|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
3-544 |
0e+00 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 1047.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 3 NNPRAGQPARQSDLINVAQLTSQYYVLQPEAGNAAHAVKFGTSGHRGSAQRHSFNEAHILAIAQAIAEVRHQQGTTGPCY 82
Cdd:PRK07564 1 IHPRAGQPAQPSDLINVPRLVSAYYTLKPDPTNPFQDVKFGTSGHRGSSLQPSFNENHILAIFQAICEYRGKQGITGPLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 83 VGKDTHALSEPAFISVLEVLTANGVDVIVQENNGFTPTPAVSHAILCHNRRGGAQADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:PRK07564 81 VGGDTHALSEPAIQSALEVLAANGVGVVIVGRGGYTPTPAVSHAILKYNGRGGGLADGIVITPSHNPPEDGGIKYNPPNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 163 GPADTNLTSVIEKRANELLAQQLKGVQRQSLDKAWNSGHLHAKDLVQPYVEGLVDVVDMPAIQRAGLKLGVDPLGGSGIA 242
Cdd:PRK07564 161 GPADTDVTDAIEARANELLAYGLKGVKRIPLDRALASMTVEVIDPVADYVEDLENVFDFDAIRKAGLRLGVDPLGGATGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 243 YWQRVAEHYKLDLTLVNDSIDQTFRFMHLDHDGIIRMDCSSESAMAGLLALRDKFDLAFANDPDYDRHGIVTPKGLMNPN 322
Cdd:PRK07564 241 YWKAIAERYGLDLTVVNAPVDPTFNFMPLDDDGKIRMDCSSPYAMAGLLALKDAFDLAFANDPDGDRHGIVTPGGLMNPN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 323 HYLAVAINYLFQHRPQWGADVAVGKTLVSSAMIDRVVADLGRKLVEVPVGFKWFVDGLFDGSLGFGGEESAGASFLRFNG 402
Cdd:PRK07564 321 HYLAVAIAYLFHHRPGWRAGAGVGKTLVSSAMIDRVAAKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESAGASFLRRDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 403 QPWSTDKDGIIMCLLAAEITAVTGENPQHHYDDLAKRFGAPSYNRIQAPATHAQKAALSKLSPEMVKASTLGGDPITARL 482
Cdd:PRK07564 401 SVWTTDKDGLIAVLLAAEILAVTGKSPSEIYRELWARFGRPYYSRHDAPATPEQKAALRKLSPELVGATELAGDPIDASL 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515495496 483 TAAPGNGASIGGLKVMTDNGWFAARPSGTEEAYKIYCESFLGAEHREKIEHEAVEIVSEVLA 544
Cdd:PRK07564 481 TEAPGNGAAIGGLKVVTENGWFAARPSGTETTYKIYAESFEGDEHLHQIQKEAQEIVADLIA 542
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
20-539 |
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: 1034.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 20 AQLTSQYYVLQPEAGNAAHAVKFGTSGHRGSAQRHSFNEAHILAIAQAIAEVRHQQGTTGPCYVGKDTHALSEPAFISVL 99
Cdd:cd05801 1 PRLITAYYTLKPDPSNPAQRVAFGTSGHRGSSLKGSFNEAHILAISQAICDYRKSQGITGPLFLGKDTHALSEPAFISAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 100 EVLTANGVDVIVQENNGFTPTPAVSHAILCHNR-RGGAQADGIVITPSHNPPEDGGIKYNPPNGGPADTNLTSVIEKRAN 178
Cdd:cd05801 81 EVLAANGVEVIIQQNDGYTPTPVISHAILTYNRgRTEGLADGIVITPSHNPPEDGGFKYNPPHGGPADTDITRWIEKRAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 179 ELLAQQLKGVQRQSLDKAWNSGHLHAKDLVQPYVEGLVDVVDMPAIQRAGLKLGVDPLGGSGIAYWQRVAEHYKLDLTLV 258
Cdd:cd05801 161 ALLANGLKGVKRIPLEAALASGYTHRHDFVTPYVADLGNVIDMDAIRKSGLRLGVDPLGGASVPYWQPIAEKYGLNLTVV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 259 NDSIDQTFRFMHLDHDGIIRMDCSSESAMAGLLALRDKFDLAFANDPDYDRHGIVTPK-GLMNPNHYLAVAINYLFQHRP 337
Cdd:cd05801 241 NPKVDPTFRFMTLDHDGKIRMDCSSPYAMAGLLKLKDKFDLAFANDPDADRHGIVTPSaGLMNPNHYLSVAIDYLFTHRP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 338 QWGADVAVGKTLVSSAMIDRVVADLGRKLVEVPVGFKWFVDGLFDGSLGFGGEESAGASFLRFNGQPWSTDKDGIIMCLL 417
Cdd:cd05801 321 LWNKSAGVGKTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDGLLDGSLGFGGEESAGASFLRRDGTVWTTDKDGIIMCLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 418 AAEITAVTGENPQHHYDDLAKRFGAPSYNRIQAPATHAQKAALSKLSPEMVKASTLGGDPITARLTAAPGNGASIGGLKV 497
Cdd:cd05801 401 AAEILAVTGKDPGQLYQELTERFGEPYYARIDAPATPEQKARLKKLSPEQVTATELAGDPILAKLTRAPGNGASIGGLKV 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 515495496 498 MTDNGWFAARPSGTEEAYKIYCESFLGAEHREKIEHEAVEIV 539
