|
Name |
Accession |
Description |
Interval |
E-value |
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
44-558 |
0e+00 |
|
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: 648.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 44 RLAFGTAGLRGVVGAGPMRMNRLVIRQTTAGLGQYLLAQVKDAASRGVVIGFDGRHDSRTFAHDAASVLTAMGIKVRLTA 123
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRHNSREFAELTAAVLAANGIKVYLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 124 KVAATPLVAFGVKHFEAAAGIVVTASHNPPQYNGYKVYWGNGAQIIPPHDSGIAACIDKaaNEELPWLEQSEATKQGKLI 203
Cdd:cd05799 81 DLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEA--VLEPLDIKFEEALDSGLIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 204 WLQDDFYQDYRrgvfhADVLQHKTAPER-----VSLAYTAMHGVGAEMAKTVLKDAGFTQVYSVAAQEKPDGDFPTVKFP 278
Cdd:cd05799 159 YIGEEIDDAYL-----EAVKKLLVNPELnegkdLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKFP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 279 NPEEKGAMDLVIAEAKQHQALLACANDPDADRLAVAVRRDDGEYQMLTGDQVGALLGHYLLS------KAPANQRLLgTT 352
Cdd:cd05799 234 NPEEPGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEqrkekgKLPKNPVIV-KT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 353 IVSSTLLSKIAKAKGGEFYTTLTGFKWLTNVGMQRQSDSNKFLFAYEEALGYTVGSMVWDKDGLSALVAFAQLTAELAAQ 432
Cdd:cd05799 313 IVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAYLKAQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 433 DKTIWDRLEELYRDYGLHLNTQVSIALKPGT-----PDIGAHLRANPpesiagmavlvtedlksaerryadgrreiielp 507
Cdd:cd05799 393 GKTLLDRLDELYEKYGYYKEKTISITFEGKEgpekiKAIMDRLRNNP--------------------------------- 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1011991059 508 asDVLTFHLEGGARVIVRPSGTEPKIKCYYEVVEPmqasDSLADAESRARA 558
Cdd:cd05799 440 --NVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVGK----KTLEEAEKKLDA 484
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
1-556 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 538.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 1 MNTHLELQLKHWLDIDPDPKTRDELLSLKAEGNETELAARFAGRLAFGTAGLRGVVGAGPMRMNRLVIRQTTAGLGQYLL 80
Cdd:PTZ00150 1 MMESLEAQVELWLKWDKDPETRKEIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 81 AQV-KDAASRGVVIGFDGRHDSRTFAHDAASVLTAMGIKVRLTAKVAATPLVAFGVKHFEAAAGIVVTASHNPPQYNGYK 159
Cdd:PTZ00150 81 ETFgQALKSRGVVIGYDGRYHSRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 160 VYWGNGAQIIPPHDSGIAACIDkaANEElPWLEQSEATKQGKLI----WLQDDFYQDYRrgvfhADVLQHKTAPERVSLA 235
Cdd:PTZ00150 161 VYWSNGAQIIPPHDKNISAKIL--SNLE-PWSSSWEYLTETLVEdplaEVSDAYFATLK-----SEYNPACCDRSKVKIV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 236 YTAMHGVGAEMAKTVLKDAGFTQVYSVAAQEKPDGDFPTVKFPNPEE-KGAMDLVIAEAKQHQALLACANDPDADRLAVA 314
Cdd:PTZ00150 233 YTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEgKGALKLSMETAEAHGSTVVLANDPDADRLAVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 315 VRRDDGEYQmLTGDQVGALLGHYLLSKA-----PANQRLLGTTIVSSTLLSKIAKAKGGEFYTTLTGFKWLTNVGMQRQS 389
Cdd:PTZ00150 313 EKLNNGWKI-FTGNELGALLAWWAMKRYrrqgiDKSKCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIELNA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 390 -DSNKFLFAYEEALGYTVGSMVWDKDGLSALVAFAQLTAELAAQDKTIWDRLEELYRDYGLHL-NTQVSIALKPG-TPDI 466
Cdd:PTZ00150 392 eNGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYHFtNNSYYICYDPSrIVSI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 467 GAHLRANP--PESIAGMAVLVTEDLKSA-ERRYADGRREIIELPASDVLTFHLEGGARVIVRPSGTEPKIKCYYE--VVE 541
Cdd:PTZ00150 472 FNDIRNNGsyPTKLGGYPVTRIRDLTTGyDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLKWYAElsGTK 551
|
570
....*....|....*
gi 1011991059 542 PMQASDSLADAESRA 556
Cdd:PTZ00150 552 DEAVEKELAALVDEV 566
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
47-560 |
4.40e-123 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 370.30 E-value: 4.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 47 FGTAGLRGVVGAGpmrMNRLVIRQTTAGLGQYLlaqvKDAASRGVVIGFDGRHDSRTFAHDAASVLTAMGIKVRLtAKVA 126
Cdd:COG1109 7 FGTDGIRGIVGEE---LTPEFVLKLGRAFGTYL----KEKGGPKVVVGRDTRLSSPMLARALAAGLASAGIDVYD-LGLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 127 ATPLVAFGVKHFEAAAGIVVTASHNPPQYNGYKVYWGNGAQIIPPHDSGIAACIDKaaneelPWLEQSEATKQGKLIWLq 206
Cdd:COG1109 79 PTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEK------EDFRRAEAEEIGKVTRI- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 207 DDFYQDYRRGVfhADVLQHKTAPERVSLAYTAMHGVGAEMAKTVLKDAGFTqVYSVAAQekPDGDFPTVkFPNPEEKgAM 286
Cdd:COG1109 152 EDVLEAYIEAL--KSLVDEALRLRGLKVVVDCGNGAAGGVAPRLLRELGAE-VIVLNAE--PDGNFPNH-NPNPEPE-NL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 287 DLVIAEAKQHQALLACANDPDADRLAVAvrrdDGEYQMLTGDQVGALLGHYLLSKAPANqrLLGTTIVSSTLLSKIAKAK 366
Cdd:COG1109 225 EDLIEAVKETGADLGIAFDGDADRLGVV----DEKGRFLDGDQLLALLARYLLEKGPGG--TVVVTVMSSLALEDIAEKH 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 367 GGEFYTTLTGFKWLTNVgMQRqsdsNKFLFAYEEALGYTVGSMVWDKDGlsaLVAFAQLTAELAAQDKTiwdrLEELYRD 446
Cdd:COG1109 299 GGEVVRTKVGFKYIKEK-MRE----TGAVLGGEESGGIIFPDFVPTDDG---ILAALLLLELLAKQGKS----LSELLAE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 447 YGLHLNTQVSIALkPGTPDIGAHLRAnppesiagmavlVTEDLKSAErryadgrreiiELPASDVLTFHLEGGARVIVRP 526
Cdd:COG1109 367 LPRYPQPEINVRV-PDEEKIGAVMEK------------LREAVEDKE-----------ELDTIDGVKVDLEDGGWVLVRP 422
|
490 500 510
....*....|....*....|....*....|....
