|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
3-544 |
0e+00 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 1045.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 3 NHSRAGQPAQQSDLINVAQLTAQYYVLKPVVGNAEHAVKFGTSGHRGSAARHSFNEPHILAIAQAIAEERAKNGVTGPCY 82
Cdd:PRK07564 1 IHPRAGQPAQPSDLINVPRLVSAYYTLKPDPTNPFQDVKFGTSGHRGSSLQPSFNENHILAIFQAICEYRGKQGITGPLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 83 VGKDTHALSEPAFISVLEVLAANGVDVIVQENNGFTPTPAVSNAILVHNKKGGALADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:PRK07564 81 VGGDTHALSEPAIQSALEVLAANGVGVVIVGRGGYTPTPAVSHAILKYNGRGGGLADGIVITPSHNPPEDGGIKYNPPNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 163 GPADTNVTKVVEDRANALLADGLKGVKRISLDAAMASGHVKEQDLVQPFVEGLADIVDMAAIQKAGLKLGVDPLGGSGIE 242
Cdd:PRK07564 161 GPADTDVTDAIEARANELLAYGLKGVKRIPLDRALASMTVEVIDPVADYVEDLENVFDFDAIRKAGLRLGVDPLGGATGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 243 YWKRIAEHYKLDLTIVNDHVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTPAGLMNPN 322
Cdd:PRK07564 241 YWKAIAERYGLDLTVVNAPVDPTFNFMPLDDDGKIRMDCSSPYAMAGLLALKDAFDLAFANDPDGDRHGIVTPGGLMNPN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 323 HYLAVAINYLFQHRPQWGKEVAVGKTLVSSAMIDRVVDALGRKLVEVPVGFKWFVDGLHDGSFGFGGEESAGASFLRFDG 402
Cdd:PRK07564 321 HYLAVAIAYLFHHRPGWRAGAGVGKTLVSSAMIDRVAAKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESAGASFLRRDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 403 TPWSTDKDGIIMCLLAAEITAVTGKNPQEHYNDLAARFGAPSYNRIQASATSAQKAALSKLSPEMVSANTLAGDPITARL 482
Cdd:PRK07564 401 SVWTTDKDGLIAVLLAAEILAVTGKSPSEIYRELWARFGRPYYSRHDAPATPEQKAALRKLSPELVGATELAGDPIDASL 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504695918 483 TAAPGNGASIGGLKVMTDNGWFAARPSGTEDAYKIYCESFLGAEHRQQIEKEAVEIVSEVLK 544
Cdd:PRK07564 481 TEAPGNGAAIGGLKVVTENGWFAARPSGTETTYKIYAESFEGDEHLHQIQKEAQEIVADLIA 542
|
|
| pgm |
TIGR01132 |
phosphoglucomutase, alpha-D-glucose phosphate-specific; This enzyme interconverts ... |
2-544 |
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: 1042.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 2 ANHSRAGQPAQQSDLINVAQLTAQYYVLKPVVGNAEHAVKFGTSGHRGSAARHSFNEPHILAIAQAIAEERAKNGVTGPC 81
Cdd:TIGR01132 1 AIHPRAGQPAQQEDLINVAQLVAQYYVLQPEAGNAAHAVKFGTSGHRGSALRGTFNEPHILAIAQAIAEYRAAQGITGPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 82 YVGKDTHALSEPAFISVLEVLAANGVDVIVQENNGFTPTPAVSNAILVHNKKGGALADGIVITPSHNPPEDGGIKYNPPN 161
Cdd:TIGR01132 81 YIGKDTHALSEPAFISVLEVLAANGVEVIVQENNGFTPTPAVSHAILTHNKKGEPLADGIVITPSHNPPEDGGIKYNPPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 162 GGPADTNVTKVVEDRANALLADGLKGVKRISLDAAMASGHVKEQDLVQPFVEGLADIVDMAAIQKAGLKLGVDPLGGSGI 241
Cdd:TIGR01132 161 GGPADTEATQAIEDRANALLANGLKGVKRLPLAQALASGTVKAHDLVQPYVDGLADIVDMAAIQKAGLRLGVDPLGGSGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 242 EYWKRIAEHYKLDLTIVNDHVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTPAGLMNP 321
Cdd:TIGR01132 241 DYWKRIAEKYNLNLTLVNPQVDPTFRFMTLDKDGKIRMDCSSPYAMAGLLALRDKYDLAFGNDPDYDRHGIVTPAGLMNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 322 NHYLAVAINYLFQHRPQWGKEVAVGKTLVSSAMIDRVVDALGRKLVEVPVGFKWFVDGLHDGSFGFGGEESAGASFLRFD 401
Cdd:TIGR01132 321 NHYLAVAINYLFQHRPQWGGDVAVGKTLVSSAMIDRVVADLGRQLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 402 GTPWSTDKDGIIMCLLAAEITAVTGKNPQEHYNDLAARFGAPSYNRIQASATSAQKAALSKLSPEMVSANTLAGDPITAR 481
Cdd:TIGR01132 401 GTPWSTDKDGIIMCLLAAEITAVTGKNPQQHYNELAAKFGAPSYNRIQAPATSAQKARLKKLSPEMVSATTLAGDPITAR 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504695918 482 LTAAPGNGASIGGLKVMTDNGWFAARPSGTEDAYKIYCESFLGAEHRQQIEKEAVEIVSEVLK 544
