
Cdd:TIGR01132 240 IDYWKRIAEKYNLNLTLVNPQVDPTFRFMTLDKDGKIRMDCSSPYAMAGLLA----LRDKYDLAFGNDPDYDRHGIVTP- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 319 EGLLNPNHYLAVAIEYLYTHRPSWPAGIAVGKTVVSSSIIDRVVAGIGRQLVEVPVGFKWFVDGLIGATLGFGGEESAGA 398
Cdd:TIGR01132 315 AGLMNPNHYLAVAINYLFQHRPQWGGDVAVGKTLVSSAMIDRVVADLGRQLVEVPVGFKWFVDGLFDGSFGFGGEESAGA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 399 SFLRRDGSVWTTDKDGIIMALLAAEILAVTGATPSQRYHALAGEYGGPCYARIDAPADREQKARLARLSADQVSATELAG 478
Cdd:TIGR01132 395 SFLRFDGTPWSTDKDGIIMCLLAAEITAVTGKNPQQHYNELAAKFGAPSYNRIQAPATSAQKARLKKLSPEMVSATTLAG 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 623360049 479 EPITAKLTTAPGNGAALGGLKVTTANAWFAARPSGTEDVYKIYAESFRGPQHLVEVQQTAREVVDRVIG 547
Cdd:TIGR01132 475 DPITARLTAAPGNGAAIGGLKVTTDNGWFAARPSGTEDVYKIYCESFKGEEHLKQIEKEAVEIVSEVLK 543
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
20-542 |
0e+00 |
|
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100094 [Multi-domain] Cd Length: 522 Bit Score: 975.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 20 PHLVTAYYSIEPDPDDLAQQVAFGTSGHRGSALTGTFNELHILAITQAIVEYRAAQGTTGPLFIGRDTHGLSEPAWVSAL 99
Cdd:cd05801 1 PRLITAYYTLKPDPSNPAQRVAFGTSGHRGSSLKGSFNEAHILAISQAICDYRKSQGITGPLFLGKDTHALSEPAFISAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 100 EVLAANQVVAVVDSRDRYTPTPAISHAILTYNRGRTEALADGIVVTPSHNPPSDGGIKYNPPNGGPADTAATTAIAKRAN 179
Cdd:cd05801 81 EVLAANGVEVIIQQNDGYTPTPVISHAILTYNRGRTEGLADGIVITPSHNPPEDGGFKYNPPHGGPADTDITRWIEKRAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 180 EILLARSM-VKRLPLARALR--TAQRHDYLGHYVDDLPNVVDIAAIREAGVRIGADPLGGASVDYWGEIAHRHGLDLTVV 256
Cdd:cd05801 161 ALLANGLKgVKRIPLEAALAsgYTHRHDFVTPYVADLGNVIDMDAIRKSGLRLGVDPLGGASVPYWQPIAEKYGLNLTVV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 257 NPLVDATWRFMTLDTDGKIRMDCSSPDAMAGLIRTmfgnRERYQIATGNDADADRHGIVTPDEGLLNPNHYLAVAIEYLY 336
Cdd:cd05801 241 NPKVDPTFRFMTLDHDGKIRMDCSSPYAMAGLLKL----KDKFDLAFANDPDADRHGIVTPSAGLMNPNHYLSVAIDYLF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 337 THRPSWPAGIAVGKTVVSSSIIDRVVAGIGRQLVEVPVGFKWFVDGLIGATLGFGGEESAGASFLRRDGSVWTTDKDGII 416
Cdd:cd05801 317 THRPLWNKSAGVGKTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDGLLDGSLGFGGEESAGASFLRRDGTVWTTDKDGII 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 417 MALLAAEILAVTGATPSQRYHALAGEYGGPCYARIDAPADREQKARLARLSADQVSATELAGEPITAKLTTAPGNGAALG 496
Cdd:cd05801 397 MCLLAAEILAVTGKDPGQLYQELTERFGEPYYARIDAPATPEQKARLKKLSPEQVTATELAGDPILAKLTRAPGNGASIG 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 623360049 497 GLKVTTANAWFAARPSGTEDVYKIYAESFRGPQHLVEVQQTAREVV 542
Cdd:cd05801 477 GLKVTTANGWFAARPSGTEDVYKIYAESFLSEEHLKKIQKEAQEIV 522
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
3-547 |
0e+00 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 951.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 3 ANPRAGQPAQPEDLVDLPHLVTAYYSIEPDPDDLAQQVAFGTSGHRGSALTGTFNELHILAITQAIVEYRAAQGTTGPLF 82
Cdd:PRK07564 1 IHPRAGQPAQPSDLINVPRLVSAYYTLKPDPTNPFQDVKFGTSGHRGSSLQPSFNENHILAIFQAICEYRGKQGITGPLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 83 IGRDTHGLSEPAWVSALEVLAANQVVAVVDSRDRYTPTPAISHAILTYNrGRTEALADGIVVTPSHNPPSDGGIKYNPPN 162