gi 1011991059 527 SGTEPKIKCYYEVVEPMQASDSLADAESRARAAL 560
Cdd:COG1109 423 SGTEPLLRVYAEAKDEEEAEELLAELAELVEEAL 456
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
47-564 |
2.32e-65 |
|
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: 220.50 E-value: 2.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 47 FGTAGLRGVVGAGpmrMNRLVIRQTTAGLGQYLLAqvKDAASRGVVIGFDGRHDSRTFAHDAASVLTAMGIKVRLTAKVA 126
Cdd:cd05800 3 FGTDGWRGIIAED---FTFENVRRVAQAIADYLKE--EGGGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSDRPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 127 ATPLVAFGVKHFEAAAGIVVTASHNPPQYNGYKVYWGNGAQIIPPHDSGIAACIDKAANEELPWLEQSEATKQGklIWlq 206
Cdd:cd05800 78 PTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAEGLIETID--PK-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 207 dDFYQDYRRGVFHADVLqhKTAPERVslAYTAMHGVGAEMAKTVLKDAGFtQVYSVAAQEKPD-GDFPtvkfPNPEEKGA 285
Cdd:cd05800 154 -PDYLEALRSLVDLEAI--REAGLKV--VVDPMYGAGAGYLEELLRGAGV-DVEEIRAERDPLfGGIP----PEPIEKNL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 286 MDLvIAEAKQHQALLACANDPDADRLAVAVrrDDGEYqmLTGDQVGALLGHYLLskapANQRLLGT---TIVSSTLLSKI 362
Cdd:cd05800 224 GEL-AEAVKEGGADLGLATDGDADRIGAVD--EKGNF--LDPNQILALLLDYLL----ENKGLRGPvvkTVSTTHLIDRI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 363 AKAKGGEFYTTLTGFKWLTNVGMQrqsdsNKFLFAYEEALGYTVGSMVWDKDG-LSALvafaqLTAELAAQ-DKTIWDRL 440
Cdd:cd05800 295 AEKHGLPVYETPVGFKYIAEKMLE-----EDVLIGGEESGGLGIRGHIPERDGiLAGL-----LLLEAVAKtGKPLSELV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 441 EELYRDYGLHLNTQVSIALKP-GTPDIGAHLRANPPESIAGMAVLVTEDLksaerryaDGrreiielpasdvLTFHLEGG 519
Cdd:cd05800 365 AELEEEYGPSYYDRIDLRLTPaQKEAILEKLKNEPPLSIAGGKVDEVNTI--------DG------------VKLVLEDG 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1011991059 520 ARVIVRPSGTEPKIKCYYEvvepmqasdslADAESRARAALDAFV 564
Cdd:cd05800 425 SWLLIRPSGTEPLLRIYAE-----------APSPEKVEALLDAGK 458
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
44-182 |
3.13e-49 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 167.02 E-value: 3.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 44 RLAFGTAGLRGVVGAGPMrmNRLVIRQTTAGLGQYLLAQVKDaasRGVVIGFDGRHDSRTFAHDAASVLTAMGIKVRLtA 123
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGEL--TPEFALKLGQAIASYLRAQGGG---GKVVVGRDTRYSSRELARALAAGLASNGVEVIL-L 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1011991059 124 KVAATPLVAFGVKHFEAAAGIVVTASHNPPQYNGYKVYWGNGAQIIPPHDSGIAACIDK 182
Cdd:pfam02878 75 GLLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
119-538 |
1.97e-46 |
|
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: 166.76 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 119 VRLTAKVAATPLVAFGVKH-FEAAAGIVVTASHNPPQYNGYKVYWGNGAQIIPPHDSGIAACIDKaanEELPWLEQSEAT 197
Cdd:cd03084 7 VRGVVGDDITPETAVALGQaIGSTGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEK---EDEPSAVAYELG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 198 KQGKLIWLQDDFYQDYRRGVFHAdvlqhKTAPERVSLAYTAMHGVGAEMAKTVLKDAGfTQVYSVAAQekPDGDFPTVKF 277
Cdd:cd03084 84 GSVKAVDILQRYFEALKKLFDVA-----ALSNKKFKVVVDSVNGVGGPIAPQLLEKLG-AEVIPLNCE--PDGNFGNINP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 278 PNPEEKGAMDLvIAEAKQHQALLACANDPDADRLAVAvrrdDGEYQMLTGDQVGALLGHYLLSKAPANQRLLGTTiVSST 357
Cdd:cd03084 156 DPGSETNLKQL-LAVVKAEKADFGVAFDGDADRLIVV----DENGGFLDGDELLALLAVELFLTFNPRGGVVKTV-VSSG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 358 LLSKIAKAKGGEFYTTLTGFKWLTNvGMQRqsdsNKFLFAYEEALGYTVGSMVWDKDGLSALVAFAQLtaeLAAQDKTIW 437
Cdd:cd03084 230 ALDKVAKKLGIKVIRTKTGFKWVGE-AMQE----GDVVLGGEESGGVIFPEFHPGRDGISAALLLLEI---LANLGKSLS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 438 DRLEELYRDYGLHLNTqvsialkpgtpdigahlranppesiagmavlvtedlksaerryadgrreiielpasdvltfhle 517
Cdd:cd03084 302 ELFSELPRYYYIRLKV---------------------------------------------------------------- 317
|
410 420
....*....|....*....|.