Cdd:cd05801 481 TTANGWFAARPSGTEDVYKIYAESFLSEEHLKKIQKEAQEIV 522
|
|
| pgm |
TIGR01132 |
phosphoglucomutase, alpha-D-glucose phosphate-specific; This enzyme interconverts ... |
2-543 |
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: 1016.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 2 ANNPRAGQPARQSDLINVAQLTSQYYVLQPEAGNAAHAVKFGTSGHRGSAQRHSFNEAHILAIAQAIAEVRHQQGTTGPC 81
Cdd:TIGR01132 1 AIHPRAGQPAQQEDLINVAQLVAQYYVLQPEAGNAAHAVKFGTSGHRGSALRGTFNEPHILAIAQAIAEYRAAQGITGPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 82 YVGKDTHALSEPAFISVLEVLTANGVDVIVQENNGFTPTPAVSHAILCHNRRGGAQADGIVITPSHNPPEDGGIKYNPPN 161
Cdd:TIGR01132 81 YIGKDTHALSEPAFISVLEVLAANGVEVIVQENNGFTPTPAVSHAILTHNKKGEPLADGIVITPSHNPPEDGGIKYNPPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 162 GGPADTNLTSVIEKRANELLAQQLKGVQRQSLDKAWNSGHLHAKDLVQPYVEGLVDVVDMPAIQRAGLKLGVDPLGGSGI 241
Cdd:TIGR01132 161 GGPADTEATQAIEDRANALLANGLKGVKRLPLAQALASGTVKAHDLVQPYVDGLADIVDMAAIQKAGLRLGVDPLGGSGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 242 AYWQRVAEHYKLDLTLVNDSIDQTFRFMHLDHDGIIRMDCSSESAMAGLLALRDKFDLAFANDPDYDRHGIVTPKGLMNP 321
Cdd:TIGR01132 241 DYWKRIAEKYNLNLTLVNPQVDPTFRFMTLDKDGKIRMDCSSPYAMAGLLALRDKYDLAFGNDPDYDRHGIVTPAGLMNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 322 NHYLAVAINYLFQHRPQWGADVAVGKTLVSSAMIDRVVADLGRKLVEVPVGFKWFVDGLFDGSLGFGGEESAGASFLRFN 401
Cdd:TIGR01132 321 NHYLAVAINYLFQHRPQWGGDVAVGKTLVSSAMIDRVVADLGRQLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 402 GQPWSTDKDGIIMCLLAAEITAVTGENPQHHYDDLAKRFGAPSYNRIQAPATHAQKAALSKLSPEMVKASTLGGDPITAR 481
Cdd:TIGR01132 401 GTPWSTDKDGIIMCLLAAEITAVTGKNPQQHYNELAAKFGAPSYNRIQAPATSAQKARLKKLSPEMVSATTLAGDPITAR 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515495496 482 LTAAPGNGASIGGLKVMTDNGWFAARPSGTEEAYKIYCESFLGAEHREKIEHEAVEIVSEVL 543
Cdd:TIGR01132 481 LTAAPGNGAAIGGLKVTTDNGWFAARPSGTEDVYKIYCESFKGEEHLKQIEKEAVEIVSEVL 542
|
|
| Pgm |
COG0033 |
Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism]; |
3-545 |
0e+00 |
|
Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 439803 Cd Length: 544 Bit Score: 1013.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 3 NNPRAGQPARQSDLINVAQLTSQYYVLQPEAGNAAHAVKFGTSGHRGSAQRHSFNEAHILAIAQAIAEVRHQQGTTGPCY 82
Cdd:COG0033 1 LHPRAGQPAPPSDLIDVPRLVSAYYTIKPDPTTPFQDVKFGTSGHRGSSLKGSFNEPHILAITQAIFDYRKAQGITGPLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 83 VGKDTHALSEPAFISVLEVLTANGVDVIVQENNGFTPTPAVSHAILCHNRRGGAQADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:COG0033 81 LGGDTHALSEPAIQTALEVLAANGVGVVIVGQGGYTPTPAVSHAILKYNRGTSGAADGIVLTPSHNPPEDGGIKYNPPNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 163 GPADTNLTSVIEKRANELLAQQLKGVQRQSLDKAWNSGHLHAKDLVQPYVEGLVDVVDMPAIQRAGLKLGVDPLGGSGIA 242
Cdd:COG0033 161 GPADEDVTDAIEARANEILEYGLADVKRVPLDRAGTAMTVEVIDPVADYVELLESVFDFDAIRAAGFRIGFDPLGGATGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 243 YWQRVAEHYKLDLTLVNDSIDQTFRFMHLDHDGIIRMDCSSESAMAGLLALRDKFDLAFANDPDYDRHGIVTPK-GLMNP 321
Cdd:COG0033 241 YWKAIAERYGLDLTVVNGVPDPDFRFMTLDWDGGIRMDPSSPYAMASLIAGKDAPDFAAANDGDGDRHGIVTPRgGLMNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 322 NHYLAVAINYLFQHRPQWGADVAVGKTLVSSAMIDRVVADLGRKLVEVPVGFKWFVDGLFDGSLGFGGEESAGASFLRFN 401
Cdd:COG0033 321 NHYLAVAIAYLFTHRPGWAALAGVGKTMVTSSAIDRVAAALGRPLYEVPVGFKWFVNGLDAGSLGFGGEESAGASFLRRD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 402 GQPWSTDKDGIIMCLLAAEITAVTGENPQHHYDDLAKRFGAPSYNRIQAPATHAQKAALSKLSPEMVKASTLGGDPITAR 481
Cdd:COG0033 401 GSVWTTDKDGLWAVLLAAEILAVTGKSPAEIYRELWARFGRPYYSRHDAEATDEQKARLAKLSGEQVGATTLAGEDIFAY 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515495496 482 LTAAPGNGASIGGLKVMTDNGWFAARPSGTEEAYKIYCESFLGAEHREKIEHEAVEIVSEVLAS 545
