|
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: 1047.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 2 AIHNRAGQPAQQSDLINVAQLTAQYYVLKPEAGNAEHAVKFGTSGHRGSAARHSFNEPHILAIAQAIAEERAKNGITGPC 81
Cdd:TIGR01132 1 AIHPRAGQPAQQEDLINVAQLVAQYYVLQPEAGNAAHAVKFGTSGHRGSALRGTFNEPHILAIAQAIAEYRAAQGITGPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 82 YVGKDTHALSEPAFISVLEVLAANGVDVIVQENNGFTPTPAVSNAILVHNKKGGPLADGIVITPSHNPPEDGGIKYNPPN 161
Cdd:TIGR01132 81 YIGKDTHALSEPAFISVLEVLAANGVEVIVQENNGFTPTPAVSHAILTHNKKGEPLADGIVITPSHNPPEDGGIKYNPPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 162 GGPADTNVTKVVEDRANALLADGLKGVKRISLDEAMASGHVKEQDLVQPFVEGLADIVDMAAIQKAGLTLGVDPLGGSGI 241
Cdd:TIGR01132 161 GGPADTEATQAIEDRANALLANGLKGVKRLPLAQALASGTVKAHDLVQPYVDGLADIVDMAAIQKAGLRLGVDPLGGSGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 242 EYWKRIGEYYNLNLTIVNDQVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTPAGLMNP 321
Cdd:TIGR01132 241 DYWKRIAEKYNLNLTLVNPQVDPTFRFMTLDKDGKIRMDCSSPYAMAGLLALRDKYDLAFGNDPDYDRHGIVTPAGLMNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 322 NHYLAVAINYLFQHRPQWGKDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFD 401
Cdd:TIGR01132 321 NHYLAVAINYLFQHRPQWGGDVAVGKTLVSSAMIDRVVADLGRQLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 402 GTPWSTDKDGIIMCLLAAEITAVTGKNPQEHYNELAKRFGAPSYNRLQAAATSAQKAALSKLSPEMVSASTLAGDPITAR 481
Cdd:TIGR01132 401 GTPWSTDKDGIIMCLLAAEITAVTGKNPQQHYNELAAKFGAPSYNRIQAPATSAQKARLKKLSPEMVSATTLAGDPITAR 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128664 482 LTAAPGNGASIGGLKVMTDNGWFAARPSGTEDAYKIYCESFLGEEHRKQIEKEAVEIVSEVLK 544
Cdd:TIGR01132 481 LTAAPGNGAAIGGLKVTTDNGWFAARPSGTEDVYKIYCESFKGEEHLKQIEKEAVEIVSEVLK 543
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
3-544 |
0e+00 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 1030.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 3 IHNRAGQPAQQSDLINVAQLTAQYYVLKPEAGNAEHAVKFGTSGHRGSAARHSFNEPHILAIAQAIAEERAKNGITGPCY 82
Cdd:PRK07564 1 IHPRAGQPAQPSDLINVPRLVSAYYTLKPDPTNPFQDVKFGTSGHRGSSLQPSFNENHILAIFQAICEYRGKQGITGPLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 83 VGKDTHALSEPAFISVLEVLAANGVDVIVQENNGFTPTPAVSNAILVHNKKGGPLADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:PRK07564 81 VGGDTHALSEPAIQSALEVLAANGVGVVIVGRGGYTPTPAVSHAILKYNGRGGGLADGIVITPSHNPPEDGGIKYNPPNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 163 GPADTNVTKVVEDRANALLADGLKGVKRISLDEAMASGHVKEQDLVQPFVEGLADIVDMAAIQKAGLTLGVDPLGGSGIE 242
Cdd:PRK07564 161 GPADTDVTDAIEARANELLAYGLKGVKRIPLDRALASMTVEVIDPVADYVEDLENVFDFDAIRKAGLRLGVDPLGGATGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 243 YWKRIGEYYNLNLTIVNDQVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTPAGLMNPN 322
Cdd:PRK07564 241 YWKAIAERYGLDLTVVNAPVDPTFNFMPLDDDGKIRMDCSSPYAMAGLLALKDAFDLAFANDPDGDRHGIVTPGGLMNPN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 323 HYLAVAINYLFQHRPQWGKDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFDG 402
Cdd:PRK07564 321 HYLAVAIAYLFHHRPGWRAGAGVGKTLVSSAMIDRVAAKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESAGASFLRRDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 403 TPWSTDKDGIIMCLLAAEITAVTGKNPQEHYNELAKRFGAPSYNRLQAAATSAQKAALSKLSPEMVSASTLAGDPITARL 482
Cdd:PRK07564 401 SVWTTDKDGLIAVLLAAEILAVTGKSPSEIYRELWARFGRPYYSRHDAPATPEQKAALRKLSPELVGATELAGDPIDASL 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128664 483 TAAPGNGASIGGLKVMTDNGWFAARPSGTEDAYKIYCESFLGEEHRKQIEKEAVEIVSEVLK 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: 1027.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 20 AQLTAQYYVLKPEAGNAEHAVKFGTSGHRGSAARHSFNEPHILAIAQAIAEERAKNGITGPCYVGKDTHALSEPAFISVL 99