gi 1011991059 518 gGARVIVRPSGTEPKIKCYYE 538
Cdd:cd03084 318 -RGWVLVRASGTEPAIRIYAE 337
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
47-565 |
3.74e-45 |
|
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: 165.38 E-value: 3.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 47 FGTAGLRGVVGAGpmrMNRLVIRQTTAGLGQYLlaqvkdAASRgVVIGFDGRHDSRTFAHDAASVLTAMGIKVrLTAKVA 126
Cdd:TIGR03990 4 FGTSGIRGIVGEE---LTPELALKVGKAFGTYL------RGGK-VVVGRDTRTSGPMLENAVIAGLLSTGCDV-VDLGIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 127 ATPLVAFGVKHFEAAAGIVVTASHNPPQYNGYKVYWGNGAQIIPPHDSGIAACIDKAANEELPWLEQSEATKqgkliwlQ 206
Cdd:TIGR03990 73 PTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAESGDFERADWDEIGTVTS-------D 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 207 DDFYQDYRRGVF-HADVLQHKTAPERVslAYTAMHGVGAEMAKTVLKDAGfTQVYSVAAQekPDGDFPTvKFPNPEEKGA 285
Cdd:TIGR03990 146 EDAIDDYIEAILdKVDVEAIRKKGFKV--VVDCGNGAGSLTTPYLLRELG-CKVITLNCQ--PDGTFPG-RNPEPTPENL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 286 MDLvIAEAKQHQALLACANDPDADRLAVAvrrdDGEYQMLTGDQVGALLGHYLLSKAPANqrlLGTTIVSSTLLSKIAKA 365
Cdd:TIGR03990 220 KDL-SALVKATGADLGIAHDGDADRLVFI----DEKGRFIGGDYTLALFAKYLLEHGGGK---VVTNVSSSRAVEDVAER 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 366 KGGEFYTTLTGfkwLTNV--GMQRQSDsnkfLFAYEEAlgytvGSMVWDK-----DGLSALVAFAQLtaeLAAQDKTiwd 438
Cdd:TIGR03990 292 HGGEVIRTKVG---EVNVaeKMKEEGA----VFGGEGN-----GGWIFPDhhycrDGLMAAALFLEL---LAEEGKP--- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 439 rLEELYRDYGLHLNTQVSIALKpgtpdigahlRANPPESIAGMAvlvtEDLKSAERRYADGRReiIELPASDVLtfhleg 518
Cdd:TIGR03990 354 -LSELLAELPKYPMSKEKVELP----------DEDKEEVMEAVE----EEFADAEIDTIDGVR--IDFEDGWVL------ 410
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1011991059 519 garviVRPSGTEPKIKCYYEvvepmqasdslADAESRARAALDAFVS 565
Cdd:TIGR03990 411 -----VRPSGTEPIVRIYAE-----------AKTEERAEELLEEGRS 441
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
47-565 |
1.01e-37 |
|
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: 144.64 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 47 FGTAGLRGVVGagpmrmnrlviRQTTAGLGQYL-LAQVKDAASRGVVIGFDGRHDSRTFAHDAASVLTAMGIKVrLTAKV 125
Cdd:cd03087 2 FGTSGIRGVVG-----------EELTPELALKVgKALGTYLGGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDV-IDIGI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 126 AATPLVAFGVKHFeAAAGIVVTASHNPPQYNGYKVYWGNGAQIIPPHDSGIAACIDKAANEELPWLEQSEATKQGKLIwl 205
Cdd:cd03087 70 VPTPALQYAVRKL-GDAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSERFRRVAWDEVGSVRREDSAI-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 206 qddfyQDYRRGVFhADVLQHKTAPERVslAYTAMHGVGAEMAKTVLKDAGfTQVYSVAAQekPDGDFPTVKF-PNPEE-K 283
Cdd:cd03087 147 -----DEYIEAIL-DKVDIDGGKGLKV--VVDCGNGAGSLTTPYLLRELG-CKVITLNAN--PDGFFPGRPPePTPENlS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 284 GAMDLVIAEAkqhqALLACANDPDADRlAVAVrrdDGEYQMLTGDQVGALLGHYLLSKAPanqRLLGTTIVSSTLLSKIA 363
Cdd:cd03087 216 ELMELVRATG----ADLGIAHDGDADR-AVFV---DEKGRFIDGDKLLALLAKYLLEEGG---GKVVTPVDASMLVEDVV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 364 KAKGGEFYTTLTGfkwLTNVGmqRQSDSNKFLFAYEEAlgytvGSMVWDK-----DGLSAlvafAQLTAELAAQDKTIWD 438
Cdd:cd03087 285 EEAGGEVIRTPVG---DVHVA--EEMIENGAVFGGEPN-----GGWIFPDhqlcrDGIMT----AALLLELLAEEKPLSE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 439 RLEELYRDYglhlNTQVSIALKpgtpdigahlRANPPESIAGMAVLVTEDLKSAErrYADGRReiIELPASDVLtfhleg 518
Cdd:cd03087 351 LLDELPKYP----LLREKVECP----------DEKKEEVMEAVEEELSDADEDVD--TIDGVR--IEYEDGWVL------ 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1011991059 519 garviVRPSGTEPKIKCYYEvvepmqasdslADAESRARAALDAFVS 565
Cdd:cd03087 407 -----IRPSGTEPKIRITAE-----------AKTEERAKELLEEGRS 437
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
75-533 |
3.89e-35 |
|
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: 137.26 E-value: 3.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 75 LGQYLLAQVKDAASRGVVIGFDGRHDSRTFAHDAASVLTAMGIKVrLTAKVAATPLVAFGVKHFEAAAGIVVTASHNPPQ 154
Cdd:cd03089 23 IGRAFGSWLLEKGAKKVVVGRDGRLSSPELAAALIEGLLAAGCDV-IDIGLVPTPVLYFATFHLDADGGVMITASHNPPE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 155 YNGYKVYWGNGaqiiPPHDSGIAACIDKAANEELPwleqsEATKQGKLIwlQDDFYQDYrrgvfHADVLQH-KTAPERVS 233