Cdd:COG0033 481 LDPAPGNGAAIGGLKVVTENGWFAARPSGTETTYKIYAESFEGDEHLHQIDAEAADLVDAALAL 544
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
41-539 |
2.06e-96 |
|
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: 296.96 E-value: 2.06e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 41 KFGTSGHRGSAQRHsFNEAHILAIAQAIAEVrhqqgttgpcyvgkdthalsepafisvlevltangvdvivqenngftpt 120
Cdd:cd03084 1 IFGTSGVRGVVGDD-ITPETAVALGQAIGST------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 121 pavshailchnrrggaqaDGIVITPSHNPPEDGGIKYNPPNGGPADTNLTSVIEKRANELLAQQLKGVQRqsldkawnSG 200
Cdd:cd03084 31 ------------------GGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYEL--------GG 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 201 HLHAKDLVQPYVEGLVDVVDMPAIQRAGLKLGVDPLGGSGIAYWQRVAEHYKLDLTLVNDSIDQTFrfmhldhdGIIRMD 280
Cdd:cd03084 85 SVKAVDILQRYFEALKKLFDVAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNF--------GNINPD 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 281 CSSESAMAGLLALRD--KFDLAFANDPDYDRHGIVTPKG-LMNPNHYLAVAINYLFQHrpqWGADVAVGKTLVSSAMIDR 357
Cdd:cd03084 157 PGSETNLKQLLAVVKaeKADFGVAFDGDADRLIVVDENGgFLDGDELLALLAVELFLT---FNPRGGVVKTVVSSGALDK 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 358 VVADLGRKLVEVPVGFKWFVDGLFDGSLGFGGEESAGASFLRFngqpwSTDKDGIIMCLLAAEITAVTGENPQHHYDDLA 437
Cdd:cd03084 234 VAKKLGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGVIFPEF-----HPGRDGISAALLLLEILANLGKSLSELFSELP 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 438 KRFgapsYNRIQAPathaqkaalsklspemvkastlggdpitarltaapgngasigglkvmtdnGWFAARPSGTEEAYKI 517
Cdd:cd03084 309 RYY----YIRLKVR--------------------------------------------------GWVLVRASGTEPAIRI 334
|
490 500
....*....|....*....|..
gi 515495496 518 YCESFLGaEHREKIEHEAVEIV 539
Cdd:cd03084 335 YAEADTQ-EDVEQIKKEARELV 355
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
40-539 |
8.39e-94 |
|
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: 294.07 E-value: 8.39e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 40 VKFGTSGHRGSAQRhSFNEAHILAIAQAIAEVRHQQGTTGP-CYVGKDTHALSEPAFISVLEVLTANGVDVIVQEnnGFT 118
Cdd:cd05800 1 IKFGTDGWRGIIAE-DFTFENVRRVAQAIADYLKEEGGGGRgVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSD--RPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 119 PTPAVSHAILCHNRRGGaqadgIVITPSHNPPEDGGIKYNPPNGGPADTNLTSVIEKRANELLAQQLKGVQRqsldkawn 198
Cdd:cd05800 78 PTPAVSWAVKKLGAAGG-----VMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAE-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 199 sGHLHAKDLVQPYVEGLVDVVDMPAIQRAGLKLGVDPLGGSGIAYWQRVAEHYKLDLTLVNDSIDQTFrfmhldhDGIir 278
Cdd:cd05800 145 -GLIETIDPKPDYLEALRSLVDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLF-------GGI-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 279 MDCSSESAMAGLLAL--RDKFDLAFANDPDYDRHGIVTPKG-LMNPNHYLAVAINYLFQHRpQWGADVAvgKTLVSSAMI 355
Cdd:cd05800 215 PPEPIEKNLGELAEAvkEGGADLGLATDGDADRIGAVDEKGnFLDPNQILALLLDYLLENK-GLRGPVV--KTVSTTHLI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 356 DRVVADLGRKLVEVPVGFKWFVDGLFDGSLGFGGEESAGASFLRFngQPwstDKDGIIMCLLAAEITAVTGENPQHHYDD 435
Cdd:cd05800 292 DRIAEKHGLPVYETPVGFKYIAEKMLEEDVLIGGEESGGLGIRGH--IP---ERDGILAGLLLLEAVAKTGKPLSELVAE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 436 LAKRFGAPSYNRIQAPATHAQKAA-LSKLSPEmvKASTLGGDPITARLTaapgngasIGGLKVMTDNG-WFAARPSGTEE 513
Cdd:cd05800 367 LEEEYGPSYYDRIDLRLTPAQKEAiLEKLKNE--PPLSIAGGKVDEVNT--------IDGVKLVLEDGsWLLIRPSGTEP 436
|
490 500
....*....|....*....|....*.
