|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 1050.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 2 AIDKRAGQPAQQSDLINVAQLTAQYYVLKPEAGNAEHAVKFGTSGHRGSAGRHNFNEQHILAIAQAIAEDRAKNGITGPC 81
Cdd:TIGR01132 1 AIHPRAGQPAQQEDLINVAQLVAQYYVLQPEAGNAAHAVKFGTSGHRGSALRGTFNEPHILAIAQAIAEYRAAQGITGPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 82 YVGKDTHALSEPAFISVLEVLAANGVDVIVQENNGFTPTPAISNAILVHNKKGGPLADGIVITPSHNPPEDGGIKYNPPN 161
Cdd:TIGR01132 81 YIGKDTHALSEPAFISVLEVLAANGVEVIVQENNGFTPTPAVSHAILTHNKKGEPLADGIVITPSHNPPEDGGIKYNPPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 162 GGPADTNVTKVVENRANELLASGLQGVRRLSLDAALASGHVKEQDLVQPFIEGLADIVDMAAIQKAGLKLGVDPLGGSGI 241
Cdd:TIGR01132 161 GGPADTEATQAIEDRANALLANGLKGVKRLPLAQALASGTVKAHDLVQPYVDGLADIVDMAAIQKAGLRLGVDPLGGSGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 242 EYWKRIAEYYKLDLTIVNDHVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTPAGLMNP 321
Cdd:TIGR01132 241 DYWKRIAEKYNLNLTLVNPQVDPTFRFMTLDKDGKIRMDCSSPYAMAGLLALRDKYDLAFGNDPDYDRHGIVTPAGLMNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 322 NHYLAVAINYLFRHRPQWGQDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFD 401
Cdd:TIGR01132 321 NHYLAVAINYLFQHRPQWGGDVAVGKTLVSSAMIDRVVADLGRQLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 402 GTPWSTDKDGIIMCLLAAEITAVTGKNPQEHYDELAARFGAPSYNRLQASATSAQKAALSKLSPEMVSASQLAGDPITAR 481
Cdd:TIGR01132 401 GTPWSTDKDGIIMCLLAAEITAVTGKNPQQHYNELAAKFGAPSYNRIQAPATSAQKARLKKLSPEMVSATTLAGDPITAR 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336437369 482 LTAAPGNGASIGGLKVMTDNGWFAARPSGTEDAYKIYCESFLGEAHRKQIEKEAVEIVSEVLK 544
Cdd:TIGR01132 481 LTAAPGNGAAIGGLKVTTDNGWFAARPSGTEDVYKIYCESFKGEEHLKQIEKEAVEIVSEVLK 543
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
3-544 |
0e+00 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 1039.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 3 IDKRAGQPAQQSDLINVAQLTAQYYVLKPEAGNAEHAVKFGTSGHRGSAGRHNFNEQHILAIAQAIAEDRAKNGITGPCY 82
Cdd:PRK07564 1 IHPRAGQPAQPSDLINVPRLVSAYYTLKPDPTNPFQDVKFGTSGHRGSSLQPSFNENHILAIFQAICEYRGKQGITGPLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 83 VGKDTHALSEPAFISVLEVLAANGVDVIVQENNGFTPTPAISNAILVHNKKGGPLADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:PRK07564 81 VGGDTHALSEPAIQSALEVLAANGVGVVIVGRGGYTPTPAVSHAILKYNGRGGGLADGIVITPSHNPPEDGGIKYNPPNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 163 GPADTNVTKVVENRANELLASGLQGVRRLSLDAALASGHVKEQDLVQPFIEGLADIVDMAAIQKAGLKLGVDPLGGSGIE 242
Cdd:PRK07564 161 GPADTDVTDAIEARANELLAYGLKGVKRIPLDRALASMTVEVIDPVADYVEDLENVFDFDAIRKAGLRLGVDPLGGATGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 243 YWKRIAEYYKLDLTIVNDHVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTPAGLMNPN 322
Cdd:PRK07564 241 YWKAIAERYGLDLTVVNAPVDPTFNFMPLDDDGKIRMDCSSPYAMAGLLALKDAFDLAFANDPDGDRHGIVTPGGLMNPN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 323 HYLAVAINYLFRHRPQWGQDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFDG 402
Cdd:PRK07564 321 HYLAVAIAYLFHHRPGWRAGAGVGKTLVSSAMIDRVAAKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESAGASFLRRDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 403 TPWSTDKDGIIMCLLAAEITAVTGKNPQEHYDELAARFGAPSYNRLQASATSAQKAALSKLSPEMVSASQLAGDPITARL 482
Cdd:PRK07564 401 SVWTTDKDGLIAVLLAAEILAVTGKSPSEIYRELWARFGRPYYSRHDAPATPEQKAALRKLSPELVGATELAGDPIDASL 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336437369 483 TAAPGNGASIGGLKVMTDNGWFAARPSGTEDAYKIYCESFLGEAHRKQIEKEAVEIVSEVLK 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: 1039.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 20 AQLTAQYYVLKPEAGNAEHAVKFGTSGHRGSAGRHNFNEQHILAIAQAIAEDRAKNGITGPCYVGKDTHALSEPAFISVL 99