Cdd:PRK07564 81 VGGDTHALSEPAIQSALEVLAANGVGVVIVGRGGYTPTPAVSHAILKYN-GRGGGLADGIVITPSHNPPEDGGIKYNPPN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 163 GGPADTAATTAIAKRANEILLAR-SMVKRLPLARALR--TAQRHDYLGHYVDDLPNVVDIAAIREAGVRIGADPLGGASV 239
Cdd:PRK07564 160 GGPADTDVTDAIEARANELLAYGlKGVKRIPLDRALAsmTVEVIDPVADYVEDLENVFDFDAIRKAGLRLGVDPLGGATG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 240 DYWGEIAHRHGLDLTVVNPLVDATWRFMTLDTDGKIRMDCSSPDAMAGLIrtmfGNRERYQIATGNDADADRHGIVTPDe 319
Cdd:PRK07564 240 PYWKAIAERYGLDLTVVNAPVDPTFNFMPLDDDGKIRMDCSSPYAMAGLL----ALKDAFDLAFANDPDGDRHGIVTPG- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 320 GLLNPNHYLAVAIEYLYTHRPSWPAGIAVGKTVVSSSIIDRVVAGIGRQLVEVPVGFKWFVDGLIGATLGFGGEESAGAS 399
Cdd:PRK07564 315 GLMNPNHYLAVAIAYLFHHRPGWRAGAGVGKTLVSSAMIDRVAAKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESAGAS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 400 FLRRDGSVWTTDKDGIIMALLAAEILAVTGATPSQRYHALAGEYGGPCYARIDAPADREQKARLARLSADQVSATELAGE 479
Cdd:PRK07564 395 FLRRDGSVWTTDKDGLIAVLLAAEILAVTGKSPSEIYRELWARFGRPYYSRHDAPATPEQKAALRKLSPELVGATELAGD 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 623360049 480 PITAKLTTAPGNGAALGGLKVTTANAWFAARPSGTEDVYKIYAESFRGPQHLVEVQQTAREVVDRVIG 547
Cdd:PRK07564 475 PIDASLTEAPGNGAAIGGLKVVTENGWFAARPSGTETTYKIYAESFEGDEHLHQIQKEAQEIVADLIA 542
|
|
| Pgm |
COG0033 |
Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism]; |
4-547 |
0e+00 |
|
Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 439803 Cd Length: 544 Bit Score: 936.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 4 NPRAGQPAQPEDLVDLPHLVTAYYSIEPDPDDLAQQVAFGTSGHRGSALTGTFNELHILAITQAIVEYRAAQGTTGPLFI 83
Cdd:COG0033 2 HPRAGQPAPPSDLIDVPRLVSAYYTIKPDPTTPFQDVKFGTSGHRGSSLKGSFNEPHILAITQAIFDYRKAQGITGPLFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 84 GRDTHGLSEPAWVSALEVLAANQVVAVVDSRDRYTPTPAISHAILTYNRGrTEALADGIVVTPSHNPPSDGGIKYNPPNG 163
Cdd:COG0033 82 GGDTHALSEPAIQTALEVLAANGVGVVIVGQGGYTPTPAVSHAILKYNRG-TSGAADGIVLTPSHNPPEDGGIKYNPPNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 164 GPADTAATTAIAKRANEILLAR-SMVKRLPLARALR--TAQRHDYLGHYVDDLPNVVDIAAIREAGVRIGADPLGGASVD 240
Cdd:COG0033 161 GPADEDVTDAIEARANEILEYGlADVKRVPLDRAGTamTVEVIDPVADYVELLESVFDFDAIRAAGFRIGFDPLGGATGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 241 YWGEIAHRHGLDLTVVNPLVDATWRFMTLDTDGKIRMDCSSPDAMAGLIrtmfGNRERYQIATGNDADADRHGIVTPDEG 320
Cdd:COG0033 241 YWKAIAERYGLDLTVVNGVPDPDFRFMTLDWDGGIRMDPSSPYAMASLI----AGKDAPDFAAANDGDGDRHGIVTPRGG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 321 LLNPNHYLAVAIEYLYTHRPSWPAGIAVGKTVVSSSIIDRVVAGIGRQLVEVPVGFKWFVDGLIGATLGFGGEESAGASF 400
Cdd:COG0033 317 LMNPNHYLAVAIAYLFTHRPGWAALAGVGKTMVTSSAIDRVAAALGRPLYEVPVGFKWFVNGLDAGSLGFGGEESAGASF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 401 LRRDGSVWTTDKDGIIMALLAAEILAVTGATPSQRYHALAGEYGGPCYARIDAPADREQKARLARLSADQVSATELAGEP 480
Cdd:COG0033 397 LRRDGSVWTTDKDGLWAVLLAAEILAVTGKSPAEIYRELWARFGRPYYSRHDAEATDEQKARLAKLSGEQVGATTLAGED 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 623360049 481 ITAKLTTAPGNGAALGGLKVTTANAWFAARPSGTEDVYKIYAESFRGPQHLVEVQQTAREVVDRVIG 547
Cdd:COG0033 477 IFAYLDPAPGNGAAIGGLKVVTENGWFAARPSGTETTYKIYAESFEGDEHLHQIDAEAADLVDAALA 543
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
40-542 |
6.92e-80 |
|
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model.