gi 515495496 514 AYKIYCESFlGAEHREKIEHEAVEIV 539
Cdd:cd05800 437 LLRIYAEAP-SPEKVEALLDAGKKLA 461
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
42-543 |
9.15e-68 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 225.85 E-value: 9.15e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 42 FGTSGHRGSAQRHsFNEAHILAIAQAIAEVRHQQGTtGPCYVGKDTHALSEPAFISVLEVLTANGVDVIvqeNNGFTPTP 121
Cdd:COG1109 7 FGTDGIRGIVGEE-LTPEFVLKLGRAFGTYLKEKGG-PKVVVGRDTRLSSPMLARALAAGLASAGIDVY---DLGLVPTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 122 AVSHAIlchnRRGGAQAdGIVITPSHNPPEDGGIKYNPPNGGPADTNLTSVIEKRANELLAQQLKGVQRqsldkawnsGH 201
Cdd:COG1109 82 ALAFAV----RHLGADG-GIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEI---------GK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 202 LH-AKDLVQPYVEGLVDVVDmPAIQRAGLKLGVDPLGGSGIAYWQRVAEHYKLDLTLVNDSIDQTFrfmhldhdgiIRMD 280
Cdd:COG1109 148 VTrIEDVLEAYIEALKSLVD-EALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNF----------PNHN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 281 CSSES-AMAGL--LALRDKFDLAFANDPDYDRHGIVTPKG-LMNPNHYLAVAINYLFQHRPqwGADVAvgKTLVSSAMID 356
Cdd:COG1109 217 PNPEPeNLEDLieAVKETGADLGIAFDGDADRLGVVDEKGrFLDGDQLLALLARYLLEKGP--GGTVV--VTVMSSLALE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 357 RVVADLGRKLVEVPVGFKWFVDGLFDGSLGFGGEESAGASFLRFNgqpwsTDKDGIIMCLLAAEITAVTGENPqhhyDDL 436
Cdd:COG1109 293 DIAEKHGGEVVRTKVGFKYIKEKMRETGAVLGGEESGGIIFPDFV-----PTDDGILAALLLLELLAKQGKSL----SEL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 437 AKRFGAPSYNRIQAPAthAQKAALSKLSPEMVKASTLGGDPITarltaapgngasIGGLKV-MTDNGWFAARPSGTEEAY 515
Cdd:COG1109 364 LAELPRYPQPEINVRV--PDEEKIGAVMEKLREAVEDKEELDT------------IDGVKVdLEDGGWVLVRPSGTEPLL 429
|
490 500
....*....|....*....|....*...
gi 515495496 516 KIYCESFlGAEHREKIEHEAVEIVSEVL 543
Cdd:COG1109 430 RVYAEAK-DEEEAEELLAELAELVEEAL 456
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
40-179 |
2.58e-42 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 148.14 E-value: 2.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 40 VKFGTSGHRGSAQRHSFNEAHILAIAQAIAEVRHQQGTTGPCYVGKDTHALSEPAFISVLEVLTANGVDVIVqenNGFTP 119
Cdd:pfam02878 2 QLFGTSGIRGKVGVGELTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVIL---LGLLP 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 120 TPAVSHAIlchnRRGGAqADGIVITPSHNPPEDGGIKYNPPNGGPADTNLTSVIEKRANE 179
Cdd:pfam02878 79 TPAVSFAT----RKLKA-DGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
320-440 |
1.50e-39 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 139.89 E-value: 1.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 320 NPNHYLAVAINYLFQHRpQWGADVAVGKTLVSSAMIDRVVADLGRKLVEVPVGFKWFVDGLFDGSLGFGGEESAGASFLR 399
Cdd:pfam02880 1 DGDQILALLAKYLLEQG-KLPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 515495496 400 FNgqpwsTDKDGIIMCLLAAEITAVTGENPQHHYDDLAKRF 440
Cdd:pfam02880 80 HA-----TTKDGILAALLVLEILARTGKSLSELLEELPEKY 115
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
42-544 |
4.80e-35 |
|
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: 136.87 E-value: 4.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 42 FGTSGHRGSAQRhSFNEAHILAIAQAIAE-VRHqqgttGPCYVGKDTHAlSEPAFIS-VLEVLTANGVDVIvqeNNGFTP 119
Cdd:TIGR03990 4 FGTSGIRGIVGE-ELTPELALKVGKAFGTyLRG-----GKVVVGRDTRT-SGPMLENaVIAGLLSTGCDVV---DLGIAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 120 TPAVSHAIlchnRRGGAQAdGIVITPSHNPPEDGGIKynppnggpadtnltsVIEKRANELLAQQLKGVQRQSLDK---- 195
Cdd:TIGR03990 74 TPTLQYAV----RELGADG-GIMITASHNPPEYNGIK---------------LLNSDGTELSREQEEEIEEIAESGdfer 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 196 -AWNS-GHLH-AKDLVQPYVEGLVDVVDMPAIQRAGLKLGVDPLGGSGIAYWQRVAEHYKLDLTLVNDSIDQTFrfmhld 272
Cdd:TIGR03990 134 aDWDEiGTVTsDEDAIDDYIEAILDKVDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTF------ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 273 hdgIIRMdcsSESAMAGLLALRD-----KFDLAFANDPDYDRHGIVTPKG-LMNPNHYLAVAINYLFQHRpqwGADVAVg 346