Cdd:cd05801 1 PRLITAYYTLKPDPSNPAQRVAFGTSGHRGSSLKGSFNEAHILAISQAICDYRKSQGITGPLFLGKDTHALSEPAFISAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 100 EVLAANGVDVIVQENNGFTPTPAISNAILVHNKKG-GPLADGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVENRAN 178
Cdd:cd05801 81 EVLAANGVEVIIQQNDGYTPTPVISHAILTYNRGRtEGLADGIVITPSHNPPEDGGFKYNPPHGGPADTDITRWIEKRAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 179 ELLASGLQGVRRLSLDAALASGHVKEQDLVQPFIEGLADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIAEYYKLDLTIV 258
Cdd:cd05801 161 ALLANGLKGVKRIPLEAALASGYTHRHDFVTPYVADLGNVIDMDAIRKSGLRLGVDPLGGASVPYWQPIAEKYGLNLTVV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 259 NDHVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTP-AGLMNPNHYLAVAINYLFRHRP 337
Cdd:cd05801 241 NPKVDPTFRFMTLDHDGKIRMDCSSPYAMAGLLKLKDKFDLAFANDPDADRHGIVTPsAGLMNPNHYLSVAIDYLFTHRP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 338 QWGQDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFDGTPWSTDKDGIIMCLL 417
Cdd:cd05801 321 LWNKSAGVGKTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDGLLDGSLGFGGEESAGASFLRRDGTVWTTDKDGIIMCLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 418 AAEITAVTGKNPQEHYDELAARFGAPSYNRLQASATSAQKAALSKLSPEMVSASQLAGDPITARLTAAPGNGASIGGLKV 497
Cdd:cd05801 401 AAEILAVTGKDPGQLYQELTERFGEPYYARIDAPATPEQKARLKKLSPEQVTATELAGDPILAKLTRAPGNGASIGGLKV 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1336437369 498 MTDNGWFAARPSGTEDAYKIYCESFLGEAHRKQIEKEAVEIV 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: 1006.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 3 IDKRAGQPAQQSDLINVAQLTAQYYVLKPEAGNAEHAVKFGTSGHRGSAGRHNFNEQHILAIAQAIAEDRAKNGITGPCY 82
Cdd:COG0033 1 LHPRAGQPAPPSDLIDVPRLVSAYYTIKPDPTTPFQDVKFGTSGHRGSSLKGSFNEPHILAITQAIFDYRKAQGITGPLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 83 VGKDTHALSEPAFISVLEVLAANGVDVIVQENNGFTPTPAISNAILVHNKKGGPLADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:COG0033 81 LGGDTHALSEPAIQTALEVLAANGVGVVIVGQGGYTPTPAVSHAILKYNRGTSGAADGIVLTPSHNPPEDGGIKYNPPNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 163 GPADTNVTKVVENRANELLASGLQGVRRLSLDAALASGHVKEQDLVQPFIEGLADIVDMAAIQKAGLKLGVDPLGGSGIE 242
Cdd:COG0033 161 GPADEDVTDAIEARANEILEYGLADVKRVPLDRAGTAMTVEVIDPVADYVELLESVFDFDAIRAAGFRIGFDPLGGATGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 243 YWKRIAEYYKLDLTIVNDHVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTP-AGLMNP 321
Cdd:COG0033 241 YWKAIAERYGLDLTVVNGVPDPDFRFMTLDWDGGIRMDPSSPYAMASLIAGKDAPDFAAANDGDGDRHGIVTPrGGLMNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 322 NHYLAVAINYLFRHRPQWGQDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFD 401
Cdd:COG0033 321 NHYLAVAIAYLFTHRPGWAALAGVGKTMVTSSAIDRVAAALGRPLYEVPVGFKWFVNGLDAGSLGFGGEESAGASFLRRD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 402 GTPWSTDKDGIIMCLLAAEITAVTGKNPQEHYDELAARFGAPSYNRLQASATSAQKAALSKLSPEMVSASQLAGDPITAR 481
Cdd:COG0033 401 GSVWTTDKDGLWAVLLAAEILAVTGKSPAEIYRELWARFGRPYYSRHDAEATDEQKARLAKLSGEQVGATTLAGEDIFAY 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336437369 482 LTAAPGNGASIGGLKVMTDNGWFAARPSGTEDAYKIYCESFLGEAHRKQIEKEAVEIVSEVLK 544
Cdd:COG0033 481 LDPAPGNGAAIGGLKVVTENGWFAARPSGTETTYKIYAESFEGDEHLHQIDAEAADLVDAALA 543
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
41-539 |