Cdd:cd03089 102 YNGFKIVIGGG----PLSGEDIQALRERAEKGDFA-----AATGRGSVE--KVDILPDY-----IDRLLSDiKLGKRPLK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 234 LAYTAMHGVGAEMAKTVLKDAGFTqVYSVAAQekPDGDFPTvKFPNPEEKGAMDLVIAEAKQHQALLACANDPDADRLAV 313
Cdd:cd03089 166 VVVDAGNGAAGPIAPQLLEALGCE-VIPLFCE--PDGTFPN-HHPDPTDPENLEDLIAAVKENGADLGIAFDGDGDRLGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 314 AvrrdDGEYQMLTGDQVGALLGHYLLSKAPanqrllGTTIV----SSTLLSKIAKAKGGEFYTTLTGFKWLTNVGMQRQS 389
Cdd:cd03089 242 V----DEKGEIIWGDRLLALFARDILKRNP------GATIVydvkCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKETGA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 390 D-----SNKFLFAyEEALGYtvgsmvwDkdglSALVAFAQLTAELAAQDKTIWDRLEELyRDYglhlntqvsialkPGTP 464
Cdd:cd03089 312 LlagemSGHIFFK-DRWYGF-------D----DGIYAALRLLELLSKSGKTLSELLADL-PKY-------------FSTP 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011991059 465 DIgahlraNPPesiagmavlVTEDLKSA-----ERRYADGRREIIELpasDVLTFHLEGGaRVIVRPSGTEPKI 533
Cdd:cd03089 366 EI------RIP---------VTEEDKFAvierlKEHFEFPGAEIIDI---DGVRVDFEDG-WGLVRASNTEPVL 420
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
47-533 |
4.63e-30 |
|
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: 122.59 E-value: 4.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 47 FGTAGLRGVVGAgPMrMNRLVIRqttagLGQYLLAQVKDAASRG-VVIGFDGRHDSRTFAHDAASVLTAMGIKVrLTAKV 125
Cdd:cd05802 2 FGTDGIRGVANE-PL-TPELALK-----LGRAAGKVLGKGGGRPkVLIGKDTRISGYMLESALAAGLTSAGVDV-LLLGV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 126 AATPLVAFGVKHFEAAAGIVVTASHNPPQYNGYKVYWGNGAQIipPHD--SGIAACIDKaaneelPWLEQSEATKQGKLI 203
Cdd:cd05802 74 IPTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKL--PDEveEEIEALIDK------ELELPPTGEKIGRVY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 204 WLQD--DFYQDYRRGVFHADVLQhktapeRVSLAYTAMHGVGAEMAKTVLKDAGfTQVYSVAAQekPDGDfptvkfpNPE 281
Cdd:cd05802 146 RIDDarGRYIEFLKSTFPKDLLS------GLKIVLDCANGAAYKVAPEVFRELG-AEVIVINNA--PDGL-------NIN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 282 EK-GAMDL-VIAEA-KQHQALLACANDPDADRLaVAVrrdDGEYQMLTGDQVGALLGHYLLSKapanQRLLGTTIVSSTL 358
Cdd:cd05802 210 VNcGSTHPeSLQKAvLENGADLGIAFDGDADRV-IAV---DEKGNIVDGDQILAICARDLKER----GRLKGNTVVGTVM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 359 ----LSKIAKAKGGEFYTtltgfkwlTNVGmqrqsdsNKFLFAYEEALGYTVG---S---MVWDK----DG-LSALvafa 423
Cdd:cd05802 282 snlgLEKALKELGIKLVR--------TKVG-------DRYVLEEMLKHGANLGgeqSghiIFLDHsttgDGlLTAL---- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 424 QLTAELAAQDKTiwdrLEELYRDygLHLNTQVSIALKPGtpdigahlRANPPESIAGmavlVTEDLKSAERRyadgrrei 503
Cdd:cd05802 343 QLLAIMKRSGKS----LSELASD--MKLYPQVLVNVRVK--------DKKALLENPR----VQAAIAEAEKE-------- 396
|
490 500 510
....*....|....*....|....*....|
gi 1011991059 504 ielpasdvltfhLEGGARVIVRPSGTEPKI 533
Cdd:cd05802 397 ------------LGGEGRVLVRPSGTEPLI 414
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
44-562 |
3.25e-29 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 121.78 E-value: 3.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 44 RLAFGTAGLRGVVGAGpmRMNRLVIRQTTAGLGQYllaqvkdAASRGV----VIGFDGRHDSRTFAHDAASVLTAMGIKV 119
Cdd:PRK07564 37 DVKFGTSGHRGSSLQP--SFNENHILAIFQAICEY-------RGKQGItgplFVGGDTHALSEPAIQSALEVLAANGVGV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 120 RLTAK--VAATPLV-----AFGVKHFEAAAGIVVTASHNPPQYNGYKVYWGNGAqiipPHDSGIAACIDKAANE------ 186
Cdd:PRK07564 108 VIVGRggYTPTPAVshailKYNGRGGGLADGIVITPSHNPPEDGGIKYNPPNGG----PADTDVTDAIEARANEllaygl 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 187 -ELPWLEQSEATKQGKLIwlQDDFYQDYrrgvfhADVLQH-------KTAPerVSLAYTAMHGVGAEMAKTVLKDAGF-- 256
Cdd:PRK07564 184 kGVKRIPLDRALASMTVE--VIDPVADY------VEDLENvfdfdaiRKAG--LRLGVDPLGGATGPYWKAIAERYGLdl 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 257 TQVysvaaQEKPDgdfPTVKF----------PNPEEKGAMDLVIAEAKQHQalLACANDPDADR---------------L 311
Cdd:PRK07564 254 TVV-----NAPVD---PTFNFmpldddgkirMDCSSPYAMAGLLALKDAFD--LAFANDPDGDRhgivtpgglmnpnhyL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 312 AVAVrrddgeyqmltgdqvgallgHYLLSKAP--ANQRLLGTTIVSSTLLSKIAKAKGGEFYTTLTGFKWLTNvGMqrqs 389