Pssm-ID: 100093 Cd Length: 461 Bit Score: 257.87 E-value: 6.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 40 VAFGTSGHRGS-ALTGTFNELHILAitQAIVEYRAAQGTTGP-LFIGRDTHGLSEPAWVSALEVLAANQVVAVVDsrDRY 117
Cdd:cd05800 1 IKFGTDGWRGIiAEDFTFENVRRVA--QAIADYLKEEGGGGRgVVVGYDTRFLSEEFARAVAEVLAANGIDVYLS--DRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 118 TPTPAISHAILTYNrgrteaLADGIVVTPSHNPPSDGGIKYNPPNGGPADTAATTAIakranEILLArSMVKRLPLARAL 197
Cdd:cd05800 77 VPTPAVSWAVKKLG------AAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAI-----EARLA-SGEPPGLEARAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 198 RTAQRHDYLGHYVDDLPNVVDIAAIREAGVRIGADPLGGASVDYWGEIAHRHGLDLTVVNplvdatwrfMTLDTDGKIRM 277
Cdd:cd05800 145 GLIETIDPKPDYLEALRSLVDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIR---------AERDPLFGGIP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 278 DCSSPDAMAGLIRTMfgNRERYQIATGNDADADRHGIVTPDEGLLNPNHYLAVAIEYLYTHRPsWPAGIAvgKTVVSSSI 357
Cdd:cd05800 216 PEPIEKNLGELAEAV--KEGGADLGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLENKG-LRGPVV--KTVSTTHL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 358 IDRVVAGIGRQLVEVPVGFKWFVDGLIGATLGFGGEESAGASFLrrdGSVwtTDKDGIIMALLAAEILAVTGATPSQRYH 437
Cdd:cd05800 291 IDRIAEKHGLPVYETPVGFKYIAEKMLEEDVLIGGEESGGLGIR---GHI--PERDGILAGLLLLEAVAKTGKPLSELVA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 438 ALAGEYGGPCYARIDAPADREQKARLARLsADQVSATELAGEPITAKLTtapgngaaLGGLKVTTAN-AWFAARPSGTED 516
Cdd:cd05800 366 ELEEEYGPSYYDRIDLRLTPAQKEAILEK-LKNEPPLSIAGGKVDEVNT--------IDGVKLVLEDgSWLLIRPSGTEP 436
|
490 500
....*....|....*....|....*.
gi 623360049 517 VYKIYAESfRGPQHLVEVQQTAREVV 542
Cdd:cd05800 437 LLRIYAEA-PSPEKVEALLDAGKKLA 461
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
122-542 |
6.08e-62 |
|
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this family include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). These enzymes play important and diverse roles in carbohydrate metabolism in organisms from bacteria to humans. Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100086 [Multi-domain] Cd Length: 355 Bit Score: 207.59 E-value: 6.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 122 AISHAILTYnrgrtealaDGIVVTPSHNPPSDGGIKYNPPNGGPADTAATTAIAKRANEILLARsmvkrLPLARALRTAQ 201
Cdd:cd03084 22 ALGQAIGST---------GGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPS-----AVAYELGGSVK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 202 RHDYLGHYVDDLPNVVDIAAIREAGVRIGADPLGGASVDYWGEIAHRHGLDLTVVNPLVDATWRFmtldtdgkIRMDCSS 281
Cdd:cd03084 88 AVDILQRYFEALKKLFDVAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNFGN--------INPDPGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 282 PDAMAGLIRTMfgNRERYQIATGNDADADRHGIVTPDEGLLNPNHYLAVAIEYLYTHrpsWPAGIAVGKTVVSSSIIDRV 361
Cdd:cd03084 160 ETNLKQLLAVV--KAEKADFGVAFDGDADRLIVVDENGGFLDGDELLALLAVELFLT---FNPRGGVVKTVVSSGALDKV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 362 VAGIGRQLVEVPVGFKWFVDGLIGATLGFGGEESAGASFLRRdgsvwTTDKDGIIMALLAAEILAVTGATPSQRYHALAG 441
Cdd:cd03084 235 AKKLGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGVIFPEF-----HPGRDGISAALLLLEILANLGKSLSELFSELPR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 442 EYggpcYARIDAPadreqkarlarlsadqvsatelagepitaklttapgngaalgglkvttanAWFAARPSGTEDVYKIY 521
Cdd:cd03084 310 YY----YIRLKVR--------------------------------------------------GWVLVRASGTEPAIRIY 335
|
410 420
....*....|....*....|.
gi 623360049 522 AESFRgPQHLVEVQQTAREVV 542
Cdd:cd03084 336 AEADT-QEDVEQIKKEARELV 355
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
42-546 |
7.78e-53 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 186.18 E-value: 7.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 42 FGTSGHRGSALTgTFNELHILAITQAIVEYrAAQGTTGPLFIGRDTHgLSEPAWVSAL-EVLAANQVvAVVDSRdrYTPT 120
Cdd:COG1109 7 FGTDGIRGIVGE-ELTPEFVLKLGRAFGTY-LKEKGGPKVVVGRDTR-LSSPMLARALaAGLASAGI-DVYDLG--LVPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 121 PAISHAILTYNrgrtealAD-GIVVTPSHNPPSDGGIKYNPPNGGPadtaattAIAKRANEI--LLARSMVKRLPLARAL 197