Cdd:cd05801 1 PRLITAYYTLKPDPSNPAQRVAFGTSGHRGSSLKGSFNEAHILAISQAICDYRKSQGITGPLFLGKDTHALSEPAFISAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 100 EVLAANGVDVIVQENNGFTPTPAVSNAILVHNKKG-GPLADGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRAN 178
Cdd:cd05801 81 EVLAANGVEVIIQQNDGYTPTPVISHAILTYNRGRtEGLADGIVITPSHNPPEDGGFKYNPPHGGPADTDITRWIEKRAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 179 ALLADGLKGVKRISLDEAMASGHVKEQDLVQPFVEGLADIVDMAAIQKAGLTLGVDPLGGSGIEYWKRIGEYYNLNLTIV 258
Cdd:cd05801 161 ALLANGLKGVKRIPLEAALASGYTHRHDFVTPYVADLGNVIDMDAIRKSGLRLGVDPLGGASVPYWQPIAEKYGLNLTVV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 259 NDQVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTP-AGLMNPNHYLAVAINYLFQHRP 337
Cdd:cd05801 241 NPKVDPTFRFMTLDHDGKIRMDCSSPYAMAGLLKLKDKFDLAFANDPDADRHGIVTPsAGLMNPNHYLSVAIDYLFTHRP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 338 QWGKDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFDGTPWSTDKDGIIMCLL 417
Cdd:cd05801 321 LWNKSAGVGKTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDGLLDGSLGFGGEESAGASFLRRDGTVWTTDKDGIIMCLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 418 AAEITAVTGKNPQEHYNELAKRFGAPSYNRLQAAATSAQKAALSKLSPEMVSASTLAGDPITARLTAAPGNGASIGGLKV 497
Cdd:cd05801 401 AAEILAVTGKDPGQLYQELTERFGEPYYARIDAPATPEQKARLKKLSPEQVTATELAGDPILAKLTRAPGNGASIGGLKV 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 16128664 498 MTDNGWFAARPSGTEDAYKIYCESFLGEEHRKQIEKEAVEIV 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: 1004.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 3 IHNRAGQPAQQSDLINVAQLTAQYYVLKPEAGNAEHAVKFGTSGHRGSAARHSFNEPHILAIAQAIAEERAKNGITGPCY 82
Cdd:COG0033 1 LHPRAGQPAPPSDLIDVPRLVSAYYTIKPDPTTPFQDVKFGTSGHRGSSLKGSFNEPHILAITQAIFDYRKAQGITGPLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 83 VGKDTHALSEPAFISVLEVLAANGVDVIVQENNGFTPTPAVSNAILVHNKKGGPLADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:COG0033 81 LGGDTHALSEPAIQTALEVLAANGVGVVIVGQGGYTPTPAVSHAILKYNRGTSGAADGIVLTPSHNPPEDGGIKYNPPNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 163 GPADTNVTKVVEDRANALLADGLKGVKRISLDEAMASGHVKEQDLVQPFVEGLADIVDMAAIQKAGLTLGVDPLGGSGIE 242
Cdd:COG0033 161 GPADEDVTDAIEARANEILEYGLADVKRVPLDRAGTAMTVEVIDPVADYVELLESVFDFDAIRAAGFRIGFDPLGGATGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 243 YWKRIGEYYNLNLTIVNDQVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTP-AGLMNP 321
Cdd:COG0033 241 YWKAIAERYGLDLTVVNGVPDPDFRFMTLDWDGGIRMDPSSPYAMASLIAGKDAPDFAAANDGDGDRHGIVTPrGGLMNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 322 NHYLAVAINYLFQHRPQWGKDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFD 401
Cdd:COG0033 321 NHYLAVAIAYLFTHRPGWAALAGVGKTMVTSSAIDRVAAALGRPLYEVPVGFKWFVNGLDAGSLGFGGEESAGASFLRRD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 402 GTPWSTDKDGIIMCLLAAEITAVTGKNPQEHYNELAKRFGAPSYNRLQAAATSAQKAALSKLSPEMVSASTLAGDPITAR 481
Cdd:COG0033 401 GSVWTTDKDGLWAVLLAAEILAVTGKSPAEIYRELWARFGRPYYSRHDAEATDEQKARLAKLSGEQVGATTLAGEDIFAY 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128664 482 LTAAPGNGASIGGLKVMTDNGWFAARPSGTEDAYKIYCESFLGEEHRKQIEKEAVEIVSEVLK 544
Cdd:COG0033 481 LDPAPGNGAAIGGLKVVTENGWFAARPSGTETTYKIYAESFEGDEHLHQIDAEAADLVDAALA 543
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