Cdd:TIGR01132 481 LTAAPGNGAAIGGLKVTTDNGWFAARPSGTEDVYKIYCESFKGEEHLKQIEKEAVEIVSEVLK 543
|
|
| 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: 1036.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 20 AQLTAQYYVLKPVVGNAEHAVKFGTSGHRGSAARHSFNEPHILAIAQAIAEERAKNGVTGPCYVGKDTHALSEPAFISVL 99
Cdd:cd05801 1 PRLITAYYTLKPDPSNPAQRVAFGTSGHRGSSLKGSFNEAHILAISQAICDYRKSQGITGPLFLGKDTHALSEPAFISAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 100 EVLAANGVDVIVQENNGFTPTPAVSNAILVHNKKG-GALADGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRAN 178
Cdd:cd05801 81 EVLAANGVEVIIQQNDGYTPTPVISHAILTYNRGRtEGLADGIVITPSHNPPEDGGFKYNPPHGGPADTDITRWIEKRAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 179 ALLADGLKGVKRISLDAAMASGHVKEQDLVQPFVEGLADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIAEHYKLDLTIV 258
Cdd:cd05801 161 ALLANGLKGVKRIPLEAALASGYTHRHDFVTPYVADLGNVIDMDAIRKSGLRLGVDPLGGASVPYWQPIAEKYGLNLTVV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 259 NDHVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTP-AGLMNPNHYLAVAINYLFQHRP 337
Cdd:cd05801 241 NPKVDPTFRFMTLDHDGKIRMDCSSPYAMAGLLKLKDKFDLAFANDPDADRHGIVTPsAGLMNPNHYLSVAIDYLFTHRP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 338 QWGKEVAVGKTLVSSAMIDRVVDALGRKLVEVPVGFKWFVDGLHDGSFGFGGEESAGASFLRFDGTPWSTDKDGIIMCLL 417
Cdd:cd05801 321 LWNKSAGVGKTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDGLLDGSLGFGGEESAGASFLRRDGTVWTTDKDGIIMCLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 418 AAEITAVTGKNPQEHYNDLAARFGAPSYNRIQASATSAQKAALSKLSPEMVSANTLAGDPITARLTAAPGNGASIGGLKV 497
Cdd:cd05801 401 AAEILAVTGKDPGQLYQELTERFGEPYYARIDAPATPEQKARLKKLSPEQVTATELAGDPILAKLTRAPGNGASIGGLKV 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 504695918 498 MTDNGWFAARPSGTEDAYKIYCESFLGAEHRQQIEKEAVEIV 539
Cdd:cd05801 481 TTANGWFAARPSGTEDVYKIYAESFLSEEHLKKIQKEAQEIV 522
|
|
| Pgm |
COG0033 |
Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism]; |
3-544 |
0e+00 |
|
Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 439803 Cd Length: 544 Bit Score: 1017.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 3 NHSRAGQPAQQSDLINVAQLTAQYYVLKPVVGNAEHAVKFGTSGHRGSAARHSFNEPHILAIAQAIAEERAKNGVTGPCY 82
Cdd:COG0033 1 LHPRAGQPAPPSDLIDVPRLVSAYYTIKPDPTTPFQDVKFGTSGHRGSSLKGSFNEPHILAITQAIFDYRKAQGITGPLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 83 VGKDTHALSEPAFISVLEVLAANGVDVIVQENNGFTPTPAVSNAILVHNKKGGALADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:COG0033 81 LGGDTHALSEPAIQTALEVLAANGVGVVIVGQGGYTPTPAVSHAILKYNRGTSGAADGIVLTPSHNPPEDGGIKYNPPNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 163 GPADTNVTKVVEDRANALLADGLKGVKRISLDAAMASGHVKEQDLVQPFVEGLADIVDMAAIQKAGLKLGVDPLGGSGIE 242
Cdd:COG0033 161 GPADEDVTDAIEARANEILEYGLADVKRVPLDRAGTAMTVEVIDPVADYVELLESVFDFDAIRAAGFRIGFDPLGGATGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 243 YWKRIAEHYKLDLTIVNDHVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTP-AGLMNP 321
Cdd:COG0033 241 YWKAIAERYGLDLTVVNGVPDPDFRFMTLDWDGGIRMDPSSPYAMASLIAGKDAPDFAAANDGDGDRHGIVTPrGGLMNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 322 NHYLAVAINYLFQHRPQWGKEVAVGKTLVSSAMIDRVVDALGRKLVEVPVGFKWFVDGLHDGSFGFGGEESAGASFLRFD 401
Cdd:COG0033 321 NHYLAVAIAYLFTHRPGWAALAGVGKTMVTSSAIDRVAAALGRPLYEVPVGFKWFVNGLDAGSLGFGGEESAGASFLRRD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 402 GTPWSTDKDGIIMCLLAAEITAVTGKNPQEHYNDLAARFGAPSYNRIQASATSAQKAALSKLSPEMVSANTLAGDPITAR 481
Cdd:COG0033 401 GSVWTTDKDGLWAVLLAAEILAVTGKSPAEIYRELWARFGRPYYSRHDAEATDEQKARLAKLSGEQVGATTLAGEDIFAY 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504695918 482 LTAAPGNGASIGGLKVMTDNGWFAARPSGTEDAYKIYCESFLGAEHRQQIEKEAVEIVSEVLK 544