8.32e-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: 318.53 E-value: 8.32e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 41 KFGTSGHRGSAGRHnFNEQHILAIAQAIAEdrakngitgpcyvgkdthalsepafisvlevlaangvdvivqenngftpt 120
Cdd:cd03084 1 IFGTSGVRGVVGDD-ITPETAVALGQAIGS-------------------------------------------------- 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 121 paisnailvhnkkggplADGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVENRANELLASGLQGVRrlsldaalASG 200
Cdd:cd03084 30 -----------------TGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYE--------LGG 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 201 HVKEQDLVQPFIEGLADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIAEYYKLDLTIVNDHVDQTFrfmhldkdGAIRMD 280
Cdd:cd03084 85 SVKAVDILQRYFEALKKLFDVAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNF--------GNINPD 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 281 CSSECAMAGLLALRD--KFDLAFANDPDYDRHGIVTP-AGLMNPNHYLAVAINYLFRHrpqWGQDVAVGKTLVSSAMIDR 357
Cdd:cd03084 157 PGSETNLKQLLAVVKaeKADFGVAFDGDADRLIVVDEnGGFLDGDELLALLAVELFLT---FNPRGGVVKTVVSSGALDK 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 358 VVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFdgtpwSTDKDGIIMCLLAAEITAVTGKNPQEHYDELA 437
Cdd:cd03084 234 VAKKLGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGVIFPEF-----HPGRDGISAALLLLEILANLGKSLSELFSELP 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 438 ARFgapsYNRLQASatsaqkaalsklspemvsasqlagdpitarltaapgngasigglkvmtdnGWFAARPSGTEDAYKI 517
Cdd:cd03084 309 RYY----YIRLKVR--------------------------------------------------GWVLVRASGTEPAIRI 334
|
490 500
....*....|....*....|..
gi 1336437369 518 YCESFLGEaHRKQIEKEAVEIV 539
Cdd:cd03084 335 YAEADTQE-DVEQIKKEARELV 355
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
40-522 |
1.24e-92 |
|
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: 290.99 E-value: 1.24e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 40 VKFGTSGHRGSAGRhNFNEQHILAIAQAIAEDRAKNGITGP-CYVGKDTHALSEPAFISVLEVLAANGVDVIVQEnnGFT 118
Cdd:cd05800 1 IKFGTDGWRGIIAE-DFTFENVRRVAQAIADYLKEEGGGGRgVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSD--RPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 119 PTPAISNAILVHNkkggpLADGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVENRANELLASGLQgvrrlsldaALA 198
Cdd:cd05800 78 PTPAVSWAVKKLG-----AAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLE---------ARA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 199 SGHVKEQDLVQPFIEGLADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIAEYYKLDLTIVNDHVDQTFrfmhldkdGAIR 278
Cdd:cd05800 144 EGLIETIDPKPDYLEALRSLVDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLF--------GGIP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 279 MDCSSEcAMAGLLAL--RDKFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFRHRPQWGqdvAVGKTLVSSAMI 355
Cdd:cd05800 216 PEPIEK-NLGELAEAvkEGGADLGLATDGDADRIGAVDEKGnFLDPNQILALLLDYLLENKGLRG---PVVKTVSTTHLI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 356 DRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFdgTPwstDKDGIIMCLLAAEITAVTGKNPQEHYDE 435
Cdd:cd05800 292 DRIAEKHGLPVYETPVGFKYIAEKMLEEDVLIGGEESGGLGIRGH--IP---ERDGILAGLLLLEAVAKTGKPLSELVAE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 436 LAARFGAPSYNRLQASATSAQKAA-LSKLSPEmvSASQLAGDPITARLTaapgngasIGGLKVMTDNG-WFAARPSGTED 513
Cdd:cd05800 367 LEEEYGPSYYDRIDLRLTPAQKEAiLEKLKNE--PPLSIAGGKVDEVNT--------IDGVKLVLEDGsWLLIRPSGTEP 436
|
....*....