41-539 |
2.55e-107 |
|
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: 325.08 E-value: 2.55e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 41 KFGTSGHRGSAARHsFNEPHILAIAQAIAEErakngitgpcyvgkdthalsepafisvlevlaangvdvivqenngftpt 120
Cdd:cd03084 1 IFGTSGVRGVVGDD-ITPETAVALGQAIGST------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 121 pavsnailvhnkkggplaDGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANALLADGLKGVKrisldeamASG 200
Cdd:cd03084 31 ------------------GGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYE--------LGG 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 201 HVKEQDLVQPFVEGLADIVDMAAIQKAGLTLGVDPLGGSGIEYWKRIGEYYNLNLTIVNDQVDQTFrfmhldkdGAIRMD 280
Cdd:cd03084 85 SVKAVDILQRYFEALKKLFDVAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNF--------GNINPD 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 281 CSSECAMAGLLALRD--KFDLAFANDPDYDRHGIVTP-AGLMNPNHYLAVAINYLFQHrpqWGKDVAVGKTLVSSAMIDR 357
Cdd:cd03084 157 PGSETNLKQLLAVVKaeKADFGVAFDGDADRLIVVDEnGGFLDGDELLALLAVELFLT---FNPRGGVVKTVVSSGALDK 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 358 VVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFdgtpwSTDKDGIIMCLLAAEITAVTGKNPQEHYNELA 437
Cdd:cd03084 234 VAKKLGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGVIFPEF-----HPGRDGISAALLLLEILANLGKSLSELFSELP 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 438 KRFgapsYNRLQAAatsaqkaalsklspemvsastlagdpitarltaapgngasigglkvmtdnGWFAARPSGTEDAYKI 517
Cdd:cd03084 309 RYY----YIRLKVR--------------------------------------------------GWVLVRASGTEPAIRI 334
|
490 500
....*....|....*....|..
gi 16128664 518 YCESFLgEEHRKQIEKEAVEIV 539
Cdd:cd03084 335 YAEADT-QEDVEQIKKEARELV 355
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
40-539 |
1.09e-89 |
|
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: 283.29 E-value: 1.09e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 40 VKFGTSGHRGSAARhSFNEPHILAIAQAIAEERAKNGITGP-CYVGKDTHALSEPAFISVLEVLAANGVDVIVQEnnGFT 118
Cdd:cd05800 1 IKFGTDGWRGIIAE-DFTFENVRRVAQAIADYLKEEGGGGRgVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSD--RPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 119 PTPAVSNAILVHNkkggpLADGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANALLADGLkgvkrisldEAMA 198
Cdd:cd05800 78 PTPAVSWAVKKLG-----AAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGL---------EARA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 199 SGHVKEQDLVQPFVEGLADIVDMAAIQKAGLTLGVDPLGGSGIEYWKRIGEYYNLNLTIVNDQVDQTFrfmhldkdGAIR 278
Cdd:cd05800 144 EGLIETIDPKPDYLEALRSLVDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLF--------GGIP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 279 MDCSSEcAMAGLLAL--RDKFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRPQWGkdvAVGKTLVSSAMI 355
Cdd:cd05800 216 PEPIEK-NLGELAEAvkEGGADLGLATDGDADRIGAVDEKGnFLDPNQILALLLDYLLENKGLRG---PVVKTVSTTHLI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 356 DRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFdgTPwstDKDGIIMCLLAAEITAVTGKNPQEHYNE 435
Cdd:cd05800 292 DRIAEKHGLPVYETPVGFKYIAEKMLEEDVLIGGEESGGLGIRGH--IP---ERDGILAGLLLLEAVAKTGKPLSELVAE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 436 LAKRFGAPSYNRL-QAAATSAQKAALSKLSPEmvSASTLAGDPITARLTaapgngasIGGLKVMTDNG-WFAARPSGTED 513
Cdd:cd05800 367 LEEEYGPSYYDRIdLRLTPAQKEAILEKLKNE--PPLSIAGGKVDEVNT--------IDGVKLVLEDGsWLLIRPSGTEP 436
|
490 500
....*....|....*....|....*.