Cdd:COG0033 481 LDPAPGNGAAIGGLKVVTENGWFAARPSGTETTYKIYAESFEGDEHLHQIDAEAADLVDAALA 543
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
41-539 |
3.95e-105 |
|
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: 319.69 E-value: 3.95e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 41 KFGTSGHRGSAARHsFNEPHILAIAQAIAEErakngvtgpcyvgkdthalsepafisvlevlaangvdvivqenngftpt 120
Cdd:cd03084 1 IFGTSGVRGVVGDD-ITPETAVALGQAIGST------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 121 pavsnailvhnkkggalaDGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANALLADGLKGVKrisldaamASG 200
Cdd:cd03084 31 ------------------GGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYE--------LGG 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 201 HVKEQDLVQPFVEGLADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIAEHYKLDLTIVNDHVDQTFrfmhldkdGAIRMD 280
Cdd:cd03084 85 SVKAVDILQRYFEALKKLFDVAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNF--------GNINPD 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 281 CSSECAMAGLLALRD--KFDLAFANDPDYDRHGIVTP-AGLMNPNHYLAVAINYLFQHrpqWGKEVAVGKTLVSSAMIDR 357
Cdd:cd03084 157 PGSETNLKQLLAVVKaeKADFGVAFDGDADRLIVVDEnGGFLDGDELLALLAVELFLT---FNPRGGVVKTVVSSGALDK 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 358 VVDALGRKLVEVPVGFKWFVDGLHDGSFGFGGEESAGASFLRFdgtpwSTDKDGIIMCLLAAEITAVTGKNPQEHYNDLA 437
Cdd:cd03084 234 VAKKLGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGVIFPEF-----HPGRDGISAALLLLEILANLGKSLSELFSELP 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 438 ARFgapsYNRIQASatsaqkaalsklspemvsantlagdpitarltaapgngasigglkvmtdnGWFAARPSGTEDAYKI 517
Cdd:cd03084 309 RYY----YIRLKVR--------------------------------------------------GWVLVRASGTEPAIRI 334
|
490 500
....*....|....*....|..
gi 504695918 518 YCESFLGaEHRQQIEKEAVEIV 539
Cdd:cd03084 335 YAEADTQ-EDVEQIKKEARELV 355
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
40-539 |
2.57e-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: 295.23 E-value: 2.57e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 40 VKFGTSGHRGSAARhSFNEPHILAIAQAIAEERAKNGVTGP-CYVGKDTHALSEPAFISVLEVLAANGVDVIVQEnnGFT 118
Cdd:cd05800 1 IKFGTDGWRGIIAE-DFTFENVRRVAQAIADYLKEEGGGGRgVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSD--RPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 119 PTPAVSNAILVHNkkggaLADGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANALLADGLKGVKRisldaama 198
Cdd:cd05800 78 PTPAVSWAVKKLG-----AAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAE-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 199 sGHVKEQDLVQPFVEGLADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIAEHYKLDLTIVNDHVDQTFrfmhldkdGAIR 278
Cdd:cd05800 145 -GLIETIDPKPDYLEALRSLVDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLF--------GGIP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 279 MDCSSEcAMAGLLAL--RDKFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRpqwGKEVAVGKTLVSSAMI 355
Cdd:cd05800 216 PEPIEK-NLGELAEAvkEGGADLGLATDGDADRIGAVDEKGnFLDPNQILALLLDYLLENK---GLRGPVVKTVSTTHLI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 356 DRVVDALGRKLVEVPVGFKWFVDGLHDGSFGFGGEESAGASFLRFdgTPwstDKDGIIMCLLAAEITAVTGKNPQEHYND 435
Cdd:cd05800 292 DRIAEKHGLPVYETPVGFKYIAEKMLEEDVLIGGEESGGLGIRGH--IP---ERDGILAGLLLLEAVAKTGKPLSELVAE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 436 LAARFGAPSYNRIQASATSAQKAA-LSKLSPEmvSANTLAGDPITARLTaapgngasIGGLKVMTDNG-WFAARPSGTED 513
Cdd:cd05800 367 LEEEYGPSYYDRIDLRLTPAQKEAiLEKLKNE--PPLSIAGGKVDEVNT--------IDGVKLVLEDGsWLLIRPSGTEP 436
|
490 500
....*....|....*....|....*.