Cdd:TIGR03990 208 ---PGRN---PEPTPENLKDLSAlvkatGADLGIAHDGDADRLVFIDEKGrFIGGDYTLALFAKYLLEHG---GGKVVT- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 347 kTLVSSAMIDRVVADLGRKLVEVPVGFKWFVDGLFDGSLGFGGEESAGASFLRFngQPWstdKDGIIMCLLAAEITAVTG 426
Cdd:TIGR03990 278 -NVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGAVFGGEGNGGWIFPDH--HYC---RDGLMAAALFLELLAEEG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 427 ENPqhhyDDLAKRFgaPSYN--RIQAPATHAQKAALSklspEMVKASTLGGDPITarltaapgngasIGGLKVMTDNGWF 504
Cdd:TIGR03990 352 KPL----SELLAEL--PKYPmsKEKVELPDEDKEEVM----EAVEEEFADAEIDT------------IDGVRIDFEDGWV 409
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 515495496 505 AARPSGTEEAYKIYCESflgaehreKIEHEAVEIVSEVLA 544
Cdd:TIGR03990 410 LVRPSGTEPIVRIYAEA--------KTEERAEELLEEGRS 441
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
42-539 |
2.65e-30 |
|
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: 123.06 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 42 FGTSGHRGSaqrhsFNEAH----ILAIAQAIAEVRhqqgTTGPCYVGKDTHAlSEPAFISVLE-VLTANGVDVIVQennG 116
Cdd:cd03087 2 FGTSGIRGV-----VGEELtpelALKVGKALGTYL----GGGTVVVGRDTRT-SGPMLKNAVIaGLLSAGCDVIDI---G 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 117 FTPTPAVSHAILCHNRRGgaqadgIVITPSHNPPEDGGIKYNPPNGGPADTNLTSVIEKRaneLLAQQLKGVqrqsldkA 196
Cdd:cd03087 69 IVPTPALQYAVRKLGDAG------VMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEI---IFSERFRRV-------A 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 197 WNS-GHLHAKD-LVQPYVEGLVDVVDMPAiqRAGLKLGVDPLGGSGIAYWQRVAEHYKLDLTLVNDSIDQTFrfmhldhd 274
Cdd:cd03087 133 WDEvGSVRREDsAIDEYIEAILDKVDIDG--GKGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFF-------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 275 gIIRMdcsSESAMAGLLALRD-----KFDLAFANDPDYDRHGIVTPKG-LMNPNHYLAVAINYLFQHRPqwgaDVAVgkT 348
Cdd:cd03087 203 -PGRP---PEPTPENLSELMElvratGADLGIAHDGDADRAVFVDEKGrFIDGDKLLALLAKYLLEEGG----GKVV--T 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 349 LVSSAM-IDRVVADLGRKLVEVPVGfKWFVDGLFDGSLG-FGGEESAGASFLRFngQPWstdKDGIIMCLLAAEItaVTG 426
Cdd:cd03087 273 PVDASMlVEDVVEEAGGEVIRTPVG-DVHVAEEMIENGAvFGGEPNGGWIFPDH--QLC---RDGIMTAALLLEL--LAE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 427 ENPqhhyddLAKRFGA-PSYN--RIQAPATHAQKAALsklsPEMVKA--STLGGDPITarltaapgngasIGGLKVMTDN 501
Cdd:cd03087 345 EKP------LSELLDElPKYPllREKVECPDEKKEEV----MEAVEEelSDADEDVDT------------IDGVRIEYED 402
|
490 500 510
....*....|....*....|....*....|....*...
gi 515495496 502 GWFAARPSGTEEAYKIYCESfLGAEHREKIEHEAVEIV 539
Cdd:cd03087 403 GWVLIRPSGTEPKIRITAEA-KTEERAKELLEEGRSKV 439
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
41-427 |
2.45e-23 |
|
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: 103.84 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 41 KFGTSGHRGS---AQRHSFNEAHILAIAQAIAEVRHQQGTTGpcyVGKDTHALSEPAFISVLEVLTANGVDVIVQENNGF 117
Cdd:cd03085 12 KPGTSGLRKKvkvFQQPNYLENFVQSIFNALPPEKLKGATLV---VGGDGRYYNKEAIQIIIKIAAANGVGKVVVGQNGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 118 TPTPAVSHAIlchnRRGGAQAdGIVITPSHNP--PE-DGGIKYNPPNGGPADTNLTSVIEKRANELlaQQLKGVQRQSLD 194
Cdd:cd03085 89 LSTPAVSAVI----RKRKATG-GIILTASHNPggPEgDFGIKYNTSNGGPAPESVTDKIYEITKKI--TEYKIADDPDVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 195 ------KAWNSGHLHAK--DLVQPYVEGLVDVVDMPAI----QRAGLKLGVDPLGGSGIAYWQRV-AEHYKLDL-TLVND 260
Cdd:cd03085 162 lskigvTKFGGKPFTVEviDSVEDYVELMKEIFDFDAIkkllSRKGFKVRFDAMHGVTGPYAKKIfVEELGAPEsSVVNC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 261 SIDQTFRFMHLD------HDGIIRMDcssesamagllalRDKFDLAFANDPDYDRHGIVTPKGLMNPNHYLAV------A 328
Cdd:cd03085 242 TPLPDFGGGHPDpnltyaKDLVELMK-------------SGEPDFGAASDGDGDRNMILGKGFFVTPSDSVAViaanakL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 329 INYLFQHRPQwgadvAVGKTLVSSAMIDRVVADLGRKLVEVPVGFKWFVDgLFD-GSLGFGGEES--AGASFLRfngqpw 405
Cdd:cd03085 309 IPYFYKGGLK-----GVARSMPTSGALDRVAKKLGIPLFETPTGWKFFGN-LMDaGKLSLCGEESfgTGSDHIR------ 376
|
410 420
....*....|....*....|....