gi 16128664 514 AYKIYCESFlGEEHRKQIEKEAVEIV 539
Cdd:cd05800 437 LLRIYAEAP-SPEKVEALLDAGKKLA 461
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
42-543 |
2.86e-62 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 211.21 E-value: 2.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 42 FGTSGHRGSAARHsFNEPHILAIAQAIAE---ERAKNGITgpcyVGKDTHALSEPAFISVLEVLAANGVDVIvqeNNGFT 118
Cdd:COG1109 7 FGTDGIRGIVGEE-LTPEFVLKLGRAFGTylkEKGGPKVV----VGRDTRLSSPMLARALAAGLASAGIDVY---DLGLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 119 PTPAVSNAILVHNKKGGpladgIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANAlladglkgvKRISLDEAMA 198
Cdd:COG1109 79 PTPALAFAVRHLGADGG-----IMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEK---------EDFRRAEAEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 199 SGHVKE-QDLVQPFVEGLADIVDmAAIQKAGLTLGVDPLGGSGIEYWKRIGEYYNLNLTIVNDQVDQTFRFMHLDKDgai 277
Cdd:COG1109 145 IGKVTRiEDVLEAYIEALKSLVD-EALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNPE--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 278 rmdcssECAMAGL--LALRDKFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRPqwGKDVAvgKTLVSSAM 354
Cdd:COG1109 221 ------PENLEDLieAVKETGADLGIAFDGDADRLGVVDEKGrFLDGDQLLALLARYLLEKGP--GGTVV--VTVMSSLA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 355 IDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLrfdgtPWSTDKDGIIMCLLAAEITAVTGKNPQEHYN 434
Cdd:COG1109 291 LEDIAEKHGGEVVRTKVGFKYIKEKMRETGAVLGGEESGGIIFP-----DFVPTDDGILAALLLLELLAKQGKSLSELLA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 435 ELakrfgaPSYNRLQAAATSAQKAALSKLSPEMVSASTLAGDPITarltaapgngasIGGLKV-MTDNGWFAARPSGTED 513
Cdd:COG1109 366 EL------PRYPQPEINVRVPDEEKIGAVMEKLREAVEDKEELDT------------IDGVKVdLEDGGWVLVRPSGTEP 427
|
490 500 510
....*....|....*....|....*....|
gi 16128664 514 AYKIYCESFlGEEHRKQIEKEAVEIVSEVL 543
Cdd:COG1109 428 LLRVYAEAK-DEEEAEELLAELAELVEEAL 456
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
320-440 |
5.50e-42 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 146.44 E-value: 5.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 320 NPNHYLAVAINYLFQHRpQWGKDVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLR 399
Cdd:pfam02880 1 DGDQILALLAKYLLEQG-KLPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 16128664 400 FDgtpwsTDKDGIIMCLLAAEITAVTGKNPQEHYNELAKRF 440
Cdd:pfam02880 80 HA-----TTKDGILAALLVLEILARTGKSLSELLEELPEKY 115
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
40-179 |
4.18e-39 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 139.28 E-value: 4.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 40 VKFGTSGHRGSAARHSFNEPHILAIAQAIAEERAKNGITGPCYVGKDTHALSEPAFISVLEVLAANGVDVIVqenNGFTP 119
Cdd:pfam02878 2 QLFGTSGIRGKVGVGELTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVIL---LGLLP 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 120 TPAVSNAILVHNKKGgpladGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANA 179
Cdd:pfam02878 79 TPAVSFATRKLKADG-----GIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
42-544 |
3.05e-30 |
|
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: 123.01 E-value: 3.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 42 FGTSGHRGSAARhSFNEPHILAIAQAIAEERAKNGITgpcyVGKDTHAlSEPAFIS-VLEVLAANGVDVIvqeNNGFTPT 120