Cdd:PRK07564 324 AVAI--------------------AYLFHHRPgwRAGAGVGKTLVSSAMIDRVAAKLGRKLYEVPVGFKWFVN-GL---- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 390 DSNKFLFAYEEALGYTV----GSmVW--DKDGLsALVAFAqltAE-LAAQDKTIWDRLEELYRDYGLHLNTQVSIalkPG 462
Cdd:PRK07564 379 DDGSLGFGGEESAGASFlrrdGS-VWttDKDGL-IAVLLA---AEiLAVTGKSPSEIYRELWARFGRPYYSRHDA---PA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 463 TPDIGAHLRANPPESIaGMAVL----VTEDLKSAERRYA--DGRReiielpasdVLTfhlEGGaRVIVRPSGTEPKIKCY 536
Cdd:PRK07564 451 TPEQKAALRKLSPELV-GATELagdpIDASLTEAPGNGAaiGGLK---------VVT---ENG-WFAARPSGTETTYKIY 516
|
570 580
....*....|....*....|....*.
gi 1011991059 537 YEVVEPmqaSDSLADAESRARAALDA 562
Cdd:PRK07564 517 AESFEG---DEHLHQIQKEAQEIVAD 539
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
51-563 |
7.96e-27 |
|
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: 113.56 E-value: 7.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 51 GLRGVVGAGpmrMNRLVIRQTTAGLGQYLLAqvKDAASRgVVIGFDGRHDSRTFAHDAASVLTAMGIKVrLTAKVAATPL 130
Cdd:cd05803 6 GIRGIVGEG---LTPEVITRYVAAFATWQPE--RTKGGK-IVVGRDGRPSGPMLEKIVIGALLACGCDV-IDLGIAPTPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 131 VAFGVKHFEAAAGIVVTASHNPPQYNGYKvYWGNGAQIIPPHDSgiAACIDKAANEELPWleqsEATKQGKLIWLQDDFY 210
Cdd:cd05803 79 VQVLVRQSQASGGIIITASHNPPQWNGLK-FIGPDGEFLTPDEG--EEVLSCAEAGSAQK----AGYDQLGEVTFSEDAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 211 QDYRRGVFH-ADVLQHKTAPERVSLAYTAMHGVGAEMAKTVLKDAGftqVYSVAAQEKPDGDFPTVKFPNPEE-KGAMDL 288
Cdd:cd05803 152 AEHIDKVLAlVDVDVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLG---CEVIVLNCEPTGLFPHTPEPLPENlTQLCAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 289 ViaeaKQHQALLACANDPDADRLAVAvrRDDGEY------QMLTGDQVGALLGHyllsKAPanqrlLGTTIVSSTLLSKI 362
Cdd:cd05803 229 V----KESGADVGFAVDPDADRLALV--DEDGRPigeeytLALAVDYVLKYGGR----KGP-----VVVNLSTSRALEDI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 363 AKAKGGEFYTTLTGfkwLTNVGMQRQsdSNKFLFAYEEALGytvgsmVWDKD---GLSALVAFAQLTAELAAQDKTIwDR 439
Cdd:cd05803 294 ARKHGVPVFRSAVG---EANVVEKMK--EVDAVIGGEGNGG------VILPDvhyGRDSLVGIALVLQLLAASGKPL-SE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 440 LEELYRDYGLHlNTQVSIalkpgtpdigahlranPPESIAGMAVLVTEDLKSAERRYADGrreiielpasdvLTFHLEGG 519
Cdd:cd05803 362 IVDELPQYYIS-KTKVTI----------------AGEALERLLKKLEAYFKDAEASTLDG------------LRLDSEDS 412
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1011991059 520 aRVIVRPSGTEPKIKCYYEvvepmqasdslADAESRARAALDAF 563
Cdd:cd05803 413 -WVHVRPSNTEPIVRIIAE-----------APTQDEAEALADRF 444
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
225-314 |
1.02e-21 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 90.04 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 225 HKTAPERVSLAYTAMHGVGAEMAKTVLKDAGFtqvYSVAAQEKPDGDFPTvKFPNPEEKGAMDLVIAEAKQHQALLACAN 304
Cdd:pfam02879 13 EALKKRGLKVVYDPLHGVGGGYLPELLKRLGC---DVVEENCEPDPDFPT-RAPNPEEPEALALLIELVKSVGADLGIAT 88
|
90
....*....|
gi 1011991059 305 DPDADRLAVA 314
Cdd:pfam02879 89 DGDADRLGVV 98
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
108-538 |
1.83e-20 |
|
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: 95.01 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 108 AASVLTAMGIKVRLTAK--VAATPLVAFGV-----KHFEAAA-GIVVTASHNPPQYNGYKVYWGNGAqiipPHDSGIAAC 179
Cdd:cd05801 79 ALEVLAANGVEVIIQQNdgYTPTPVISHAIltynrGRTEGLAdGIVITPSHNPPEDGGFKYNPPHGG----PADTDITRW 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 180 IDKAANEELpwleqSEATKQGKLIWLQD----------DFYQDYRRGVfhADVLQ-HKTAPERVSLAYTAMHGVGAEMAK 248
Cdd:cd05801 155 IEKRANALL-----ANGLKGVKRIPLEAalasgythrhDFVTPYVADL--GNVIDmDAIRKSGLRLGVDPLGGASVPYWQ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 249 TVLKDAGF--TQVysvaaQEKPDgdfPTVKFPNPEEKG----------AMDLVIAEAKQHQalLACANDPDADR------ 310
Cdd:cd05801 228 PIAEKYGLnlTVV-----NPKVD---PTFRFMTLDHDGkirmdcsspyAMAGLLKLKDKFD--LAFANDPDADRhgivtp 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 311 ----------LAVAVrrddgeyqmltgdqvgallgHYLLSKAPA-NQRL-LGTTIVSSTLLSKIAKAKGGEFYTTLTGFK 378
Cdd:cd05801 298 saglmnpnhyLSVAI--------------------DYLFTHRPLwNKSAgVGKTLVSSSMIDRVAAALGRKLYEVPVGFK 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 379 WLTNVGMQRqsdsnKFLFAYEEALGYTV---GSMVW--DKDGLsalvAFAQLTAELAAQ-DKTIWDRLEELYRDYGLHLN 452