gi 504695918 514 AYKIYCESFlGAEHRQQIEKEAVEIV 539
Cdd:cd05800 437 LLRIYAEAP-SPEKVEALLDAGKKLA 461
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
42-543 |
3.53e-66 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 221.61 E-value: 3.53e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 42 FGTSGHRGSAARHsFNEPHILAIAQAIAE---ERAKNGVTgpcyVGKDTHALSEPAFISVLEVLAANGVDVIvqeNNGFT 118
Cdd:COG1109 7 FGTDGIRGIVGEE-LTPEFVLKLGRAFGTylkEKGGPKVV----VGRDTRLSSPMLARALAAGLASAGIDVY---DLGLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 119 PTPAVSNAIlvhnKKGGALAdGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANAlladglkgvKRISLDAAMA 198
Cdd:COG1109 79 PTPALAFAV----RHLGADG-GIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEK---------EDFRRAEAEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 199 SGHVKE-QDLVQPFVEGLADIVDmAAIQKAGLKLGVDPLGGSGIEYWKRIAEHYKLDLTIVNDHVDQTFRFMHLDKDgai 277
Cdd:COG1109 145 IGKVTRiEDVLEAYIEALKSLVD-EALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNPE--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 278 rmdcssECAMAGL--LALRDKFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRPqwGKEVAvgKTLVSSAM 354
Cdd:COG1109 221 ------PENLEDLieAVKETGADLGIAFDGDADRLGVVDEKGrFLDGDQLLALLARYLLEKGP--GGTVV--VTVMSSLA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 355 IDRVVDALGRKLVEVPVGFKWFVDGLHDGSFGFGGEESAGASFLrfdgtPWSTDKDGIIMCLLAAEITAVTGKNPQEHYN 434
Cdd:COG1109 291 LEDIAEKHGGEVVRTKVGFKYIKEKMRETGAVLGGEESGGIIFP-----DFVPTDDGILAALLLLELLAKQGKSLSELLA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 435 DLaarfgaPSYNRIQASATSAQKAALSKLSPEMVSANTLAGDPITarltaapgngasIGGLKV-MTDNGWFAARPSGTED 513
Cdd:COG1109 366 EL------PRYPQPEINVRVPDEEKIGAVMEKLREAVEDKEELDT------------IDGVKVdLEDGGWVLVRPSGTEP 427
|
490 500 510
....*....|....*....|....*....|
gi 504695918 514 AYKIYCESFlGAEHRQQIEKEAVEIVSEVL 543
Cdd:COG1109 428 LLRVYAEAK-DEEEAEELLAELAELVEEAL 456
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
41-539 |
8.29e-44 |
|
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong 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: 100092 Cd Length: 487 Bit Score: 162.29 E-value: 8.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 41 KFGTSGHRGS--AARHSFNEPHILAIAQAIAE---ERAKNGVTGPCYVGKDTHALSEpAF-ISVLEVLAANGVDVIVqeN 114
Cdd:cd05799 3 EFGTAGLRGKmgAGTNRMNDYTVRQATQGLANylkKKGPDAKNRGVVIGYDSRHNSR-EFaELTAAVLAANGIKVYL--F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 115 NGFTPTPAVSNAIlvhnKKGGALAdGIVITPSHNPPEDGGIK-YNPpNGG----PADTNVTKVVEdrANALLADglkgvk 189
Cdd:cd05799 80 DDLRPTPLLSFAV----RHLGADA-GIMITASHNPKEYNGYKvYWE-DGAqiipPHDAEIAEEIE--AVLEPLD------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 190 rISLDAAMASGHVKE--QDLVQPFVEGL-ADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIAEHYKL-DLTIVNDH--VD 263
Cdd:cd05799 146 -IKFEEALDSGLIKYigEEIDDAYLEAVkKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFtNVIVVEEQaePD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 264 QTF---RFMHLDKDGAIRMdcssecAMAglLALRDKFDLAFANDPDYDRHGIV--TPAG---LMNPNHYLAVAINYLFQH 335
Cdd:cd05799 225 PDFptvKFPNPEEPGALDL------AIE--LAKKVGADLILATDPDADRLGVAvkDKDGewrLLTGNEIGALLADYLLEQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 336 RPQWG---KEVAVGKTLVSSAMIDRVVDALGRKLVEVPVGFKW-------FVDGlhDGSFGFGGEESAGASFlrfdgTPW 405
Cdd:cd05799 297 RKEKGklpKNPVIVKTIVSSELLRKIAKKYGVKVEETLTGFKWignkieeLESG--GKKFLFGFEESIGYLV-----GPF 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 406 STDKDGIIMCLLAAEITAV---TGKNPQEHYNDLAARFGApsYNRIQASATSAQKAALSKLspemvsantlagDPITARL 482
Cdd:cd05799 370 VRDKDGISAAALLAEMAAYlkaQGKTLLDRLDELYEKYGY--YKEKTISITFEGKEGPEKI------------KAIMDRL 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 504695918 483 TAAPGNgasiggLKVMTDNG-WFAARPSGTEDAYKIYCESFlGAEHRQQIEKEAVEIV 539
Cdd:cd05799 436 RNNPNV------LTFYLEDGsRVTVRPSGTEPKIKFYIEVV-GKKTLEEAEKKLDALK 486
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
320-440 |