Cdd:COG1109 81 PALAFAVRHLG-------ADgGIMITASHNPPEYNGIKFFDADGGK-------LSPEEEKEIeaLIEKEDFRRAEAEEIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 198 RTAQRHDYLGHYVDDLPNVVDiAAIREAGVRIGADPLGGASVDYWGEIAHRHGLDLTVVNPLVDATwrFMTLDTDGKirm 277
Cdd:COG1109 147 KVTRIEDVLEAYIEALKSLVD-EALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGN--FPNHNPNPE--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 278 dcssPDAMAGLIRTMfgNRERYQIATGNDADADRHGIVTPDEGLLNPNHYLAVAIEYLYTHRPswpaGIAVGKTVVSSSI 357
Cdd:COG1109 221 ----PENLEDLIEAV--KETGADLGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGP----GGTVVVTVMSSLA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 358 IDRVVAGIGRQLVEVPVGFKWFVDGLIGATLGFGGEESAGASFLRrdgsvWTTDKDGIIMALLAAEILAVTGATPSQryh 437
Cdd:COG1109 291 LEDIAEKHGGEVVRTKVGFKYIKEKMRETGAVLGGEESGGIIFPD-----FVPTDDGILAALLLLELLAKQGKSLSE--- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 438 aLAGEYGGPCYARIDAPADREQKarLARLSADQVSATELAGEPITaklttapgngaaLGGLKVTTAN-AWFAARPSGTED 516
Cdd:COG1109 363 -LLAELPRYPQPEINVRVPDEEK--IGAVMEKLREAVEDKEELDT------------IDGVKVDLEDgGWVLVRPSGTEP 427
|
490 500 510
....*....|....*....|....*....|
gi 623360049 517 VYKIYAESfRGPQHLVEVQQTAREVVDRVI 546
Cdd:COG1109 428 LLRVYAEA-KDEEEAEELLAELAELVEEAL 456
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
323-443 |
7.15e-38 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 135.27 E-value: 7.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 323 NPNHYLAVAIEYLYTHRpSWPAGIAVGKTVVSSSIIDRVVAGIGRQLVEVPVGFKWFVDGLIGATLGFGGEESAGASFLR 402
Cdd:pfam02880 1 DGDQILALLAKYLLEQG-KLPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 623360049 403 RDgsvwtTDKDGIIMALLAAEILAVTGATPSQRYHALAGEY 443
Cdd:pfam02880 80 HA-----TTKDGILAALLVLEILARTGKSLSELLEELPEKY 115
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
40-165 |
2.77e-36 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 131.58 E-value: 2.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 40 VAFGTSGHRGSALTGTFNELHILAITQAIVEYRAAQGTTGPLFIGRDTHGLSEPAWVSALEVLAANQVVAVVDSrdrYTP 119
Cdd:pfam02878 2 QLFGTSGIRGKVGVGELTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLG---LLP 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 623360049 120 TPAISHAILTYNrgrteaLADGIVVTPSHNPPSDGGIKYNPPNGGP 165
Cdd:pfam02878 79 TPAVSFATRKLK------ADGGIMITASHNPPEYNGIKVFDSNGGP 118
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
42-524 |
3.98e-23 |
|
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]
Pssm-ID: 274906 Cd Length: 443 Bit Score: 102.21 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 42 FGTSGHRGSALTGtFNELHILAITQAIVEYRAAqgttGPLFIGRDTHgLSEPAWVSALEVLAANQVVAVVDSRdrYTPTP 121
Cdd:TIGR03990 4 FGTSGIRGIVGEE-LTPELALKVGKAFGTYLRG----GKVVVGRDTR-TSGPMLENAVIAGLLSTGCDVVDLG--IAPTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 122 AISHAILTYNrgrtealAD-GIVVTPSHNPPSDGGIKYNPPNGgpadtaatTAIAKRANEILLARSMVKRLPLARALRTA 200
Cdd:TIGR03990 76 TLQYAVRELG-------ADgGIMITASHNPPEYNGIKLLNSDG--------TELSREQEEEIEEIAESGDFERADWDEIG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 201 QR---HDYLGHYVDDLPNVVDIAAIREAGVRIGADPLGGASvdywgeiahrhglDLTVVNPLVDATWRFMTL--DTDGK- 274
Cdd:TIGR03990 141 TVtsdEDAIDDYIEAILDKVDVEAIRKKGFKVVVDCGNGAG-------------SLTTPYLLRELGCKVITLncQPDGTf 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 275 -IRMDCSSPDAMAGLIRTMfgnRER-YQIATGNDADADRHGIVTPDEGLLNPNHYLAVAIEYLYTHRPswpagiavGKTV 352
Cdd:TIGR03990 208 pGRNPEPTPENLKDLSALV---KATgADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLLEHGG--------GKVV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 353 V---SSSIIDRVVAGIGRQLVEVPVGFKWFVDGLI--GATlgFGGEESAGasFLRRDGSVWttdKDGIIMALLAAEILAV 427
Cdd:TIGR03990 277 TnvsSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKeeGAV--FGGEGNGG--WIFPDHHYC---RDGLMAAALFLELLAE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 428 TGATPSQryhaLAGEYggPCYA--RIDAPADREQKAR-LARLsadqvsATELAGEPITAklttapgngaaLGGLKVTTAN 504
Cdd:TIGR03990 350 EGKPLSE----LLAEL--PKYPmsKEKVELPDEDKEEvMEAV------EEEFADAEIDT-----------IDGVRIDFED 406
|
490 500
....*....|....*....|
gi 623360049 505 AWFAARPSGTEDVYKIYAES 524
Cdd:TIGR03990 407 GWVLVRPSGTEPIVRIYAEA 426