Cdd:cd05801 358 WFVDGLLDG-----SLGFGGEESAGASFlrrDGTVWttDKDGI----IMCLLAAEILAVtGKDPGQLYQELTERFGEPYY 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 453 TQVSIALKPGTPDIGAHLRAN--PPESIAGMAVLVTEDlksaerrYADGRREIIelpasdvltfhleGGARVI------- 523
Cdd:cd05801 429 ARIDAPATPEQKARLKKLSPEqvTATELAGDPILAKLT-------RAPGNGASI-------------GGLKVTtangwfa 488
|
490
....*....|....*
gi 1011991059 524 VRPSGTEPKIKCYYE 538
Cdd:cd05801 489 ARPSGTEDVYKIYAE 503
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
326-447 |
7.20e-19 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 82.50 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 326 TGDQVGALLGHYLLS-KAPANQRLLGTTIVSSTLLSKIAKAKGGEFYTTLTGFKWLTNvGMQRqsdsNKFLFAYEEALGY 404
Cdd:pfam02880 1 DGDQILALLAKYLLEqGKLPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKE-KMRE----EGALFGGEESGHI 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1011991059 405 TVGSMVWDKDGlsaLVAFAQLTAELAAQDKTIWDRLEELYRDY 447
Cdd:pfam02880 76 IFLDHATTKDG---ILAALLVLEILARTGKSLSELLEELPEKY 115
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
52-390 |
5.80e-14 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 74.71 E-value: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 52 LRGVVGAG----PMRMNRLVIRQTTAGLGQYLLAQVKDAASRGVVIGFDgrHDSRTFAHDAASVLTA----MGIKVRLTA 123
Cdd:PLN02371 73 IRGVAVEGvegePVTLTPPAVEAIGAAFAEWLLEKKKADGSGELRVSVG--RDPRISGPRLADAVFAglasAGLDVVDMG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 124 kVAATPLVAFGV--KHFEAAAGIVVTASHNPPQYNGYKVYWGNGAQiipphDSG-IAACIDKAANEELPW----LEQSEA 196
Cdd:PLN02371 151 -LATTPAMFMSTltEREDYDAPIMITASHLPYNRNGLKFFTKDGGL-----GKPdIKDILERAARIYKEWsdegLLKSSS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 197 TKQGKLIWLqdDFYQDY--------RRGVFHADvlqHKTAP-ERVSLAYTAMHGVGAEMAKTVLKDAGFTQVYSVAAQek 267
Cdd:PLN02371 225 GASSVVCRV--DFMSTYakhlrdaiKEGVGHPT---NYETPlEGFKIVVDAGNGAGGFFAEKVLEPLGADTSGSLFLE-- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 268 PDGDFPTvKFPNPEEKGAMDLVIAEAKQHQALLACANDPDADRLAVAvrrdDGEYQMLTGDQVGALLGHYLLSKAPanqr 347
Cdd:PLN02371 298 PDGMFPN-HIPNPEDKAAMSATTQAVLANKADLGIIFDTDVDRSAVV----DSSGREINRNRLIALMSAIVLEEHP---- 368
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1011991059 348 llGTTIV----SSTLLSKIAKAKGGEFYTTLTGFKWLTNVGMQRQSD 390
Cdd:PLN02371 369 --GTTIVtdsvTSDGLTTFIEKKGGKHHRFKRGYKNVIDKGVRLNSD 413
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
48-551 |
6.87e-12 |
|
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate (G-1-P) and glucose-6-phosphate (G-6-P) via a glucose 1,6-diphosphate intermediate, an important metabolic step in prokaryotes and eukaryotes. In one direction, G-1-P produced from sucrose catabolism is converted to G-6-P, the first intermediate in glycolysis. In the other direction, conversion of G-6-P to G-1-P generates a substrate for synthesis of UDP-glucose which is required for synthesis of a variety of cellular constituents including cell wall polymers and glycoproteins. The PGM1 family also includes a non-enzymatic PGM-related protein (PGM-RP) thought to play a structural role in eukaryotes, as well as pp63/parafusin, a phosphoglycoprotein that plays an important role in calcium-regulated exocytosis in ciliated protozoans. PGM1 belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100087 [Multi-domain] Cd Length: 548 Bit Score: 68.02 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 48 GTAGLRGVVGagpmrmnrlVIRQT--TAGLGQYLLAQVKDAASRG--VVIGFDGRHDSRTFAHDAASVLTAMGIKVRLTA 123
Cdd:cd03085 14 GTSGLRKKVK---------VFQQPnyLENFVQSIFNALPPEKLKGatLVVGGDGRYYNKEAIQIIIKIAAANGVGKVVVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 124 K--VAATPLVAFGVKHFEAAAGIVVTASHNPPQYN---GYKVYWGNGAqiiPPHDS------GIAACIDKAANEELPwle 192
Cdd:cd03085 85 QngLLSTPAVSAVIRKRKATGGIILTASHNPGGPEgdfGIKYNTSNGG---PAPESvtdkiyEITKKITEYKIADDP--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 193 QSEATKQGKLIWLQDDF----------YQDYRRGVFHADVLQHKTAPERVSLAYTAMHGVGAEMAKTVLKDA-GFTQVYS 261
Cdd:cd03085 159 DVDLSKIGVTKFGGKPFtvevidsvedYVELMKEIFDFDAIKKLLSRKGFKVRFDAMHGVTGPYAKKIFVEElGAPESSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 262 VAAQEKPDgdfptvkF----PNPEEKGAMDLViAEAKQHQALLACANDPDADRlavavrrddgeyQMLTG--------DQ 329