3.45e-41 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 144.13 E-value: 3.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 320 NPNHYLAVAINYLFQHRpQWGKEVAVGKTLVSSAMIDRVVDALGRKLVEVPVGFKWFVDGLHDGSFGFGGEESAGASFLR 399
Cdd:pfam02880 1 DGDQILALLAKYLLEQG-KLPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 504695918 400 FDgtpwsTDKDGIIMCLLAAEITAVTGKNPQEHYNDLAARF 440
Cdd:pfam02880 80 HA-----TTKDGILAALLVLEILARTGKSLSELLEELPEKY 115
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
40-179 |
9.39e-39 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 138.51 E-value: 9.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 40 VKFGTSGHRGSAARHSFNEPHILAIAQAIAEERAKNGVTGPCYVGKDTHALSEPAFISVLEVLAANGVDVIVqenNGFTP 119
Cdd:pfam02878 2 QLFGTSGIRGKVGVGELTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVIL---LGLLP 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 120 TPAVSNAILVHNKKGgaladGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANA 179
Cdd:pfam02878 79 TPAVSFATRKLKADG-----GIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
42-544 |
3.32e-31 |
|
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: 125.70 E-value: 3.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 42 FGTSGHRGSAARhSFNEPHILAIAQAIAEE-RAKNGVtgpcyVGKDTHAlSEPAFIS-VLEVLAANGVDVIvqeNNGFTP 119
Cdd:TIGR03990 4 FGTSGIRGIVGE-ELTPELALKVGKAFGTYlRGGKVV-----VGRDTRT-SGPMLENaVIAGLLSTGCDVV---DLGIAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 120 TPAVSNAILVHNKKGGaladgIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANAlladglKGVKRISLDAamaS 199
Cdd:TIGR03990 74 TPTLQYAVRELGADGG-----IMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAES------GDFERADWDE---I 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 200 GHVKEQ-DLVQPFVEGLADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIAEHYKLDLTIVNDHVDQTFrfmhldkdgAIR 278
Cdd:TIGR03990 140 GTVTSDeDAIDDYIEAILDKVDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTF---------PGR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 279 MdcsSECAMAGLLALRD-----KFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRpqwGKEVAVgkTLVSS 352
Cdd:TIGR03990 211 N---PEPTPENLKDLSAlvkatGADLGIAHDGDADRLVFIDEKGrFIGGDYTLALFAKYLLEHG---GGKVVT--NVSSS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 353 AMIDRVVDALGRKLVEVPVGFKWFVDGLHDGSFGFGGEESAGASFLRFDGTPwstdkDGIIMCLLAAEITAVTGKNPQEh 432
Cdd:TIGR03990 283 RAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGAVFGGEGNGGWIFPDHHYCR-----DGLMAAALFLELLAEEGKPLSE- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 433 yndLAARFgaPSYNRIQASATSAQKAALSKLspEMVSANTLAGDPITarltaapgngasIGGLKVMTDNGWFAARPSGTE 512
Cdd:TIGR03990 357 ---LLAEL--PKYPMSKEKVELPDEDKEEVM--EAVEEEFADAEIDT------------IDGVRIDFEDGWVLVRPSGTE 417
|
490 500 510
....*....|....*....|....*....|..
gi 504695918 513 DAYKIYCESflgaehrqQIEKEAVEIVSEVLK 544
Cdd:TIGR03990 418 PIVRIYAEA--------KTEERAEELLEEGRS 441
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
42-544 |
3.04e-25 |
|
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: 108.43 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 42 FGTSGHRGSaarhsFNEPH----ILAIAQAIAEERAKngvtGPCYVGKDTHAlSEPAFISVLE-VLAANGVDVIVQennG 116
Cdd:cd03087 2 FGTSGIRGV-----VGEELtpelALKVGKALGTYLGG----GTVVVGRDTRT-SGPMLKNAVIaGLLSAGCDVIDI---G 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 117 FTPTPAVSNAILVHNKKGgaladgIVITPSHNPPEDGGIKYNPPNGgpadTNVTKVVEDRANALLADGlkGVKRISLDaa 196
Cdd:cd03087 69 IVPTPALQYAVRKLGDAG------VMITASHNPPEYNGIKLVNPDG----TEFSREQEEEIEEIIFSE--RFRRVAWD-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 197 mASGHVKEQD-LVQPFVEGLADIVDMAAiqKAGLKLGVDPLGGSGIEYWKRIAEHYKLDLTIVNDHVDQTFrfmhldkdg 275
Cdd:cd03087 135 -EVGSVRREDsAIDEYIEAILDKVDIDG--GKGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFF--------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 276 AIRMdcsSECAMAGLLALRD-----KFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRpqwGKEVAVgkTL 349
Cdd:cd03087 203 PGRP---PEPTPENLSELMElvratGADLGIAHDGDADRAVFVDEKGrFIDGDKLLALLAKYLLEEG---GGKVVT--PV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 350 VSSAMIDRVVDALGRKLVEVPVGfKWFV---DGLHDGSfgFGGEESAGASFLRFDGTPwstdkDGIIMCLLAAEITAVTG 426