gi 1336437369 514 AYKIYCESF 522
Cdd:cd05800 437 LLRIYAEAP 445
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
42-543 |
1.24e-64 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 217.38 E-value: 1.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 42 FGTSGHRGSAGRhNFNEQHILAIAQAIAE---DRAKNGITgpcyVGKDTHALSEPAFISVLEVLAANGVDVIvqeNNGFT 118
Cdd:COG1109 7 FGTDGIRGIVGE-ELTPEFVLKLGRAFGTylkEKGGPKVV----VGRDTRLSSPMLARALAAGLASAGIDVY---DLGLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 119 PTPAISNAILVHNKKGGpladgIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVENRANELlasglqgvrRLSLDAALA 198
Cdd:COG1109 79 PTPALAFAVRHLGADGG-----IMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKE---------DFRRAEAEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 199 SGHVKE-QDLVQPFIEGLADIVDmAAIQKAGLKLGVDPLGGSGIEYWKRIAEYYKLDLTIVNDHVDQTFRFMHLDKDgai 277
Cdd:COG1109 145 IGKVTRiEDVLEAYIEALKSLVD-EALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNPE--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 278 rmdcssECAMAGL--LALRDKFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFRHRPqwGQDVAvgKTLVSSAM 354
Cdd:COG1109 221 ------PENLEDLieAVKETGADLGIAFDGDADRLGVVDEKGrFLDGDQLLALLARYLLEKGP--GGTVV--VTVMSSLA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 355 IDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLrfdgtPWSTDKDGIIMCLLAAEITAVTGKNPQEHYD 434
Cdd:COG1109 291 LEDIAEKHGGEVVRTKVGFKYIKEKMRETGAVLGGEESGGIIFP-----DFVPTDDGILAALLLLELLAKQGKSLSELLA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 435 ELaarfgaPSYNRLQASATSAQKAALSKLSPEMVSASQLAGDPITarltaapgngasIGGLKV-MTDNGWFAARPSGTED 513
Cdd:COG1109 366 EL------PRYPQPEINVRVPDEEKIGAVMEKLREAVEDKEELDT------------IDGVKVdLEDGGWVLVRPSGTEP 427
|
490 500 510
....*....|....*....|....*....|
gi 1336437369 514 AYKIYCESFlGEAHRKQIEKEAVEIVSEVL 543
Cdd:COG1109 428 LLRVYAEAK-DEEEAEELLAELAELVEEAL 456
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
320-440 |
1.21e-41 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 145.28 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 320 NPNHYLAVAINYLFRHRpQWGQDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLR 399
Cdd:pfam02880 1 DGDQILALLAKYLLEQG-KLPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1336437369 400 FDgtpwsTDKDGIIMCLLAAEITAVTGKNPQEHYDELAARF 440
Cdd:pfam02880 80 HA-----TTKDGILAALLVLEILARTGKSLSELLEELPEKY 115
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
40-179 |
1.40e-39 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 140.82 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 40 VKFGTSGHRGSAGRHNFNEQHILAIAQAIAEDRAKNGITGPCYVGKDTHALSEPAFISVLEVLAANGVDVIVqenNGFTP 119
Cdd:pfam02878 2 QLFGTSGIRGKVGVGELTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVIL---LGLLP 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 120 TPAISNAILVHNKKGgpladGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVENRANE 179
Cdd:pfam02878 79 TPAVSFATRKLKADG-----GIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
42-544 |
1.43e-33 |
|
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: 132.64 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 42 FGTSGHRGSAGRhNFNEQHILAIAQAIAEDRAKNGITgpcyVGKDTHAlSEPAFIS-VLEVLAANGVDVIvqeNNGFTPT 120