Cdd:cd03085 239 VNCTPLPD-------FggghPDPNLTYAKDLV-ELMKSGEPDFGAASDGDGDR------------NMILGkgffvtpsDS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 330 VgALLGHYlLSKAPANQR--LLGT--TIVSSTLLSKIAKAKGGEFYTTLTGFKWLTNVgMqrqsDSNKFLFAYEEALGyT 405
Cdd:cd03085 299 V-AVIAAN-AKLIPYFYKggLKGVarSMPTSGALDRVAKKLGIPLFETPTGWKFFGNL-M----DAGKLSLCGEESFG-T 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 406 VGSMVWDKDGLSALVAFAQLtaeLAAQDKTIWDRLEELYRDYGLHLNT-----QVS--IALKpgtpdIGAHLRANPPESI 478
Cdd:cd03085 371 GSDHIREKDGLWAVLAWLSI---LAHRNVSVEDIVKEHWQKYGRNFYTrydyeEVDseAANK-----MMDHLRALVSDLP 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 479 A-GMAVLVTEDLKSAER-RYADgrreiielPASDVLTFH------LEGGARVIVRPSGTEPK---IKCYYEVVEP----- 542
Cdd:cd03085 443 GvGKSGDKGYKVAKADDfSYTD--------PVDGSVSKKqglriiFEDGSRIIFRLSGTGSSgatIRLYIESYEKdpsky 514
|
570
....*....|
gi 1011991059 543 -MQASDSLAD 551
Cdd:cd03085 515 gLDAQVALKP 524
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
89-538 |
1.11e-09 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 60.73 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 89 RGVVIGFDGRHDSRTFAHDAASVLTAMGIKVrLTAKVAATPLVAFGVKHFEAAAGIVVTASHNPPQYNGYKVYwGNGAQI 168
Cdd:PRK15414 39 KTIVLGGDVRLTSETLKLALAKGLQDAGVDV-LDIGMSGTEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLV-REGARP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 169 IpPHDSGIAACIDKAANEELPWLEQseaTKQG--KLIWLQDDfYQDYRRGVFHADVLQhktapeRVSLAYTAMHGVGAEM 246
Cdd:PRK15414 117 I-SGDTGLRDVQRLAEANDFPPVDE---TKRGryQQINLRDA-YVDHLFGYINVKNLT------PLKLVINSGNGAAGPV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 247 AKTV---LKDAGfTQVYSVAAQEKPDGDFPTvKFPNPEEKGAMDLVIAEAKQHQALLACANDPDADRLAVAvrrdDGEYQ 323
Cdd:PRK15414 186 VDAIearFKALG-APVELIKVHNTPDGNFPN-GIPNPLLPECRDDTRNAVIKHGADMGIAFDGDFDRCFLF----DEKGQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 324 MLTGDQVGALLGHYLLSKAPanqrllGTTIVSSTLLS----KIAKAKGGEFYTTLTGFKWLTNvgMQRQSDSnkfLFAYE 399
Cdd:PRK15414 260 FIEGYYIVGLLAEAFLEKNP------GAKIIHDPRLSwntvDVVTAAGGTPVMSKTGHAFIKE--RMRKEDA---IYGGE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 400 EALGYTVGSMVWDKDGLSALVAFAQLtaeLAAQDKTiwdrLEELYRDyglhlntqvSIALKPGTPDIGAHLrANPPESIA 479
Cdd:PRK15414 329 MSAHHYFRDFAYCDSGMIPWLLVAEL---VCLKGKT----LGELVRD---------RMAAFPASGEINSKL-AQPVEAIN 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1011991059 480 gmavlvtedlkSAERRYAdgrREIIELPASDVLTFHLeGGARVIVRPSGTEPKIKCYYE 538
Cdd:PRK15414 392 -----------RVEQHFS---REALAVDRTDGISMTF-ADWRFNLRSSNTEPVVRLNVE 435
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
47-165 |
1.94e-07 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 53.60 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 47 FGTAGLRGVVGAGPMRMNrLVIRQTTAgLGQYLLAQvkdaASRGVVIGFDGRHDSRTFahDAA--SVLTAMGIKVRLTAK 124
Cdd:PRK10887 4 FGTDGIRGKVGQAPITPD-FVLKLGWA-AGKVLARQ----GRPKVLIGKDTRISGYML--ESAleAGLAAAGVDVLLTGP 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1011991059 125 VAaTPLVAFGVKHFEAAAGIVVTASHNPPQYNGYKVYWGNG 165
Cdd:PRK10887 76 MP-TPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADG 115
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
53-181 |
5.49e-07 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 52.29 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 53 RGVVGAGpmrMNRLVIRQTTAGLGQYllaqVKDAASRGVVIGFDGRHDSRTFAHDAASVLTAMGIKVrLTAKVAATPLVA 132
Cdd:PRK09542 7 RGVVGEQ---IDEDLVRDVGAAFARL----MRAEGATTVVIGHDMRDSSPELAAAFAEGVTAQGLDV-VRIGLASTDQLY 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1011991059 133 FGVKHFEAAaGIVVTASHNPPQYNGYKVYWGnGAQIIpPHDSGIAACID 181
Cdd:PRK09542 79 FASGLLDCP-GAMFTASHNPAAYNGIKLCRA-GAKPV-GQDTGLAAIRD 124
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
46-161 |
1.86e-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: 47.20 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 46 AFGTAGLRGVVGAgpmrMNRLVIRQTTAGLGQYLLAQvkdAASRGVVIGFDGRHDSRTFAHDAASVLTAMGIKVrLTAKV 125
Cdd:cd03088 1 KFGTSGLRGLVTD----LTDEVCYAYTRAFLQHLESK---FPGDTVAVGRDLRPSSPRIAAACAAALRDAGFRV-VDCGA 72
|
90 100 110
....*....|....*....|....*....|....*..