Cdd:cd03087 275 DASMLVEDVVEEAGGEVIRTPVG-DVHVaeeMIENGAV--FGGEPNGGWIFPDHQLCR-----DGIMTAALLLELLAEEK 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 427 KnpqehyndLAARFGA-PSYNRIQAS-ATSAQKAAlsklspEMVSAntlagdpITARLTAAPGNGASIGGLKVMTDNGWF 504
Cdd:cd03087 347 P--------LSELLDElPKYPLLREKvECPDEKKE------EVMEA-------VEEELSDADEDVDTIDGVRIEYEDGWV 405
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 504695918 505 AARPSGTEDAYKIYCESflgaehrqQIEKEAVEIVSEVLK 544
Cdd:cd03087 406 LIRPSGTEPKIRITAEA--------KTEERAKELLEEGRS 437
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
41-447 |
1.11e-24 |
|
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: 107.69 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 41 KFGTSGHRGSAArhSFNEPH-----ILAIAQAIAEERAKNGVTGpcyVGKDTHALSEPAFISVLEVLAANGVDVIVQENN 115
Cdd:cd03085 12 KPGTSGLRKKVK--VFQQPNylenfVQSIFNALPPEKLKGATLV---VGGDGRYYNKEAIQIIIKIAAANGVGKVVVGQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 116 GFTPTPAVSNAILVHNKKGGaladgIVITPSHNP--PE-DGGIKYNPPNGGPADTNVTKVVEDRANAL----LADGLKgv 188
Cdd:cd03085 87 GLLSTPAVSAVIRKRKATGG-----IILTASHNPggPEgDFGIKYNTSNGGPAPESVTDKIYEITKKIteykIADDPD-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 189 krISLDAA----MASGH--VKEQDLVQPFVEGLADIVDMAAIQKA----GLKLGVDPLGGSGIEYWKRI-AEHYKLDL-T 256
Cdd:cd03085 160 --VDLSKIgvtkFGGKPftVEVIDSVEDYVELMKEIFDFDAIKKLlsrkGFKVRFDAMHGVTGPYAKKIfVEELGAPEsS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 257 IVNDHVDQTFRFMHLD------KDGAIRMDcssecamagllalRDKFDLAFANDPDYDRHGIVTPAGLMNPNHYLAV--- 327
Cdd:cd03085 238 VVNCTPLPDFGGGHPDpnltyaKDLVELMK-------------SGEPDFGAASDGDGDRNMILGKGFFVTPSDSVAViaa 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 328 ---AINYLFQHRPQwgkevAVGKTLVSSAMIDRVVDALGRKLVEVPVGFKWFVDGLHDGSFGFGGEESAGAsflrfdGTP 404
Cdd:cd03085 305 nakLIPYFYKGGLK-----GVARSMPTSGALDRVAKKLGIPLFETPTGWKFFGNLMDAGKLSLCGEESFGT------GSD 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 504695918 405 WSTDKDGI--IMCLLAaeITAVTGKNPQEHYNDLAARFGAPSYNR 447
Cdd:cd03085 374 HIREKDGLwaVLAWLS--ILAHRNVSVEDIVKEHWQKYGRNFYTR 416
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
30-412 |
1.75e-21 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 98.19 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 30 KPVVGNaehavKFGTSGHRGSAArhSFNEPHIL-----AIAQAIAEERAKNGVTGpcyVGKDTHALSEPAFISVLEVLAA 104
Cdd:PLN02307 18 KPIEGQ-----KPGTSGLRKKVK--VFMQENYLanfvqALFNALPAEKVKGATLV---LGGDGRYFNKEAIQIIIKIAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 105 NGVDVIVQENNGFTPTPAVSNAIlvHNKKGGALADGIVITPSHNP--P-EDGGIKYNPPNGGPADTNVT-KVVEdraNAL 180
Cdd:PLN02307 88 NGVRRVWVGQNGLLSTPAVSAVI--RERDGSKANGGFILTASHNPggPeEDFGIKYNYESGQPAPESITdKIYG---NTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 181 LADGLK---GVKRISLDAAMASGH-------VKEQDLVQPFVEGLADIVDMAAIQK----AGLKLGVDPLGGSGIEYWKR 246
Cdd:PLN02307 163 TIKEYKmaeDIPDVDLSAVGVTKFggpedfdVEVIDPVEDYVKLMKSIFDFELIKKllsrPDFTFCFDAMHGVTGAYAKR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 247 I-AEHYKLDLTIVNDHV-DQTFRFMHLD------KDGAIRMDCSSECAMAgllalrDKFDLAFANDPDYDRHGIVTPAGL 318
Cdd:PLN02307 243 IfVEELGAPESSLLNCVpKEDFGGGHPDpnltyaKELVKRMGLGKTSYGD------EPPEFGAASDGDGDRNMILGKRFF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 319 MNPNHYLAV-------AINYlFQHRPQwgkevAVGKTLVSSAMIDRVVDALGRKLVEVPVGFKWFVDGLHDGSFGFGGEE 391
Cdd:PLN02307 317 VTPSDSVAIiaanaqeAIPY-FSGGLK-----GVARSMPTSAALDVVAKKLNLPFFEVPTGWKFFGNLMDAGKLSICGEE 390
|
410 420
....*....|....*....|.
gi 504695918 392 SAGAsflrfdGTPWSTDKDGI 412
Cdd:PLN02307 391 SFGT------GSDHIREKDGI 405
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
210-317 |
1.57e-19 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 83.88 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 210 PFVEGLADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIAEHYKLDLTIVNDHVDQTFRFmhldkdGAIRMDCSSECAMAG 289
Cdd:pfam02879 1 AYIDHLLELVDSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPT------RAPNPEEPEALALLI 74
|
90 100
....*....|....*....|....*...