Cdd:TIGR03990 4 FGTSGIRGIVGE-ELTPELALKVGKAFGTYLRGGKVV----VGRDTRT-SGPMLENaVIAGLLSTGCDVV---DLGIAPT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 121 PAISNAILVHNKKGGpladgIVITPSHNPPEDGGIKYNPPNGgpadTNVTKVVENRANELLASGlqgvrrlslDAALAS- 199
Cdd:TIGR03990 75 PTLQYAVRELGADGG-----IMITASHNPPEYNGIKLLNSDG----TELSREQEEEIEEIAESG---------DFERADw 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 200 ---GHVKEQ-DLVQPFIEGLADIVDMAAIQKAGLKLGVDPLGGSGieywKRIAEY--YKLDLTI--VNDHVDQTFrfmhl 271
Cdd:TIGR03990 137 deiGTVTSDeDAIDDYIEAILDKVDVEAIRKKGFKVVVDCGNGAG----SLTTPYllRELGCKVitLNCQPDGTF----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 272 dkdgAIRMdcsSECAMAGLLALRD-----KFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFRHRpqwGQDVAV 345
Cdd:TIGR03990 208 ----PGRN---PEPTPENLKDLSAlvkatGADLGIAHDGDADRLVFIDEKGrFIGGDYTLALFAKYLLEHG---GGKVVT 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 346 gkTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFDGTPwstdkDGIIMCLLAAEITAVT 425
Cdd:TIGR03990 278 --NVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGAVFGGEGNGGWIFPDHHYCR-----DGLMAAALFLELLAEE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 426 GKNPQEHYDELaarfgaPSYnrlqasATSAQKAALS-KLSPEMVSAsqlagdpITARLTAAPGNgaSIGGLKVMTDNGWF 504
Cdd:TIGR03990 351 GKPLSELLAEL------PKY------PMSKEKVELPdEDKEEVMEA-------VEEEFADAEID--TIDGVRIDFEDGWV 409
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1336437369 505 AARPSGTEDAYKIYCESflgeahrkQIEKEAVEIVSEVLK 544
Cdd:TIGR03990 410 LVRPSGTEPIVRIYAEA--------KTEERAEELLEEGRS 441
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
42-544 |
4.88e-28 |
|
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: 116.52 E-value: 4.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 42 FGTSGHRGSAGRhNFNEQHILAIAQAIAEDRAKngitGPCYVGKDTHAlSEPAFISVLE-VLAANGVDVIVQennGFTPT 120
Cdd:cd03087 2 FGTSGIRGVVGE-ELTPELALKVGKALGTYLGG----GTVVVGRDTRT-SGPMLKNAVIaGLLSAGCDVIDI---GIVPT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 121 PAISNAILVHNKKGgpladgIVITPSHNPPEDGGIKYNPPNGgpadTNVTKVVENRANELLASGlqGVRRLSLDaalASG 200
Cdd:cd03087 73 PALQYAVRKLGDAG------VMITASHNPPEYNGIKLVNPDG----TEFSREQEEEIEEIIFSE--RFRRVAWD---EVG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 201 HVKEQD-LVQPFIEGLADIVDMAAiqKAGLKLGVDPLGGSGIEYWKRIAEYYKLDLTIVNDHVDQTFrfmhldkdgAIRM 279
Cdd:cd03087 138 SVRREDsAIDEYIEAILDKVDIDG--GKGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFF---------PGRP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 280 dcsSECAMAGLLALRD-----KFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFRHRPqwGQDVAvgkTLVSSA 353
Cdd:cd03087 207 ---PEPTPENLSELMElvratGADLGIAHDGDADRAVFVDEKGrFIDGDKLLALLAKYLLEEGG--GKVVT---PVDASM 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 354 MIDRVVNDLGRKLVEVPVGfKWFVDGLFDGSFG-FGGEESAGASFLRFDGTPwstdkDGIIMCLLAAEITAvTGKNPQEH 432
Cdd:cd03087 279 LVEDVVEEAGGEVIRTPVG-DVHVAEEMIENGAvFGGEPNGGWIFPDHQLCR-----DGIMTAALLLELLA-EEKPLSEL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 433 YDELaarfgaPSYNRLQAS-ATSAQKAAlsklspEMVSAsqlagdpITARLTAAPGNGASIGGLKVMTDNGWFAARPSGT 511
Cdd:cd03087 352 LDEL------PKYPLLREKvECPDEKKE------EVMEA-------VEEELSDADEDVDTIDGVRIEYEDGWVLIRPSGT 412
|
490 500 510
....*....|....*....|....*....|...