gi 515495496 406 stDKDGI--IMCLLAaeITAVTGE 427
Cdd:cd03085 377 --EKDGLwaVLAWLS--ILAHRNV 396
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
41-412 |
1.03e-21 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 98.96 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 41 KFGTSGHRGSAQrhSFNEAHILA-IAQAIAEVRHQQGTTGPCYV-GKDTHALSEPAFISVLEVLTANGVDVIVQENNGFT 118
Cdd:PLN02307 24 KPGTSGLRKKVK--VFMQENYLAnFVQALFNALPAEKVKGATLVlGGDGRYFNKEAIQIIIKIAAANGVRRVWVGQNGLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 119 PTPAVSHAIlchNRRGGAQADG-IVITPSHNP--P-EDGGIKYNPPNGGPADTNLTSVI---EKRANEL-LAQQLKGVQR 190
Cdd:PLN02307 102 STPAVSAVI---RERDGSKANGgFILTASHNPggPeEDFGIKYNYESGQPAPESITDKIygnTLTIKEYkMAEDIPDVDL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 191 QSLD----KAWNSGHLHAKDLVQPYVEGLVDVVDMPAI----QRAGLKLGVDPLGGSGIAYWQRV-AEHYKLDL-TLVND 260
Cdd:PLN02307 179 SAVGvtkfGGPEDFDVEVIDPVEDYVKLMKSIFDFELIkkllSRPDFTFCFDAMHGVTGAYAKRIfVEELGAPEsSLLNC 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 261 SIDQTFRFMHLD------HDGIIRMDCSSESAMAgllalrDKFDLAFANDPDYDRHGIVTPKGLMNPNHYLAV------- 327
Cdd:PLN02307 259 VPKEDFGGGHPDpnltyaKELVKRMGLGKTSYGD------EPPEFGAASDGDGDRNMILGKRFFVTPSDSVAIiaanaqe 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 328 AINYlFQHRPQwgadvAVGKTLVSSAMIDRVVADLGRKLVEVPVGFKWFvDGLFD-GSLGFGGEES--AGASFLRfngqp 404
Cdd:PLN02307 333 AIPY-FSGGLK-----GVARSMPTSAALDVVAKKLNLPFFEVPTGWKFF-GNLMDaGKLSICGEESfgTGSDHIR----- 400
|
....*...
gi 515495496 405 wstDKDGI 412
Cdd:PLN02307 401 ---EKDGI 405
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
48-512 |
4.43e-20 |
|
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: 92.96 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 48 RGSAQRhSFNEAHILAIAQAIAE--VRHQQGTtgpCYVGKDTHaLSEPAFISVL-EVLTANGVDVIvqeNNGFTPTPAVS 124
Cdd:cd03089 8 RGIAGE-ELTEEIAYAIGRAFGSwlLEKGAKK---VVVGRDGR-LSSPELAAALiEGLLAAGCDVI---DIGLVPTPVLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 125 HAIlCHNRRGGaqadGIVITPSHNPPEDGGIKYNPPNGGPADTNLTSvIEKRANELLAQQLKGvqrqsldkawnSGHLHA 204
Cdd:cd03089 80 FAT-FHLDADG----GVMITASHNPPEYNGFKIVIGGGPLSGEDIQA-LRERAEKGDFAAATG-----------RGSVEK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 205 KDLVQPYVEGLVDVVDmpaIQRAGLKLGVDPLGGSGIAYWQRVAEHYKLDLTLVNDSIDQTFrfmhLDHDGiirmDCSSE 284
Cdd:cd03089 143 VDILPDYIDRLLSDIK---LGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTF----PNHHP----DPTDP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 285 SAMAGLLA--LRDKFDLAFANDPDYDRHGIVTPKG-LMNPNHYLAVAINYLFQHRPqwGADVaVGKTLVSSAMIDrVVAD 361
Cdd:cd03089 212 ENLEDLIAavKENGADLGIAFDGDGDRLGVVDEKGeIIWGDRLLALFARDILKRNP--GATI-VYDVKCSRNLYD-FIEE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 362 LGRKLVEVPVGFKWFVDGLFD-GSLgFGGEESAGASFL-RFNGqpwsTDkDGIIMCLLAAEITAVTGENPQHHYDDLAKR 439
Cdd:cd03089 288 AGGKPIMWKTGHSFIKAKMKEtGAL-LAGEMSGHIFFKdRWYG----FD-DGIYAALRLLELLSKSGKTLSELLADLPKY 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515495496 440 FGAPSynrIQAPATHAQKAALSklspEMVKA--STLGGDPITarltaapgngasIGGLKVMTDNGWFAARPSGTE 512
Cdd:cd03089 362 FSTPE---IRIPVTEEDKFAVI----ERLKEhfEFPGAEIID------------IDGVRVDFEDGWGLVRASNTE 417
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
42-413 |
6.65e-19 |
|
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: 89.08 E-value: 6.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 42 FGTSGHRGSAQRhSFNEAHILAIAQAIAEVRHQQGTTGPCYVGKDTHaLSEPAFISVLEV-LTANGVDVIVQennGFTPT 120
Cdd:cd05802 2 FGTDGIRGVANE-PLTPELALKLGRAAGKVLGKGGGRPKVLIGKDTR-ISGYMLESALAAgLTSAGVDVLLL---GVIPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 121 PAVSHAIlchnRRGGAQAdGIVITPSHNPPEDGGIKYNPPNGGPADTNLTSVIEKRANELLAQQLKGVqrqSLDKAWNsg 200
Cdd:cd05802 77 PAVAYLT----RKLRADA-GVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKELELPPTGE---KIGRVYR-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 201 hlhAKDLVQPYVEGLVDVVdmPAIQRAGLKLGVDplGGSGIAYwqRVAEH--YKL--DLTLVNDsidqtfrfmhlDHDGI 276
Cdd:cd05802 147 ---IDDARGRYIEFLKSTF--PKDLLSGLKIVLD--CANGAAY--KVAPEvfRELgaEVIVINN-----------APDGL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 277 -IRMDCSS---ESAMAglLALRDKFDLAFANDPDYDRHGIVTPKG-LMNPNHYLAV-AINYLFQHRPQwgadvavGKTLV 350
Cdd:cd05802 207 nINVNCGSthpESLQK--AVLENGADLGIAFDGDADRVIAVDEKGnIVDGDQILAIcARDLKERGRLK-------GNTVV 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515495496 351 SSAM----IDRVVADLGRKLVEVPVGFKWFVDGLFDGSLGFGGEESAGASFLRFNgqpwsTDKDGII 413
Cdd:cd05802 278 GTVMsnlgLEKALKELGIKLVRTKVGDRYVLEEMLKHGANLGGEQSGHIIFLDHS-----TTGDGLL 339
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
210-317 |
8.64e-18 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 78.87 E-value: 8.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 210 PYVEGLVDVVDMPAIQRAGLKLGVDPLGGSGIAYWQRVAEHYKLDLTLVNDSIDQTFRFmhldhdGIIRMDCSSESAMAG 289
Cdd:pfam02879 1 AYIDHLLELVDSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPT------RAPNPEEPEALALLI 74
|
90 100
....*....|....*....|....*...