Cdd:TIGR03990 4 FGTSGIRGIVGE-ELTPELALKVGKAFGTYLRGGKVV----VGRDTRT-SGPMLENaVIAGLLSTGCDVV---DLGIAPT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 121 PAVSNAILVHNKKGGpladgIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANAlladglKGVKRISLDEamaSG 200
Cdd:TIGR03990 75 PTLQYAVRELGADGG-----IMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAES------GDFERADWDE---IG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 201 HVKEQ-DLVQPFVEGLADIVDMAAIQKAGLTLGVDPLGGSGieywKRIGEY--YNLNLTI--VNDQVDQTFrfmhldkdg 275
Cdd:TIGR03990 141 TVTSDeDAIDDYIEAILDKVDVEAIRKKGFKVVVDCGNGAG----SLTTPYllRELGCKVitLNCQPDGTF--------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 276 AIRMdcsSECAMAGLLALRD-----KFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRpqwGKDVAVgkTL 349
Cdd:TIGR03990 208 PGRN---PEPTPENLKDLSAlvkatGADLGIAHDGDADRLVFIDEKGrFIGGDYTLALFAKYLLEHG---GGKVVT--NV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 350 VSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFDGTPwstdkDGIIMCLLAAEITAVTGKNP 429
Cdd:TIGR03990 280 SSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGAVFGGEGNGGWIFPDHHYCR-----DGLMAAALFLELLAEEGKPL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 430 QEhyneLAKRFgaPSYNRLQAAATSAQKAALSKLspEMVSASTLAGDPITarltaapgngasIGGLKVMTDNGWFAARPS 509
Cdd:TIGR03990 355 SE----LLAEL--PKYPMSKEKVELPDEDKEEVM--EAVEEEFADAEIDT------------IDGVRIDFEDGWVLVRPS 414
|
490 500 510
....*....|....*....|....*....|....*
gi 16128664 510 GTEDAYKIYCESflgeehrkQIEKEAVEIVSEVLK 544
Cdd:TIGR03990 415 GTEPIVRIYAEA--------KTEERAEELLEEGRS 441
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
42-539 |
3.98e-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: 108.04 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 42 FGTSGHRGSaarhsFNEPH----ILAIAQAIAEERAKngitGPCYVGKDTHAlSEPAFISVLE-VLAANGVDVIVQennG 116
Cdd:cd03087 2 FGTSGIRGV-----VGEELtpelALKVGKALGTYLGG----GTVVVGRDTRT-SGPMLKNAVIaGLLSAGCDVIDI---G 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 117 FTPTPAVSNAILVHNKKGgpladgIVITPSHNPPEDGGIKYNPPNGgpadTNVTKVVEDRANALLADGlkGVKRISLDEa 196
Cdd:cd03087 69 IVPTPALQYAVRKLGDAG------VMITASHNPPEYNGIKLVNPDG----TEFSREQEEEIEEIIFSE--RFRRVAWDE- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 197 maSGHVKEQD-LVQPFVEGLADIVDMAAiqKAGLTLGVDPLGGSGIEYWKRIGEYYNLNLTIVNDQVDQTFrfmhldkdg 275
Cdd:cd03087 136 --VGSVRREDsAIDEYIEAILDKVDIDG--GKGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFF--------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 276 AIRMdcsSECAMAGLLALRD-----KFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRpqwGKDVAVgkTL 349
Cdd:cd03087 203 PGRP---PEPTPENLSELMElvratGADLGIAHDGDADRAVFVDEKGrFIDGDKLLALLAKYLLEEG---GGKVVT--PV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 350 VSSAMIDRVVNDLGRKLVEVPVGfKWFVDGLFDGSFG-FGGEESAGASFLRFDGTPwstdkDGIIMCLLAAEITAVTGKn 428
Cdd:cd03087 275 DASMLVEDVVEEAGGEVIRTPVG-DVHVAEEMIENGAvFGGEPNGGWIFPDHQLCR-----DGIMTAALLLELLAEEKP- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 429 pqehyneLAKRFGA-PSYNRLQAAATSAQKAAlsklsPEMVSAstlagdpITARLTAAPGNGASIGGLKVMTDNGWFAAR 507
Cdd:cd03087 348 -------LSELLDElPKYPLLREKVECPDEKK-----EEVMEA-------VEEELSDADEDVDTIDGVRIEYEDGWVLIR 408
|
490 500 510
....*....|....*....|....*....|..