gi 1336437369 512 EDAYKIYCESflgeahrkQIEKEAVEIVSEVLK 544
Cdd:cd03087 413 EPKIRITAEA--------KTEERAKELLEEGRS 437
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
41-447 |
9.54e-22 |
|
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: 98.83 E-value: 9.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 41 KFGTSGHRGSAG---RHNFNEQHILAIAQAIAEDRAKNGITGpcyVGKDTHALSEPAFISVLEVLAANGVDVIVQENNGF 117
Cdd:cd03085 12 KPGTSGLRKKVKvfqQPNYLENFVQSIFNALPPEKLKGATLV---VGGDGRYYNKEAIQIIIKIAAANGVGKVVVGQNGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 118 TPTPAISNAILVHNKKGGpladgIVITPSHNP--PE-DGGIKYNPPNGGPADTNVT-------------KVVENRANELl 181
Cdd:cd03085 89 LSTPAVSAVIRKRKATGG-----IILTASHNPggPEgDFGIKYNTSNGGPAPESVTdkiyeitkkiteyKIADDPDVDL- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 182 asGLQGVRRLSLDAALasghVKEQDLVQPFIEGLADIVDMAAIQKA----GLKLGVDPLGGSGIEYWKRI-AEYYKLDL- 255
Cdd:cd03085 163 --SKIGVTKFGGKPFT----VEVIDSVEDYVELMKEIFDFDAIKKLlsrkGFKVRFDAMHGVTGPYAKKIfVEELGAPEs 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 256 TIVNDHVDQTFRFMHLD------KDGAIRMDcssecamagllalRDKFDLAFANDPDYDRHGIVTPAGLMNPNHYLAV-- 327
Cdd:cd03085 237 SVVNCTPLPDFGGGHPDpnltyaKDLVELMK-------------SGEPDFGAASDGDGDRNMILGKGFFVTPSDSVAVia 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 328 ----AINYLFRHRPQwgqdvAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDgLFD-GSFGFGGEESAGAsflrfdG 402
Cdd:cd03085 304 anakLIPYFYKGGLK-----GVARSMPTSGALDRVAKKLGIPLFETPTGWKFFGN-LMDaGKLSLCGEESFGT------G 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1336437369 403 TPWSTDKDGI--IMCLLAaeITAVTGKNPQEHYDELAARFGAPSYNR 447
Cdd:cd03085 372 SDHIREKDGLwaVLAWLS--ILAHRNVSVEDIVKEHWQKYGRNFYTR 416
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
48-512 |
4.58e-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: 89.88 E-value: 4.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 48 RGSAGRhNFNEQHILAIAQAIAEDRAKNGItGPCYVGKDTHaLSEPAFISVL-EVLAANGVDVIvqeNNGFTPTPAISNA 126
Cdd:cd03089 8 RGIAGE-ELTEEIAYAIGRAFGSWLLEKGA-KKVVVGRDGR-LSSPELAAALiEGLLAAGCDVI---DIGLVPTPVLYFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 127 IlVHNKKGGpladGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVvenranellasgLQGVRRLSLDAALASGHVKEQD 206
Cdd:cd03089 82 T-FHLDADG----GVMITASHNPPEYNGFKIVIGGGPLSGEDIQAL------------RERAEKGDFAAATGRGSVEKVD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 207 LVQPFIEGLADIVDmaaIQKAGLKLGVDPLGGSGIEYWKRIAEYYKLDLTIVNDHVDQTFRFMHLDKdgairmdcSSECA 286
Cdd:cd03089 145 ILPDYIDRLLSDIK---LGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDP--------TDPEN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 287 MAGLLA--LRDKFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFRHRPqwGQDVaVGKTLVSSAMIDrVVNDLG 363
Cdd:cd03089 214 LEDLIAavKENGADLGIAFDGDGDRLGVVDEKGeIIWGDRLLALFARDILKRNP--GATI-VYDVKCSRNLYD-FIEEAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 364 RKLVEVPVGFKWFVDGLFDGSFGFGGEESA----GASFLRFDgtpwstdkDGIIMCLLAAEITAVTGKNPQEHYDELAAR 439
Cdd:cd03089 290 GKPIMWKTGHSFIKAKMKETGALLAGEMSGhiffKDRWYGFD--------DGIYAALRLLELLSKSGKTLSELLADLPKY 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336437369 440 FGAPSYNRlqASATSAQKAALSKLSpemVSASQLAGDPITarltaapgngasIGGLKVMTDNGWFAARPSGTE 512
Cdd:cd03089 362 FSTPEIRI--PVTEEDKFAVIERLK---EHFEFPGAEIID------------IDGVRVDFEDGWGLVRASNTE 417
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
41-412 |