gi 515495496 290 LLALRDKFDLAFANDPDYDRHGIVTPKG 317
Cdd:pfam02879 75 ELVKSVGADLGIATDGDADRLGVVDERG 102
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
45-521 |
8.24e-16 |
|
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: 79.66 E-value: 8.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 45 SGHRGSAQRhSFNEAHILAIAQAIAEVRHQQGTTGPCYVGKDTHALSEPAFISVLEVLTANGVDVIvqeNNGFTPTPAVS 124
Cdd:cd05803 5 SGIRGIVGE-GLTPEVITRYVAAFATWQPERTKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVI---DLGIAPTPTVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 125 HAIlchnRRGGAqADGIVITPSHNPPEDGGIKYNPPNG---GPAD-TNLTSVIEKRANELLAQQLKGVQRQSLDkaWNSG 200
Cdd:cd05803 81 VLV----RQSQA-SGGIIITASHNPPQWNGLKFIGPDGeflTPDEgEEVLSCAEAGSAQKAGYDQLGEVTFSED--AIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 201 HLHAkdlvqpyVEGLVDvVDMPAIQRAGLKLGVDPLGGSGIAYWQRVAEHYKLDLTLVNDSIDQTFRfmhldhdgiiRMD 280
Cdd:cd05803 154 HIDK-------VLALVD-VDVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLFP----------HTP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 281 CSSESAMAGLLAL--RDKFDLAFANDPDYDRHGIVTPKG-LMNPNHYLAVAINYLFQHRPQWGADVavgKTLVSSAMIDR 357
Cdd:cd05803 216 EPLPENLTQLCAAvkESGADVGFAVDPDADRLALVDEDGrPIGEEYTLALAVDYVLKYGGRKGPVV---VNLSTSRALED 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 358 VVADLGRKLVEVPVGFKWFVDGLFDGSLGFGGEesaGasflrfNGQPWSTD----KD---GIIMCL--LAAE---ITAVT 425
Cdd:cd05803 293 IARKHGVPVFRSAVGEANVVEKMKEVDAVIGGE---G------NGGVILPDvhygRDslvGIALVLqlLAASgkpLSEIV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 426 GENPQHHYddlakrfgapsynriqapatHAQKAALSKLSPEMVKaSTLGGDPITARLTaapgngaSIGGLKVMTDNGWFA 505
Cdd:cd05803 364 DELPQYYI--------------------SKTKVTIAGEALERLL-KKLEAYFKDAEAS-------TLDGLRLDSEDSWVH 415
|
490
....*....|....*.
gi 515495496 506 ARPSGTEEAYKIYCES 521
Cdd:cd05803 416 VRPSNTEPIVRIIAEA 431
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
40-543 |
3.12e-08 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 56.23 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 40 VKFGTSGHRGsAQRHSFNEAHILAIaqaiaevrhQQGTTGPCYVGKDTHALSEPAFISVL-----------EVLTANgvd 108
Cdd:PTZ00150 45 MEFGTAGLRG-KMGAGFNCMNDLTV---------QQTAQGLCAYVIETFGQALKSRGVVIgydgryhsrrfAEITAS--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 109 viVQENNGF--------TPTPAVSHAILCHNrrggaQADGIVITPSHNPPEDGGIKYNPPNGG----PADTNLTSVIEkr 176
Cdd:PTZ00150 112 --VFLSKGFkvylfgqtVPTPFVPYAVRKLK-----CLAGVMVTASHNPKEDNGYKVYWSNGAqiipPHDKNISAKIL-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 177 ANellaqqlkgvqRQSLDKAWNsgHLHAKDLVQPYVEgLVD--VVDMPA------IQRAGLKLGVDPLGGSGIAYWQRVA 248
Cdd:PTZ00150 183 SN-----------LEPWSSSWE--YLTETLVEDPLAE-VSDayFATLKSeynpacCDRSKVKIVYTAMHGVGTRFVQKAL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 249 EHYKL-DLTLVN-----DSIDQTFRFMHLDhDGIIRMDCSSEsamaglLALRDKFDLAFANDPDYDRHGIVTPKG----L 318
Cdd:PTZ00150 249 HTVGLpNLLSVAqqaepDPEFPTVTFPNPE-EGKGALKLSME------TAEAHGSTVVLANDPDADRLAVAEKLNngwkI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 319 MNPNHyLAVAINY--LFQHRPQWGA--DVAVGKTLVSSAMIDRVVADLGRKLVEVPVGFKWFvdglfdGSLGFGGEESAG 394
Cdd:PTZ00150 322 FTGNE-LGALLAWwaMKRYRRQGIDksKCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWI------GNKAIELNAENG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 395 ASFLrFN-----GQPWST---DKDGIIMCLLAAEITAVTGENP---QHHYDDLAKRFGA-PSYNRIqapATHAQKAALSK 462
Cdd:PTZ00150 395 LTTL-FAyeeaiGFMLGTrvrDKDGVTAAAVVAEMALYLYERGktlVEHLESLYKQYGYhFTNNSY---YICYDPSRIVS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 463 LSPEMVKA----STLGGDPITARL-------TAAPGNGASIGG------LKVMTDNGWFAA-RPSGTEEAYKIYCEsfLG 524
Cdd:PTZ00150 471 IFNDIRNNgsypTKLGGYPVTRIRdlttgydTATPDGKPLLPVsastqmITFYFENGAIITiRGSGTEPKLKWYAE--LS 548
|
570
....*....|....*....