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
42-542 |
2.44e-21 |
|
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100089 Cd Length: 439 Bit Score: 96.49 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 42 FGTSGHRGSALTGTFNELhILAITQAIVEYRAAqgttGPLFIGRDTHgLSEPAWVSALE--VLAANQVVAVVDsrdrYTP 119
Cdd:cd03087 2 FGTSGIRGVVGEELTPEL-ALKVGKALGTYLGG----GTVVVGRDTR-TSGPMLKNAVIagLLSAGCDVIDIG----IVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 120 TPAISHAILTYNRGrtealadGIVVTPSHNPPSDGGIKYNPPNGgpadtaaTTAIAKRANEI--LLARSMVKRLPLARAL 197
Cdd:cd03087 72 TPALQYAVRKLGDA-------GVMITASHNPPEYNGIKLVNPDG-------TEFSREQEEEIeeIIFSERFRRVAWDEVG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 198 RTAQRHDYLGHYVDDLPNVVDIAAIReaGVRIGADPLGGASVDYWGEIAHRHGLDLTVVNPLVDATWrfmtldtdgKIRM 277
Cdd:cd03087 138 SVRREDSAIDEYIEAILDKVDIDGGK--GLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFF---------PGRP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 278 DCSSPDAMAGLIRTM------FGnreryqIAtgNDADADRHGIVTPDEGLLNPNHYLAVAIEYLYTHRPSwpagiAVGKT 351
Cdd:cd03087 207 PEPTPENLSELMELVratgadLG------IA--HDGDADRAVFVDEKGRFIDGDKLLALLAKYLLEEGGG-----KVVTP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 352 VVSSSIIDRVVAGIGRQLVEVPVGfkwfvDGLIGATLG-----FGGEESAGasflrrdgsvWTTDK-----DGIIMALLA 421
Cdd:cd03087 274 VDASMLVEDVVEEAGGEVIRTPVG-----DVHVAEEMIengavFGGEPNGG----------WIFPDhqlcrDGIMTAALL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 422 AEILAVTGaTPSQRYHALageyggPCY--ARIDAPADREQKARLARLSADQVSatELAGEPITaklttapgngaaLGGLK 499
Cdd:cd03087 339 LELLAEEK-PLSELLDEL------PKYplLREKVECPDEKKEEVMEAVEEELS--DADEDVDT------------IDGVR 397
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 623360049 500 VTTANAWFAARPSGTEDVYKIYAESfRGPQHLVEVQQTAREVV 542
Cdd:cd03087 398 IEYEDGWVLIRPSGTEPKIRITAEA-KTEERAKELLEEGRSKV 439
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
43-431 |
1.74e-12 |
|
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate (G-1-P) and glucose-6-phosphate (G-6-P) via a glucose 1,6-diphosphate intermediate, an important metabolic step in prokaryotes and eukaryotes. In one direction, G-1-P produced from sucrose catabolism is converted to G-6-P, the first intermediate in glycolysis. In the other direction, conversion of G-6-P to G-1-P generates a substrate for synthesis of UDP-glucose which is required for synthesis of a variety of cellular constituents including cell wall polymers and glycoproteins. The PGM1 family also includes a non-enzymatic PGM-related protein (PGM-RP) thought to play a structural role in eukaryotes, as well as pp63/parafusin, a phosphoglycoprotein that plays an important role in calcium-regulated exocytosis in ciliated protozoans. PGM1 belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100087 [Multi-domain] Cd Length: 548 Bit Score: 69.94 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 43 GTSGHRGSalTGTFNELH-----ILAITQAIVEYRAAQGTtgpLFIGRDTHGLSEPAWVSALEVLAANQVVAVVDSRDRY 117
Cdd:cd03085 14 GTSGLRKK--VKVFQQPNylenfVQSIFNALPPEKLKGAT---LVVGGDGRYYNKEAIQIIIKIAAANGVGKVVVGQNGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 118 TPTPAISHAILTYNrgrteaLADGIVVTPSHNP--PS-DGGIKYNPPNGGPadtaattAIAKRANEILLARSMVKRLPLA 194
Cdd:cd03085 89 LSTPAVSAVIRKRK------ATGGIILTASHNPggPEgDFGIKYNTSNGGP-------APESVTDKIYEITKKITEYKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 195 RALR----------------TAQRHDYLGHYVDDLPNVVDIAAIREA----GVRIGADPLGGASVDYWGEIAHRH-GLDL 253
Cdd:cd03085 156 DDPDvdlskigvtkfggkpfTVEVIDSVEDYVELMKEIFDFDAIKKLlsrkGFKVRFDAMHGVTGPYAKKIFVEElGAPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 254 -TVVN--PLVDatwrFmtldtDGKirmdcsSPDA----MAGLIRTMFgnRERYQIATGNDADADRHGI------VTPDEG 320
Cdd:cd03085 236 sSVVNctPLPD----F-----GGG------HPDPnltyAKDLVELMK--SGEPDFGAASDGDGDRNMIlgkgffVTPSDS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 321 LLNPNHYlAVAIEYLYTHrpswpaGIA-VGKTVVSSSIIDRVVAGIGRQLVEVPVGFKWFVDGLIGATLGFGGEESAGAs 399
Cdd:cd03085 299 VAVIAAN-AKLIPYFYKG------GLKgVARSMPTSGALDRVAKKLGIPLFETPTGWKFFGNLMDAGKLSLCGEESFGT- 370
|
410 420 430
....*....|....*....|....*....|....