gi 504695918 290 LLALRDKFDLAFANDPDYDRHGIVTPAG 317
Cdd:pfam02879 75 ELVKSVGADLGIATDGDADRLGVVDERG 102
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
63-512 |
2.37e-19 |
|
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: 90.65 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 63 AIAQAIAEERAKNGvTGPCYVGKDTHaLSEPAFISVL-EVLAANGVDVIvqeNNGFTPTPAVSNAilVHNKKGGAladGI 141
Cdd:cd03089 22 AIGRAFGSWLLEKG-AKKVVVGRDGR-LSSPELAAALiEGLLAAGCDVI---DIGLVPTPVLYFA--TFHLDADG---GV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 142 VITPSHNPPEDGGIKYNPPNGGPADTNVTKvVEDRANALLADGLKGvkrisldaamaSGHVKEQDLVQPFVEGLADIVDm 221
Cdd:cd03089 92 MITASHNPPEYNGFKIVIGGGPLSGEDIQA-LRERAEKGDFAAATG-----------RGSVEKVDILPDYIDRLLSDIK- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 222 aaIQKAGLKLGVDPLGGSGIEYWKRIAEHYKLDLTIVNDHVDQTFRFMHLDKdgairmdcSSECAMAGLLA--LRDKFDL 299
Cdd:cd03089 159 --LGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDP--------TDPENLEDLIAavKENGADL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 300 AFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRPqwgKEVAVGKTLVSSAMIDrVVDALGRKLVEVPVGFKWFVD 378
Cdd:cd03089 229 GIAFDGDGDRLGVVDEKGeIIWGDRLLALFARDILKRNP---GATIVYDVKCSRNLYD-FIEEAGGKPIMWKTGHSFIKA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 379 GLHDGSFGFGGEESA----GASFLRFDgtpwstdkDGIIMCLLAAEITAVTGKNPQEHYNDLAARFGAPSYNRiqASATS 454
Cdd:cd03089 305 KMKETGALLAGEMSGhiffKDRWYGFD--------DGIYAALRLLELLSKSGKTLSELLADLPKYFSTPEIRI--PVTEE 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 504695918 455 AQKAALSKLSpemVSANTLAGDPITarltaapgngasIGGLKVMTDNGWFAARPSGTE 512
Cdd:cd03089 375 DKFAVIERLK---EHFEFPGAEIID------------IDGVRVDFEDGWGLVRASNTE 417
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
42-539 |
6.21e-15 |
|
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: 77.14 E-value: 6.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 42 FGTSGHRGSAarhsfNEP----HILAIAQAIAEERAKNGVTGPCYVGKDTHaLSEPAFISVLEV-LAANGVDVIVQennG 116
Cdd:cd05802 2 FGTDGIRGVA-----NEPltpeLALKLGRAAGKVLGKGGGRPKVLIGKDTR-ISGYMLESALAAgLTSAGVDVLLL---G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 117 FTPTPAVsnAILVhnKKGGALAdGIVITPSHNPPEDGGIKYNPPNGgpadTNVTKVVEDRANALLADGLKGV---KRIsl 193
Cdd:cd05802 73 VIPTPAV--AYLT--RKLRADA-GVVISASHNPFEDNGIKFFSSDG----YKLPDEVEEEIEALIDKELELPptgEKI-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 194 daamasGHVKE-QDLVQPFVEGLADIVDMAAIQkaGLKLGVDPLGGSGieYwkRIAEH--YKL--DLTIVNDhvdqtfrf 268
Cdd:cd05802 142 ------GRVYRiDDARGRYIEFLKSTFPKDLLS--GLKIVLDCANGAA--Y--KVAPEvfRELgaEVIVINN-------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 269 mhlDKDGA-IRMDCSSECaMAGLLA--LRDKFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAV-AINYLFQHRPQwgkev 343
Cdd:cd05802 202 ---APDGLnINVNCGSTH-PESLQKavLENGADLGIAFDGDADRVIAVDEKGnIVDGDQILAIcARDLKERGRLK----- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 344 avGKTLVSSAM----IDRVVDALGRKLVEVPVGFKWFVDGLHDGSFGFGGEESAGASFLRFdgtpwSTDKDGIIMCLLAA 419
Cdd:cd05802 273 --GNTVVGTVMsnlgLEKALKELGIKLVRTKVGDRYVLEEMLKHGANLGGEQSGHIIFLDH-----STTGDGLLTALQLL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 420 EITAVTGKNpqehYNDLAARFgaPSYNRIQASATSAQKAALSKLspemvsantlagDPITARLTAApgngasiggLKVMT 499
Cdd:cd05802 346 AIMKRSGKS----LSELASDM--KLYPQVLVNVRVKDKKALLEN------------PRVQAAIAEA---------EKELG 398
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 504695918 500 DNGWFAARPSGTEDAYKIYCEsflgAEHRQQIEKEAVEIV 539
Cdd:cd05802 399 GEGRVLVRPSGTEPLIRVMVE----GEDEELVEKLAEELA 434
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
60-521 |
1.54e-13 |
|
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: 72.73 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 60 HILAIAQAIAEERAKngvtGPCYVGKDTHALSEPAFISVLEVLAANGVDVIvqeNNGFTPTPAVSnaILVHNKKGGAlad 139
Cdd:cd05803 23 YVAAFATWQPERTKG----GKIVVGRDGRPSGPMLEKIVIGALLACGCDVI---DLGIAPTPTVQ--VLVRQSQASG--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 140 GIVITPSHNPPEDGGIKYNPPNG---GPAD-TNVTKVVEDRANALLADGLKGVKRISLDAAMAsgHVKEqdlvqpfVEGL 215
Cdd:cd05803 91 GIIITASHNPPQWNGLKFIGPDGeflTPDEgEEVLSCAEAGSAQKAGYDQLGEVTFSEDAIAE--HIDK-------VLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 216 ADiVDMAAIQKAGLKLGVDPLGGSGIEYWKRIAEhyKLDLTIVNDHVDQTFRFMHLDKdgAIRMDCSSECAMagllALRD 295
Cdd:cd05803 162 VD-VDVIKIRERNFKVAVDSVNGAGGLLIPRLLE--KLGCEVIVLNCEPTGLFPHTPE--PLPENLTQLCAA----VKES 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 296 KFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRPQWGKEVavgKTLVSSAMIDRVVDALGRKLVEVPVGFK 374
Cdd:cd05803 233 GADVGFAVDPDADRLALVDEDGrPIGEEYTLALAVDYVLKYGGRKGPVV---VNLSTSRALEDIARKHGVPVFRSAVGEA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 375 WFVDGLHDGSFGFGGEESAG-----ASFLRfdgtpwstdkDGIIMCLLAAEITAVTGKNPQEHYNDLaarfgaPSYNRIQ 449