gi 515495496 525 AEHREKIEHEAVEIVSEVL 543
Cdd:PTZ00150 549 GTKDEAVEKELAALVDEVV 567
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
42-196 |
5.07e-08 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 55.53 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 42 FGTSGHRGSAQRHSFNEAHILAIAQAIAEVRHQQGTtgpCYV--GKDTHaLSEPAFISVLEV-LTANGVDVivqennGFT 118
Cdd:PRK10887 4 FGTDGIRGKVGQAPITPDFVLKLGWAAGKVLARQGR---PKVliGKDTR-ISGYMLESALEAgLAAAGVDV------LLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 119 ---PTPAVshAILCHNRRggAQAdGIVITPSHNPPEDGGIKYNPPNGgpadTNLTSVIEKRANELLAQQLKGVQRQSLDK 195
Cdd:PRK10887 74 gpmPTPAV--AYLTRTLR--AEA-GIVISASHNPYYDNGIKFFSADG----TKLPDEVELAIEAELDKPLTCVESAELGK 144
|
.
gi 515495496 196 A 196
Cdd:PRK10887 145 A 145
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
41-162 |
2.19e-07 |
|
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: 53.36 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 41 KFGTSGHRG--SAQRHSFNEAHILAIAQAIAevRHQQGTTgpCYVGKDTHAlSEPAF-ISVLEVLTANGVDVIvqeNNGF 117
Cdd:cd03088 1 KFGTSGLRGlvTDLTDEVCYAYTRAFLQHLE--SKFPGDT--VAVGRDLRP-SSPRIaAACAAALRDAGFRVV---DCGA 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 515495496 118 TPTPAVSHAILchnrrgGAQADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:cd03088 73 VPTPALALYAM------KRGAPAIMVTGSHIPADRNGLKFYRPDG 111
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
135-163 |
1.57e-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: 44.51 E-value: 1.57e-04
10 20
....*....|....*....|....*....
gi 515495496 135 GAQADGIVITPSHNPPEDGGIKYNPPNGG 163
Cdd:cd03086 33 GGKTIGVMITASHNPVEDNGVKIVDPDGE 61
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
140-178 |
1.73e-04 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 44.26 E-value: 1.73e-04
10 20 30
....*....|....*....|....*....|....*....
gi 515495496 140 GIVITPSHNPPEDGGIKYNPPNGGPADTNLTSVIEKRAN 178
Cdd:PTZ00302 78 GVMITASHNPIQDNGVKIIDPDGGMLEESWEKICTDFAN 116
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
47-209 |
8.23e-04 |
|
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies protein, acts as a transcriptional repressor that regulates the expression of proteins that are part of the phosphotransferase system for sugar uptake. It regulates the expression of malT. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466924 [Multi-domain] Cd Length: 322 Bit Score: 41.53 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 47 HRGSAQRHSFNEAHILAIAQAIAEvrhqqgTTG-PCYVGKDTHALSEPAFISVLEVLTANGVDVIVQENNGFTptpAVSH 125
Cdd:cd24074 77 ESGIVHRLPFYDIKNLPLGEALEQ------HTGlPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAG---VITD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 126 AILCHNRRGGAqadgivITPSHNPPEDGGIKYNPPNGGPADTNLT-SVIEKRANELLAQ------QLKGVQRQSLDKAWN 198
Cdd:cd24074 148 GQLLHAGSSRL------GELGHTQIDPYGKRCYCGNHGCLETVASiPAILEQANQLLEQspdsmlHGQPISIESLCQAAL 221
|
170
....*....|.
gi 515495496 199 SGHLHAKDLVQ 209
Cdd:cd24074 222 AGDPLAQDIII 232
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
137-219 |
2.12e-03 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 40.78 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495496 137 QADGIVITPSHNPPEDGGIKYNPPNGGPADTNLTSVIEKRANELLAQQLKGVQRQSLDKAwNSGHLHAKDLVQPYV---- 212
Cdd:PLN02895 58 AATGLMITASHNPVSDNGVKIVDPSGGMLPQAWEPFADALANAPDPDALVQLIREFVKKE-NIPAVGGNPPAEVLLgrdt 136
|
90
....*....|.
gi 515495496 213 ----EGLVDVV 219
Cdd:PLN02895 137 rpsgPALLAAA 147
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
489-542 |
2.26e-03 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 36.86 E-value: 2.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 515495496 489 GASIGGLKVMTDNGW-FAARPSGTEEAYKIYCEsflgAEHREKIEHEAVEIVSEV 542
Cdd:pfam00408 20 KVFADAEKILGEDGRrLDVRPSGTEPVLRVMVE----GDSDEELARLADEIADLL 70
|
|
| |