gi 623360049 400 flrrdGSVWTTDKDGI--IMALLAaeILAVTGAT 431
Cdd:cd03085 371 -----GSDHIREKDGLwaVLAWLS--ILAHRNVS 397
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
209-318 |
4.54e-11 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 59.61 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 209 YVDDLPNVVDIAAIREAGVRIGADPLGGASVDYWGEIAHRHGLDLTVVNPLVDATWRFMTLDTDGkirmdcssPDAMAGL 288
Cdd:pfam02879 2 YIDHLLELVDSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPTRAPNPEE--------PEALALL 73
|
90 100 110
....*....|....*....|....*....|
gi 623360049 289 IRTMfgNRERYQIATGNDADADRHGIVTPD 318
Cdd:pfam02879 74 IELV--KSVGADLGIATDGDADRLGVVDER 101
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
42-546 |
1.04e-10 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 64.32 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 42 FGTSGHRGSALTGtFNELHILAITQAiveyraAQG-------TTGP------LFIGRD-THGLSEPAWVSA-------LE 100
Cdd:PTZ00150 47 FGTAGLRGKMGAG-FNCMNDLTVQQT------AQGlcayvieTFGQalksrgVVIGYDgRYHSRRFAEITAsvflskgFK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 101 VLAANQVVavvdsrdrytPTPAISHAILTYNrgrteALAdGIVVTPSHNPPSDGGIKYNPPNGGPADTAATTAIAKRANE 180
Cdd:PTZ00150 120 VYLFGQTV----------PTPFVPYAVRKLK-----CLA-GVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKILS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 181 ILlarsmvKRLPLARALRTAQRH-----DYLGHYVDDLPNVVDIAAIREAGVRIGADPLGGASVDYWGEIAHRHGLD--L 253
Cdd:PTZ00150 184 NL------EPWSSSWEYLTETLVedplaEVSDAYFATLKSEYNPACCDRSKVKIVYTAMHGVGTRFVQKALHTVGLPnlL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 254 TV---VNPLVD-ATWRFMTLDtDGKIRMDCSspdamaglIRTMFGNRERYQIAtgNDADADRHG----------IVTPDE 319
Cdd:PTZ00150 258 SVaqqAEPDPEfPTVTFPNPE-EGKGALKLS--------METAEAHGSTVVLA--NDPDADRLAvaeklnngwkIFTGNE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 320 gllnpnhyLAVAIEYLYTHRPSWpAGIAVGK-----TVVSSSIIDRVVAGIGRQLVEVPVGFKWFVDGLI------GATL 388
Cdd:PTZ00150 327 --------LGALLAWWAMKRYRR-QGIDKSKcfficTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIelnaenGLTT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 389 GFGGEESAgasflrrdGSVWTT---DKDGIIMALLAAEI---LAVTGATPSQRYHALAGEYG----GPCYARIDAPADRE 458
Cdd:PTZ00150 398 LFAYEEAI--------GFMLGTrvrDKDGVTAAAVVAEMalyLYERGKTLVEHLESLYKQYGyhftNNSYYICYDPSRIV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 459 qkARLARLSADQVSATELAGEPITA--KLTTAPGNGAALG-------------------GLKVTTanawfaaRPSGTEDV 517
Cdd:PTZ00150 470 --SIFNDIRNNGSYPTKLGGYPVTRirDLTTGYDTATPDGkpllpvsastqmitfyfenGAIITI-------RGSGTEPK 540
|
570 580
....*....|....*....|....*....
gi 623360049 518 YKIYAESFRGPQHlvEVQQTAREVVDRVI 546
Cdd:PTZ00150 541 LKWYAELSGTKDE--AVEKELAALVDEVV 567
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
68-546 |
7.05e-10 |
|
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate guanyltransferase domain in a protein of unknown function that is found in both prokaryotes and eukaryotes. This domain belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100096 Cd Length: 445 Bit Score: 61.17 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 68 IVEYRAAQGT-------TGPLFIGRDTH--GLSEPAWVSALEVLAANQVVAVvdsrdRYTPTPAISHAIltynrgRTEAL 138
Cdd:cd05803 20 ITRYVAAFATwqpertkGGKIVVGRDGRpsGPMLEKIVIGALLACGCDVIDL-----GIAPTPTVQVLV------RQSQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 139 ADGIVVTPSHNPPSDGGIKYNPPNGgpadtaattaiakranEILLARSMVKRLPLARAlRTAQ--RHDYLGHYV------ 210
Cdd:cd05803 89 SGGIIITASHNPPQWNGLKFIGPDG----------------EFLTPDEGEEVLSCAEA-GSAQkaGYDQLGEVTfsedai 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 211 -DDLPNV-----VDIAAIREAGVRIGADPLGGASVDYWGEIAHRHGLDLTVVNplvdatwrfmtLDTDGKIRMDCSS-PD 283
Cdd:cd05803 152 aEHIDKVlalvdVDVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLN-----------CEPTGLFPHTPEPlPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 284 AMAGLIRTMfgNRERYQIATGNDADADRHGIVTPDEGLLNPNHYLAVAIEYL--YTHRPswpagiavGKTVV---SSSII 358
Cdd:cd05803 221 NLTQLCAAV--KESGADVGFAVDPDADRLALVDEDGRPIGEEYTLALAVDYVlkYGGRK--------GPVVVnlsTSRAL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 359 DRVVAGIGRQLVEVPVGFKWFVDGLIGATLGFGGEESAGASFLR----RDGSVwttdkdGIIMALlaaEILAVTGATPSQ 434
Cdd:cd05803 291 EDIARKHGVPVFRSAVGEANVVEKMKEVDAVIGGEGNGGVILPDvhygRDSLV------GIALVL---QLLAASGKPLSE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 435 ryhaLAGEYGGPCYARIDAPADREQKARLARlsadqvsatELAGEPITAKLTTapgngaaLGGLKVTTANAWFAARPSGT 514
Cdd:cd05803 362 ----IVDELPQYYISKTKVTIAGEALERLLK---------KLEAYFKDAEAST-------LDGLRLDSEDSWVHVRPSNT 421
|
490 500 510
....*....|....*....|....*....|..