gi 16128664 508 PSGTEDAYKIYCESfLGEEHRKQIEKEAVEIV 539
Cdd:cd03087 409 PSGTEPKIRITAEA-KTEERAKELLEEGRSKV 439
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
41-447 |
8.00e-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: 105.00 E-value: 8.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 41 KFGTSGHRGSAArhSFNEPH-----ILAIAQAIAEERAKNGITGpcyVGKDTHALSEPAFISVLEVLAANGVDVIVQENN 115
Cdd:cd03085 12 KPGTSGLRKKVK--VFQQPNylenfVQSIFNALPPEKLKGATLV---VGGDGRYYNKEAIQIIIKIAAANGVGKVVVGQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 116 GFTPTPAVSNAILVHNKKGGpladgIVITPSHNP--PE-DGGIKYNPPNGGPADTNVTKVVEDRANAL----LADGLK-- 186
Cdd:cd03085 87 GLLSTPAVSAVIRKRKATGG-----IILTASHNPggPEgDFGIKYNTSNGGPAPESVTDKIYEITKKIteykIADDPDvd 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 187 ----GVKRISLDEAMasghVKEQDLVQPFVEGLADIVDMAAIQKA----GLTLGVDPLGGSGIEYWKRI-GEYYNLNL-T 256
Cdd:cd03085 162 lskiGVTKFGGKPFT----VEVIDSVEDYVELMKEIFDFDAIKKLlsrkGFKVRFDAMHGVTGPYAKKIfVEELGAPEsS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 257 IVNDQVDQTFRFMHLD------KDGAIRMDcssecamagllalRDKFDLAFANDPDYDRHGIVTPAGLMNPNHYLAV--- 327
Cdd:cd03085 238 VVNCTPLPDFGGGHPDpnltyaKDLVELMK-------------SGEPDFGAASDGDGDRNMILGKGFFVTPSDSVAViaa 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 328 ---AINYLFQHRPQwgkdvAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDgLFD-GSFGFGGEESAGAsflrfdGT 403
Cdd:cd03085 305 nakLIPYFYKGGLK-----GVARSMPTSGALDRVAKKLGIPLFETPTGWKFFGN-LMDaGKLSLCGEESFGT------GS 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 16128664 404 PWSTDKDGI--IMCLLAaeITAVTGKNPQEHYNELAKRFGAPSYNR 447
Cdd:cd03085 373 DHIREKDGLwaVLAWLS--ILAHRNVSVEDIVKEHWQKYGRNFYTR 416
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
41-412 |
4.31e-21 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 97.03 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 41 KFGTSGHRGSAArhSFNEPHIL-----AIAQAIAEERAKNGITGpcyVGKDTHALSEPAFISVLEVLAANGVDVIVQENN 115
Cdd:PLN02307 24 KPGTSGLRKKVK--VFMQENYLanfvqALFNALPAEKVKGATLV---LGGDGRYFNKEAIQIIIKIAAANGVRRVWVGQN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 116 GFTPTPAVSNAIlvHNKKGGPLADGIVITPSHNP--P-EDGGIKYNPPNGGPADTNVTKVVEDRANAL----LADGLK-- 186
Cdd:PLN02307 99 GLLSTPAVSAVI--RERDGSKANGGFILTASHNPggPeEDFGIKYNYESGQPAPESITDKIYGNTLTIkeykMAEDIPdv 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 187 -----GVKRISLDEAMAsghVKEQDLVQPFVEGLADIVDMAAIQK----AGLTLGVDPLGGSGIEYWKRI---------- 247
Cdd:PLN02307 177 dlsavGVTKFGGPEDFD---VEVIDPVEDYVKLMKSIFDFELIKKllsrPDFTFCFDAMHGVTGAYAKRIfveelgapes 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 248 ------------GEYYNLNLTIVNDQVDQtfrfMHLDKDGAIrmdcssecamagllalRDKFDLAFANDPDYDRHGIVTP 315
Cdd:PLN02307 254 sllncvpkedfgGGHPDPNLTYAKELVKR----MGLGKTSYG----------------DEPPEFGAASDGDGDRNMILGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 316 AGLMNPNHYLAV-------AINYlFQHRPQwgkdvAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGSFGFG 388
Cdd:PLN02307 314 RFFVTPSDSVAIiaanaqeAIPY-FSGGLK-----GVARSMPTSAALDVVAKKLNLPFFEVPTGWKFFGNLMDAGKLSIC 387
|
410 420
....*....|....*....|....