7.84e-19 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 89.71 E-value: 7.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 41 KFGTSGHRGSAG---RHNFNEQHILAIAQAIAEDRAKNGITGpcyVGKDTHALSEPAFISVLEVLAANGVDVIVQENNGF 117
Cdd:PLN02307 24 KPGTSGLRKKVKvfmQENYLANFVQALFNALPAEKVKGATLV---LGGDGRYFNKEAIQIIIKIAAANGVRRVWVGQNGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 118 TPTPAISNAIlvHNKKGGPLADGIVITPSHNP--P-EDGGIKYNPPNGGPADTNVT-KVVEN--RANEL-LASGLQGVrr 190
Cdd:PLN02307 101 LSTPAVSAVI--RERDGSKANGGFILTASHNPggPeEDFGIKYNYESGQPAPESITdKIYGNtlTIKEYkMAEDIPDV-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 191 lSLDAALASGH-------VKEQDLVQPFIEGLADIVDMAAIQK----AGLKLGVDPLGGSGIEYWKRI-AEYYKLDLTIV 258
Cdd:PLN02307 177 -DLSAVGVTKFggpedfdVEVIDPVEDYVKLMKSIFDFELIKKllsrPDFTFCFDAMHGVTGAYAKRIfVEELGAPESSL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 259 NDHV-DQTFRFMHLD------KDGAIRMDCSSECAMAgllalrDKFDLAFANDPDYDRHGIVTPAGLMNPNHYLAV---- 327
Cdd:PLN02307 256 LNCVpKEDFGGGHPDpnltyaKELVKRMGLGKTSYGD------EPPEFGAASDGDGDRNMILGKRFFVTPSDSVAIiaan 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 328 ---AINYlFRHRPQwgqdvAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGAsflrfdGTP 404
Cdd:PLN02307 330 aqeAIPY-FSGGLK-----GVARSMPTSAALDVVAKKLNLPFFEVPTGWKFFGNLMDAGKLSICGEESFGT------GSD 397
|
....*...
gi 1336437369 405 WSTDKDGI 412
Cdd:PLN02307 398 HIREKDGI 405
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
210-317 |
1.09e-18 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 81.18 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 210 PFIEGLADIVDMAAIQKAGLKLGVDPLGGSGIEYWKRIAEYYKLDLTIVNDHVDQTFRFmhldkdGAIRMDCSSECAMAG 289
Cdd:pfam02879 1 AYIDHLLELVDSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPT------RAPNPEEPEALALLI 74
|
90 100
....*....|....*....|....*...
gi 1336437369 290 LLALRDKFDLAFANDPDYDRHGIVTPAG 317
Cdd:pfam02879 75 ELVKSVGADLGIATDGDADRLGVVDERG 102
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
59-538 |
1.47e-15 |
|
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: 78.89 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 59 QHILAIAQAIAEDRAKngitGPCYVGKDTHALSEPAFISVLEVLAANGVDVIvqeNNGFTPTPAISnaILVHNKKGgplA 138
Cdd:cd05803 22 RYVAAFATWQPERTKG----GKIVVGRDGRPSGPMLEKIVIGALLACGCDVI---DLGIAPTPTVQ--VLVRQSQA---S 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 139 DGIVITPSHNPPEDGGIKYNPPNG---GPADtnVTKVVE-NRANELLASGLQGVRRL-SLDAALASgHVKEqdlvqpfIE 213
Cdd:cd05803 90 GGIIITASHNPPQWNGLKFIGPDGeflTPDE--GEEVLScAEAGSAQKAGYDQLGEVtFSEDAIAE-HIDK-------VL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 214 GLADiVDMAAIQKAGLKLGVDPLGGSGIEYWKRIAEyyKLDLTIVNDHVDQTFRFMHLDKdgAIRMDCSSECAMAgllaL 293
Cdd:cd05803 160 ALVD-VDVIKIRERNFKVAVDSVNGAGGLLIPRLLE--KLGCEVIVLNCEPTGLFPHTPE--PLPENLTQLCAAV----K 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 294 RDKFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFRHRPQWGQDVavgKTLVSSAMIDRVVNDLGRKLVEVPVG 372
Cdd:cd05803 231 ESGADVGFAVDPDADRLALVDEDGrPIGEEYTLALAVDYVLKYGGRKGPVV---VNLSTSRALEDIARKHGVPVFRSAVG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 373 FKWFVDGLFDGSFGFGGEESAG-----ASFLRfdgtpwstdkDGIIMCLLAAEITAVTGKNPQEHYDELaarfgaPSYNR 447
Cdd:cd05803 308 EANVVEKMKEVDAVIGGEGNGGvilpdVHYGR----------DSLVGIALVLQLLAASGKPLSEIVDEL------PQYYI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 448 LQASATSAQKA---ALSKLSPEMVSASQLAGDpitarltaapgngasigGLKVMTDNGWFAARPSGTEDAYKIYcesflG 524
Cdd:cd05803 372 SKTKVTIAGEAlerLLKKLEAYFKDAEASTLD-----------------GLRLDSEDSWVHVRPSNTEPIVRII-----A 429
|
490
....*....|....