gi 1011991059 126 AATPLVAF-GVKHfeAAAGIVVTASHNPPQYNGYKVY 161
Cdd:cd03088 73 VPTPALALyAMKR--GAPAIMVTGSHIPADRNGLKFY 107
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
91-450 |
2.57e-05 |
|
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose pyrophosphorylase, is a bifunctional enzyme with both phosphomannose isomerase (PMI) activity and GDP-mannose phosphorylase (GMP) activity. The protein contains an N-terminal NTP transferase domain, an L-beta-H domain, and a C-terminal PGM-like domain that belongs to the alpha-D-phosphohexomutase superfamily. This subfamily is limited to bacteria and archaea. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this group appear to lack conserved residues necessary for metal binding and catalytic activity. Other members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100097 Cd Length: 441 Bit Score: 46.86 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 91 VVIGFDGRHDSRTFAHDAASVLTAMGIKVRlTAKVAATPLVAFGVKHFEAAAGIVVTASHNPPQYNGYKVYWGNGAQIip 170
Cdd:cd05805 37 VTVSRDASRASRMLKRALISGLLSTGVNVR-DLGALPLPVARYAIRFLGASGGIHVRTSPDDPDKVEIEFFDSRGLNI-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 171 phDSGIAACIDKA-ANEElpwLEQSEATKQGKLIWLQDDFYQdYRRGVFHA-DVLQHKTAPERVSLAYtaMHGVGAEMAK 248
Cdd:cd05805 114 --SRAMERKIENAfFRED---FRRAHVDEIGDITEPPDFVEY-YIRGLLRAlDTSGLKKSGLKVVIDY--AYGVAGIVLP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 249 TVLKDAGFTqVYSVAAQEKPDgdfptVKFPNPEEKGAMDLVIAEAKQHQALLACANDPDADRLAVAvrrdDGEYQMLTGD 328
Cdd:cd05805 186 GLLSRLGCD-VVILNARLDED-----APRTDTERQRSLDRLGRIVKALGADFGVIIDPNGERLILV----DEAGRVISDD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011991059 329 QVGALLGHYLLSKAPanqrllGTTIV----SSTLLSKIAKAKGGEFYTTLTGFKWLTNVgMQRQSdsnkfLFAYEEALGY 404
Cdd:cd05805 256 LLTALVSLLVLKSEP------GGTVVvpvtAPSVIEQLAERYGGRVIRTKTSPQALMEA-ALENV-----VLAGDGDGGF 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1011991059 405 TVgsmVWDKDGLSALVAFAQLTAELAAQDKTIWDRLEELYRDYGLH 450
Cdd:cd05805 324 IF---PEFHPGFDAIAALVKILEMLARTNISLSQIVDELPRFYVLH 366
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
509-556 |
4.15e-05 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 41.87 E-value: 4.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1011991059 509 SDVLTFHLEGGARVIVRPSGTEPKIKCYYEVVEPMQAsDSLADAESRA 556
Cdd:pfam00408 23 ADAEKILGEDGRRLDVRPSGTEPVLRVMVEGDSDEEL-ARLADEIADL 69
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
140-160 |
7.21e-04 |
|
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 (N-acetylglucosamine-phosphate mutase), is an essential enzyme found in eukaryotes that reversibly catalyzes the conversion of GlcNAc-6-phosphate into GlcNAc-1-phosphate as part of the UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthetic pathway. UDP-GlcNAc is an essential metabolite that serves as the biosynthetic precursor of many glycoproteins and mucopolysaccharides. AGM1 is a member of the alpha-D-phosphohexomutase superfamily, which catalyzes the intramolecular phosphoryl transfer of sugar substrates. The alpha-D-phosphohexomutases have four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100088 Cd Length: 513 Bit Score: 42.20 E-value: 7.21e-04
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
142-168 |
4.97e-03 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 39.64 E-value: 4.97e-03
10 20
....*....|....*....|....*..
gi 1011991059 142 AGIVVTASHNPPQYNGYKVYWGNGAQI 168
Cdd:PTZ00302 77 VGVMITASHNPIQDNGVKIIDPDGGML 103
|
|
| |