gi 16128664 389 GEESAGAsflrfdGTPWSTDKDGI 412
Cdd:PLN02307 388 GEESFGT------GSDHIREKDGI 405
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
210-317 |
2.28e-17 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 77.72 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 210 PFVEGLADIVDMAAIQKAGLTLGVDPLGGSGIEYWKRIGEYYNLNLTIVNDQVDQTFRFmhldkdGAIRMDCSSECAMAG 289
Cdd:pfam02879 1 AYIDHLLELVDSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPT------RAPNPEEPEALALLI 74
|
90 100
....*....|....*....|....*...
gi 16128664 290 LLALRDKFDLAFANDPDYDRHGIVTPAG 317
Cdd:pfam02879 75 ELVKSVGADLGIATDGDADRLGVVDERG 102
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
63-512 |
8.33e-17 |
|
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: 82.95 E-value: 8.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 63 AIAQAIAEERAKNGItGPCYVGKDTHaLSEPAFISVL-EVLAANGVDVIvqeNNGFTPTPAVSNAIlVHNKKGGpladGI 141
Cdd:cd03089 22 AIGRAFGSWLLEKGA-KKVVVGRDGR-LSSPELAAALiEGLLAAGCDVI---DIGLVPTPVLYFAT-FHLDADG----GV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 142 VITPSHNPPEDGGIKYNPPNGGPADTNVTKvVEDRANALLADGLKGvkrisldeamaSGHVKEQDLVQPFVEGLADIVDm 221
Cdd:cd03089 92 MITASHNPPEYNGFKIVIGGGPLSGEDIQA-LRERAEKGDFAAATG-----------RGSVEKVDILPDYIDRLLSDIK- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 222 aaIQKAGLTLGVDPLGGSGIEYWKRIGEYYNLNLTIVNDQVDQTFRFMHLDKdgairmdcSSECAMAGLLA--LRDKFDL 299
Cdd:cd03089 159 --LGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDP--------TDPENLEDLIAavKENGADL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 300 AFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRPqwGKDVaVGKTLVSSAMIDrVVNDLGRKLVEVPVGFKWFVD 378
Cdd:cd03089 229 GIAFDGDGDRLGVVDEKGeIIWGDRLLALFARDILKRNP--GATI-VYDVKCSRNLYD-FIEEAGGKPIMWKTGHSFIKA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 379 GLFDGSFGFGGEESA----GASFLRFDgtpwstdkDGIIMCLLAAEITAVTGKNPQEHYNELAKRFGAPSYNrlqaaats 454
Cdd:cd03089 305 KMKETGALLAGEMSGhiffKDRWYGFD--------DGIYAALRLLELLSKSGKTLSELLADLPKYFSTPEIR-------- 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128664 455 aqkaalSKLSPEMVSAstlAGDPITARLTAAPGNGASIGGLKVMTDNGWFAARPSGTE 512
Cdd:cd03089 369 ------IPVTEEDKFA---VIERLKEHFEFPGAEIIDIDGVRVDFEDGWGLVRASNTE 417
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
42-156 |
2.18e-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: 72.13 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 42 FGTSGHRGSAarhsfNEP----HILAIAQAIAEERAKNGITGPCYVGKDTHaLSEPAFISVLEV-LAANGVDVIVQennG 116
Cdd:cd05802 2 FGTDGIRGVA-----NEPltpeLALKLGRAAGKVLGKGGGRPKVLIGKDTR-ISGYMLESALAAgLTSAGVDVLLL---G 72
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 16128664 117 FTPTPAVsnAILVHNKKggplAD-GIVITPSHNPPEDGGIK 156
Cdd:cd05802 73 VIPTPAV--AYLTRKLR----ADaGVVISASHNPFEDNGIK 107
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
60-521 |
1.86e-11 |
|
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: 66.18 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 60 HILAIAQAIAEERAKngitGPCYVGKDTHALSEPAFISVLEVLAANGVDVIvqeNNGFTPTPAVSnaILVHNKKGgplAD 139
Cdd:cd05803 23 YVAAFATWQPERTKG----GKIVVGRDGRPSGPMLEKIVIGALLACGCDVI---DLGIAPTPTVQ--VLVRQSQA---SG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 140 GIVITPSHNPPEDGGIKYNPPNG---GPADtnVTKVVE-DRANALLADGLKGVKRISLDEAMASGHVKEqdlvqpfVEGL 215
Cdd:cd05803 91 GIIITASHNPPQWNGLKFIGPDGeflTPDE--GEEVLScAEAGSAQKAGYDQLGEVTFSEDAIAEHIDK-------VLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 216 ADiVDMAAIQKAGLTLGVDPLGGSGIEYWKRIGEyyNLNLTIVndqvdqtfrFMHLDKDGAIRMdcSSECAMAGLLAL-- 293