gi 1336437369 525 EAHRkqiEKEAVEI 538
Cdd:cd05803 430 EAPT---QDEAEAL 440
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
42-156 |
1.27e-13 |
|
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: 72.90 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 42 FGTSGHRGSAGRhNFNEQHILAIAQAIAEDRAKNGITGPCYVGKDTHaLSEPAFISVLEV-LAANGVDVIVQennGFTPT 120
Cdd:cd05802 2 FGTDGIRGVANE-PLTPELALKLGRAAGKVLGKGGGRPKVLIGKDTR-ISGYMLESALAAgLTSAGVDVLLL---GVIPT 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1336437369 121 PAIsnAILVHNKKggplAD-GIVITPSHNPPEDGGIK 156
Cdd:cd05802 77 PAV--AYLTRKLR----ADaGVVISASHNPFEDNGIK 107
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
42-162 |
4.55e-05 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 45.90 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 42 FGTSGHRGSAGRHNFNEQHILAIAQAIAEDRAKNGiTGPCYVGKDTHaLSEPAFISVLEV-LAANGVDVivqennGFT-- 118
Cdd:PRK10887 4 FGTDGIRGKVGQAPITPDFVLKLGWAAGKVLARQG-RPKVLIGKDTR-ISGYMLESALEAgLAAAGVDV------LLTgp 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1336437369 119 -PTPAIsnAILVHNKKggpLADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:PRK10887 76 mPTPAV--AYLTRTLR---AEAGIVISASHNPYYDNGIKFFSADG 115
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
41-162 |
4.92e-05 |
|
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: 46.04 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336437369 41 KFGTSGHRG--SAGRHNFNEQHILAIAQAIAEDRAKNGItgpcYVGKDTHAlSEPAF-ISVLEVLAANGVDVIvqeNNGF 117
Cdd:cd03088 1 KFGTSGLRGlvTDLTDEVCYAYTRAFLQHLESKFPGDTV----AVGRDLRP-SSPRIaAACAAALRDAGFRVV---DCGA 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1336437369 118 TPTPAISNAILVHNkkggplADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:cd03088 73 VPTPALALYAMKRG------APAIMVTGSHIPADRNGLKFYRPDG 111
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
140-163 |
2.03e-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: 44.12 E-value: 2.03e-04
10 20
....*....|....*....|....
gi 1336437369 140 GIVITPSHNPPEDGGIKYNPPNGG 163
Cdd:cd03086 38 GVMITASHNPVEDNGVKIVDPDGE 61
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
140-188 |
2.85e-04 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 43.49 E-value: 2.85e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1336437369 140 GIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVENRANELLASGLQGV 188
Cdd:PTZ00302 78 GVMITASHNPIQDNGVKIIDPDGGMLEESWEKICTDFANARTGEDLVSV 126
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
489-539 |
2.42e-03 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 36.86 E-value: 2.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1336437369 489 GASIGGLKVMTDNGW-FAARPSGTEDAYKIYCESFlGEAHRKQIEKEAVEIV 539
Cdd:pfam00408 20 KVFADAEKILGEDGRrLDVRPSGTEPVLRVMVEGD-SDEELARLADEIADLL 70
|
|
| |