gi 623360049 515 EDVYKIYAESfrgpqhlvEVQQTAREVVDRVI 546
Cdd:cd05803 422 EPIVRIIAEA--------PTQDEAEALADRFI 445
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
43-426 |
1.85e-09 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 60.05 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 43 GTSGHRGSAltGTFNELHILA-ITQAIVEYRAAQGTTG-PLFIGRDTHGLSEPAWVSALEVLAANQVVAVVDSRDRYTPT 120
Cdd:PLN02307 26 GTSGLRKKV--KVFMQENYLAnFVQALFNALPAEKVKGaTLVLGGDGRYFNKEAIQIIIKIAAANGVRRVWVGQNGLLST 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 121 PAISHAIltynRGRTEALADG-IVVTPSHNP--PS-DGGIKYNPPNGGPadtaattAIAKRANEILLARSMVKRLPLARA 196
Cdd:PLN02307 104 PAVSAVI----RERDGSKANGgFILTASHNPggPEeDFGIKYNYESGQP-------APESITDKIYGNTLTIKEYKMAED 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 197 LR------------------TAQRHDYLGHYVDDLPNVVDIAAIREAGVRIG----ADPLGGASvdywGEIAHRhgldlt 254
Cdd:PLN02307 173 IPdvdlsavgvtkfggpedfDVEVIDPVEDYVKLMKSIFDFELIKKLLSRPDftfcFDAMHGVT----GAYAKR------ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 255 vvnPLVDAtwrfmtLDTDGKIRMDCSSPDAMAG------------LIRTMFGNRERY-----QIATGNDADADRHGI--- 314
Cdd:PLN02307 243 ---IFVEE------LGAPESSLLNCVPKEDFGGghpdpnltyakeLVKRMGLGKTSYgdeppEFGAASDGDGDRNMIlgk 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 315 ---VTPDEGllnpnhyLAV-------AIEYLythrPSWPAGIAvgKTVVSSSIIDRVVAGIGRQLVEVPVGFKWFVDGLI 384
Cdd:PLN02307 314 rffVTPSDS-------VAIiaanaqeAIPYF----SGGLKGVA--RSMPTSAALDVVAKKLNLPFFEVPTGWKFFGNLMD 380
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 623360049 385 GATLGFGGEESAGAsflrrdGSVWTTDKDGIIMALLAAEILA 426
Cdd:PLN02307 381 AGKLSICGEESFGT------GSDHIREKDGIWAVLAWLSILA 416
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
42-157 |
2.03e-09 |
|
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the alpha-D-phosphohexomutase superfamily. It is required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate in the biosynthetic pathway of UDP-N-acetylglucosamine, an essential precursor to components of the cell envelope. In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. Other members of the alpha-D-phosphohexomutase superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100095 Cd Length: 434 Bit Score: 59.81 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 42 FGTSGHRGSA---LTGTFnelhILAITQAIVEYRAAQGTTGPLFIGRDTHgLSEPAWVSALE--VLAANQVVAVVDSrdr 116
Cdd:cd05802 2 FGTDGIRGVAnepLTPEL----ALKLGRAAGKVLGKGGGRPKVLIGKDTR-ISGYMLESALAagLTSAGVDVLLLGV--- 73
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 623360049 117 yTPTPAISHaiLTynrgRTEALADGIVVTPSHNPPSDGGIK 157
Cdd:cd05802 74 -IPTPAVAY--LT----RKLRADAGVVISASHNPFEDNGIK 107
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
48-542 |
5.09e-08 |
|
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100091 Cd Length: 443 Bit Score: 55.21 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 48 RGSALTgTFNELHILAITQAIVEYRAAQGTtGPLFIGRDTHgLSEPAWVSALE--VLAANqvVAVVD---SrdrytPTPA 122
Cdd:cd03089 8 RGIAGE-ELTEEIAYAIGRAFGSWLLEKGA-KKVVVGRDGR-LSSPELAAALIegLLAAG--CDVIDiglV-----PTPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 123 ISHAILTYNRGrtealaDGIVVTPSHNPPSDGGIKYNPPNGGPadtaattaiakRANEI--LLARSMVKRLPLARALRTA 200
Cdd:cd03089 78 LYFATFHLDAD------GGVMITASHNPPEYNGFKIVIGGGPL-----------SGEDIqaLRERAEKGDFAAATGRGSV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 201 QRHDYLGHYVDDLpnvVDIAAIREAGVRIGADPLGGASVDYWGEIAHRHGLDLTVVNplvdatwrfmtLDTDGKI---RM 277
Cdd:cd03089 141 EKVDILPDYIDRL---LSDIKLGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLF-----------CEPDGTFpnhHP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 278 DCSSPDAMAGLIRTMfgNRERYQIATGNDADADRHGIVTPDEGLLNPNHYLAV-AIEYLYTHrpswPAGIAVGKTVVSSS 356
Cdd:cd03089 207 DPTDPENLEDLIAAV--KENGADLGIAFDGDGDRLGVVDEKGEIIWGDRLLALfARDILKRN----PGATIVYDVKCSRN 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 357 IIDRVVAGIGRQlVEVPVGFKwfvdgLIGATLG-----FGGEESAGASFlrRDGsvWTTDKDGIIMALLAAEILAVTGAT 431
Cdd:cd03089 281 LYDFIEEAGGKP-IMWKTGHS-----FIKAKMKetgalLAGEMSGHIFF--KDR--WYGFDDGIYAALRLLELLSKSGKT 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 432 PSQRYHALageyggPCYA-----RIDAPADrEQKARLARLSAdqvSATELAGEPITaklttapgngaaLGGLKVTTANAW 506
Cdd:cd03089 351 LSELLADL------PKYFstpeiRIPVTEE-DKFAVIERLKE---HFEFPGAEIID------------IDGVRVDFEDGW 408
|
490 500 510
....*....|....*....|....*....|....*.