Cdd:cd05803 162 VD-VDVIKIRERNFKVAVDSVNGAGGLLIPRLLE--KLGCEVI---------VLNCEPTGLFPH--TPEPLPENLTQLca 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 294 ---RDKFDLAFANDPDYDRHGIVTPAG-LMNPNHYLAVAINYLFQHRPQWGKDVavgKTLVSSAMIDRVVNDLGRKLVEV 369
Cdd:cd05803 228 avkESGADVGFAVDPDADRLALVDEDGrPIGEEYTLALAVDYVLKYGGRKGPVV---VNLSTSRALEDIARKHGVPVFRS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 370 PVGFKWFVDGLFDGSFGFGGEESAG-----ASFLR--FDGTpwstdkdGIIMCLLAAE---ITAVTGKNPQehYNELAKR 439
Cdd:cd05803 305 AVGEANVVEKMKEVDAVIGGEGNGGvilpdVHYGRdsLVGI-------ALVLQLLAASgkpLSEIVDELPQ--YYISKTK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 440 FGAPSYNRlqaaatsaqKAALSKLSPEMVSASTLAGDpitarltaapgngasigGLKVMTDNGWFAARPSGTEDAYKIYC 519
Cdd:cd05803 376 VTIAGEAL---------ERLLKKLEAYFKDAEASTLD-----------------GLRLDSEDSWVHVRPSNTEPIVRIIA 429
|
..
gi 16128664 520 ES 521
Cdd:cd05803 430 EA 431
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
41-162 |
1.18e-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: 47.97 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 41 KFGTSGHRG---------SAArhsfnepHILAIAQAIAEERAKNGItgpcYVGKDTHAlSEPAF-ISVLEVLAANGVDVI 110
Cdd:cd03088 1 KFGTSGLRGlvtdltdevCYA-------YTRAFLQHLESKFPGDTV----AVGRDLRP-SSPRIaAACAAALRDAGFRVV 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 16128664 111 vqeNNGFTPTPAVSNAILVHNkkggplADGIVITPSHNPPEDGGIKYNPPNG 162
Cdd:cd03088 69 ---DCGAVPTPALALYAMKRG------APAIMVTGSHIPADRNGLKFYRPDG 111
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
140-195 |
2.28e-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: 47.20 E-value: 2.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128664 140 GIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANALLADGLKGVKRISLDE 195
Cdd:cd03086 38 GVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDDELLVLVLMLISVK 93
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
140-188 |
4.22e-05 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 46.19 E-value: 4.22e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 16128664 140 GIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANALLADGLKGV 188
Cdd:PTZ00302 78 GVMITASHNPIQDNGVKIIDPDGGMLEESWEKICTDFANARTGEDLVSV 126
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
83-162 |
1.51e-04 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 44.36 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 83 VGKDTHaLSEPAFISVLEV-LAANGVDVivqennGFT---PTPAVsnAILVHNKKggpLADGIVITPSHNPPEDGGIKYN 158
Cdd:PRK10887 44 IGKDTR-ISGYMLESALEAgLAAAGVDV------LLTgpmPTPAV--AYLTRTLR---AEAGIVISASHNPYYDNGIKFF 111
|
....
gi 16128664 159 PPNG 162
Cdd:PRK10887 112 SADG 115
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
489-539 |
1.34e-03 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 37.63 E-value: 1.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 16128664 489 GASIGGLKVMTDNGW-FAARPSGTEDAYKIYCESFlGEEHRKQIEKEAVEIV 539
Cdd:pfam00408 20 KVFADAEKILGEDGRrLDVRPSGTEPVLRVMVEGD-SDEELARLADEIADLL 70
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
140-202 |
1.88e-03 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 41.16 E-value: 1.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128664 140 GIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVEDRANALLADGLKGVKR-------ISLDEAMASGHV 202
Cdd:PLN02895 61 GLMITASHNPVSDNGVKIVDPSGGMLPQAWEPFADALANAPDPDALVQLIRefvkkenIPAVGGNPPAEV 130
|
|
| |