Cdd:cd05803 310 NVVEKMKEVDAVIGGEGNGGvilpdVHYGR----------DSLVGIALVLQLLAASGKPLSEIVDEL------PQYYISK 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504695918 450 ASATSAQKA---ALSKLSPEMVSANTLAGDpitarltaapgngasigGLKVMTDNGWFAARPSGTEDAYKIYCES 521
Cdd:cd05803 374 TKVTIAGEAlerLLKKLEAYFKDAEASTLD-----------------GLRLDSEDSWVHVRPSNTEPIVRIIAEA 431
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
119-543 |
5.58e-09 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 58.54 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 119 PTPAVSNAIlvhnKKGGALAdGIVITPSHNPPEDGGIKYNPPNGG----PADTNVTKVVEDRANALladglkgvkRISLD 194
Cdd:PTZ00150 128 PTPFVPYAV----RKLKCLA-GVMVTASHNPKEDNGYKVYWSNGAqiipPHDKNISAKILSNLEPW---------SSSWE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 195 AAMASGHVKE-QDLVQPFVEGLADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIAEHYKLdltivNDH--VDQ------- 264
Cdd:PTZ00150 194 YLTETLVEDPlAEVSDAYFATLKSEYNPACCDRSKVKIVYTAMHGVGTRFVQKALHTVGL-----PNLlsVAQqaepdpe 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 265 --TFRFMHlDKDGAIRMDCSSEcamaglLALRDKFDLAFANDPDYDRHGIvtpAGLMNPNHY------LAVAINYLFQHR 336
Cdd:PTZ00150 269 fpTVTFPN-PEEGKGALKLSME------TAEAHGSTVVLANDPDADRLAV---AEKLNNGWKiftgneLGALLAWWAMKR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 337 PQWgKEVAVGK-----TLVSSAMIDRVVDALGRKLVEVPVGFKWFVDGLHD------GSFGFGGEESAGasflrFDGTPW 405
Cdd:PTZ00150 339 YRR-QGIDKSKcfficTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIElnaengLTTLFAYEEAIG-----FMLGTR 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 406 STDKDGIIMCLLAAEIT---AVTGKNPQEHYNDLAARFGA-PSYNRIqasATSAQKAALSKLSPEMVSA----NTLAGDP 477
Cdd:PTZ00150 413 VRDKDGVTAAAVVAEMAlylYERGKTLVEHLESLYKQYGYhFTNNSY---YICYDPSRIVSIFNDIRNNgsypTKLGGYP 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 478 ITARL-------TAAPGNGASIGG------LKVMTDNGWFAA-RPSGTEDAYKIYCEsfLGAEHRQQIEKEAVEIVSEVL 543
Cdd:PTZ00150 490 VTRIRdlttgydTATPDGKPLLPVsastqmITFYFENGAIITiRGSGTEPKLKWYAE--LSGTKDEAVEKELAALVDEVV 567
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
41-162 |
7.20e-06 |
|
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: 48.74 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 41 KFGTSGHRG---------SAArhsfnepHILAIAQAIAEERAKNGVtgpcYVGKDTHAlSEPAF-ISVLEVLAANGVDVI 110
Cdd:cd03088 1 KFGTSGLRGlvtdltdevCYA-------YTRAFLQHLESKFPGDTV----AVGRDLRP-SSPRIaAACAAALRDAGFRVV 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 504695918 111 vqeNNGFTPTPAVSNAilvhnkkggALADG---IVITPSHNPPEDGGIKYNPPNG 162
Cdd:cd03088 69 ---DCGAVPTPALALY---------AMKRGapaIMVTGSHIPADRNGLKFYRPDG 111
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
133-188 |
2.63e-05 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 46.96 E-value: 2.63e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 504695918 133 KGGALADGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANALLADGLKGV 188
Cdd:PTZ00302 71 KRGNKSVGVMITASHNPIQDNGVKIIDPDGGMLEESWEKICTDFANARTGEDLVSV 126
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
140-195 |
3.43e-05 |
|
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: 46.43 E-value: 3.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 504695918 140 GIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANALLADGLKGVKRISLDA 195
Cdd:cd03086 38 GVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDDELLVLVLMLISVK 93
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
83-162 |
8.97e-05 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 45.13 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 83 VGKDTHaLSEPAFISVLEV-LAANGVDVivqennGFT---PTPAVsnAILVHnkkggAL-AD-GIVITPSHNPPEDGGIK 156
Cdd:PRK10887 44 IGKDTR-ISGYMLESALEAgLAAAGVDV------LLTgpmPTPAV--AYLTR-----TLrAEaGIVISASHNPYYDNGIK 109
|
....*.
gi 504695918 157 YNPPNG 162
Cdd:PRK10887 110 FFSADG 115
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
489-542 |
8.79e-04 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 38.02 E-value: 8.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 504695918 489 GASIGGLKVMTDNGW-FAARPSGTEDAYKIYCEsflgAEHRQQIEKEAVEIVSEV 542
Cdd:pfam00408 20 KVFADAEKILGEDGRrLDVRPSGTEPVLRVMVE----GDSDEELARLADEIADLL 70
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
140-202 |
2.13e-03 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 40.78 E-value: 2.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695918 140 GIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANALLADGLKGVKR-------ISLDAAMASGHV 202
Cdd:PLN02895 61 GLMITASHNPVSDNGVKIVDPSGGMLPQAWEPFADALANAPDPDALVQLIRefvkkenIPAVGGNPPAEV 130
|
|
| |