gi 623360049 507 FAARPSGTEDVYKIYAESfRGPQHLVEVQQTAREVV 542
Cdd:cd03089 409 GLVRASNTEPVLVLRFEA-DTEEGLEEIKAELRKLL 443
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
204-525 |
4.67e-05 |
|
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose pyrophosphorylase, is a bifunctional enzyme with both phosphomannose isomerase (PMI) activity and GDP-mannose phosphorylase (GMP) activity. The protein contains an N-terminal NTP transferase domain, an L-beta-H domain, and a C-terminal PGM-like domain that belongs to the alpha-D-phosphohexomutase superfamily. This subfamily is limited to bacteria and archaea. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this group appear to lack conserved residues necessary for metal binding and catalytic activity. Other members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100097 Cd Length: 441 Bit Score: 46.09 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 204 DYLGHYVDDLPNVVDIAAIREAGVRIGADPLGGASVDYWGEIAHRHGLDLTVVNPLVDATWRFMTldtdgkiRMDCSSPD 283
Cdd:cd05805 146 DFVEYYIRGLLRALDTSGLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVILNARLDEDAPRTD-------TERQRSLD 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 284 AMAGLIRTM---FGnrerYQIatgnDADADRHGIVTpDEG-LLNPNHYLAVaieYLYTHRPSWPagiavGKTVV----SS 355
Cdd:cd05805 219 RLGRIVKALgadFG----VII----DPNGERLILVD-EAGrVISDDLLTAL---VSLLVLKSEP-----GGTVVvpvtAP 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 356 SIIDRVvagIGRQLVEVpVGFKWFVDGLIGATLG---FGGEESAGASFLRRDGSVwttdkDGIIMALLAAEILAVTGATP 432
Cdd:cd05805 282 SVIEQL---AERYGGRV-IRTKTSPQALMEAALEnvvLAGDGDGGFIFPEFHPGF-----DAIAALVKILEMLARTNISL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 433 SQRYHALAGEYggpcYARIDAPADREQKARLARlsadqvsatELAGEPITAKLTTapgngaaLGGLKVTTANAWFAARPS 512
Cdd:cd05805 353 SQIVDELPRFY----VLHKEVPCPWEAKGRVMR---------RLIEEAPDKSIEL-------IDGVKIYEDDGWVLVLPD 412
|
330
....*....|...
gi 623360049 513 GTEDVYKIYAESF 525
Cdd:cd05805 413 ADEPLCHIYAEGS 425
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
41-163 |
1.60e-04 |
|
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose 6-phosphate to mannose-1-phosphate in the second of three steps in the GDP-mannose pathway, in which GDP-D-mannose is synthesized from fructose-6-phosphate. In Mycobacterium tuberculosis, the causative agent of tuberculosis, PMM is involved in the biosynthesis of mannosylated lipoglycans that participate in the association of mycobacteria with host macrophage phagocytic receptors. ManB belongs to the the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100090 Cd Length: 459 Bit Score: 44.11 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 623360049 41 AFGTSGHRG--SALTGtfneLHILAITQAIVEYRAAQGTTGPLFIGRDTHGlSEPAWVSALEVLAANQVVAVVDSRDryT 118
Cdd:cd03088 1 KFGTSGLRGlvTDLTD----EVCYAYTRAFLQHLESKFPGDTVAVGRDLRP-SSPRIAAACAAALRDAGFRVVDCGA--V 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 623360049 119 PTPAISHAiltynrgrteALADG---IVVTPSHNPPSDGGIKYNPPNG 163
Cdd:cd03088 74 PTPALALY----------AMKRGapaIMVTGSHIPADRNGLKFYRPDG 111
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
141-164 |
6.94e-04 |
|
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 (N-acetylglucosamine-phosphate mutase), is an essential enzyme found in eukaryotes that reversibly catalyzes the conversion of GlcNAc-6-phosphate into GlcNAc-1-phosphate as part of the UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthetic pathway. UDP-GlcNAc is an essential metabolite that serves as the biosynthetic precursor of many glycoproteins and mucopolysaccharides. AGM1 is a member of the alpha-D-phosphohexomutase superfamily, which catalyzes the intramolecular phosphoryl transfer of sugar substrates. The alpha-D-phosphohexomutases have four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100088 Cd Length: 513 Bit Score: 42.20 E-value: 6.94e-04
10 20
....*....|....*....|....
gi 623360049 141 GIVVTPSHNPPSDGGIKYNPPNGG 164
Cdd:cd03086 38 GVMITASHNPVEDNGVKIVDPDGE 61
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
130-164 |
8.04e-04 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 42.33 E-value: 8.04e-04
10 20 30
....*....|....*....|....*....|....*
gi 623360049 130 YNRGRTEALADGIVVTPSHNPPSDGGIKYNPPNGG 164
Cdd:PTZ00302 67 GKRAKRGNKSVGVMITASHNPIQDNGVKIIDPDGG 101
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
119-163 |
6.40e-03 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 38.96 E-value: 6.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 623360049 119 PTPAIshAILTynrgRTEALADGIVVTPSHNPPSDGGIKYNPPNG 163
Cdd:PRK10887 77 PTPAV--AYLT----RTLRAEAGIVISASHNPYYDNGIKFFSADG 115
|
|
| |
