|
Name |
Accession |
Description |
Interval |
E-value |
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
41-559 |
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: 700.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 41 DLEFGTAGLRGIVGVGTNRMNKYTVGKATQGLANYIVKN--NGQDKGVAIAYDSRNMSQEFSKLAALILNANGIKTYRFE 118
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKgpDAKNRGVVIGYDSRHNSREFAELTAAVLAANGIKVYLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 119 SLRPTPELSYTVRELGCISGIVITASHNPPKYNGYKVYWEDGAQISAPVDAGITEEVNAIKNYSDIKeitEEEATEKGLY 198
Cdd:cd05799 81 DLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIK---FEEALDSGLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 199 NTIGEEIDNKYIEYLKSIALNKEIDKeyGKDIKIVYTPLHGTGKKLALRILNELGFTNVHIVKEQAEPDGRFPTVSYPNP 278
Cdd:cd05799 158 KYIGEEIDDAYLEAVKKLLVNPELNE--GKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKFPNP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 279 EDPAAFELALKFAKEIQADIVVANDPDADRIGLHVRDsKTGDYILFNGNMIGLTVADYLINQKREKGLLDKNVALIKTIV 358
Cdd:cd05799 236 EEPGALDLAIELAKKVGADLILATDPDADRLGVAVKD-KDGEWRLLTGNEIGALLADYLLEQRKEKGKLPKNPVIVKTIV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 359 SSNMTDKICEENGVKLFEVLTGFKNVAAKIREFEKENsYKCIMGYEESYGCLVGDRVRDKDGIAALMLLSEAAALYKKQG 438
Cdd:cd05799 315 SSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGG-KKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAYLKAQG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 439 LTLWDNMQNMYKKYGYYKESQIAIVLEGAEGAQKIKDMMEDIRNNPpkeigkykvlklrdysngkikdcitgetynedlp 518
Cdd:cd05799 394 KTLLDRLDELYEKYGYYKEKTISITFEGKEGPEKIKAIMDRLRNNP---------------------------------- 439
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 524608991 519 ksNVIYFELENDFWGCIRPSGTEPKIKLYMGVKG-ENLEEAD 559
Cdd:cd05799 440 --NVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVGkKTLEEAE 479
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
5-559 |
4.30e-150 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 444.13 E-value: 4.30e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 5 KRYQEWLESDEiDEETKEELRKI--KNDETEIKDSFYKDLEFGTAGLRGIVGVGTNRMNKYTVGKATQGLANYIVK---N 79
Cdd:PTZ00150 7 AQVELWLKWDK-DPETRKEIEELlaSKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIEtfgQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 80 NGQDKGVAIAYDSRNMSQEFSKLAALILNANGIKTYRFESLRPTPELSYTVRELGCISGIVITASHNPPKYNGYKVYWED 159
Cdd:PTZ00150 86 ALKSRGVVIGYDGRYHSRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 160 GAQISAPVDAGITEEVNA-IKNYSDIKEITEEEATEKGLYntigeEIDNKYIEYLKSIALNKEIDkeyGKDIKIVYTPLH 238
Cdd:PTZ00150 166 GAQIIPPHDKNISAKILSnLEPWSSSWEYLTETLVEDPLA-----EVSDAYFATLKSEYNPACCD---RSKVKIVYTAMH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 239 GTGKKLALRILNELGFTNVHIVKEQAEPDGRFPTVSYPNPEDPA-AFELALKFAKEIQADIVVANDPDADRIGLHVRdsK 317
Cdd:PTZ00150 238 GVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEGKgALKLSMETAEAHGSTVVLANDPDADRLAVAEK--L 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 318 TGDYILFNGNMIGLTVADYLINQKREKGLLDKNVALIKTIVSSNMTDKICEENGVKLFEVLTGFKNVAAKIREFEKENSY 397
Cdd:PTZ00150 316 NNGWKIFTGNELGALLAWWAMKRYRRQGIDKSKCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIELNAENGL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 398 KCIMGYEESYGCLVGDRVRDKDGIAALMLLSEAAALYKKQGLTLWDNMQNMYKKYGYY-KESQIAIVLEGAegaqKIKDM 476
Cdd:PTZ00150 396 TTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYHfTNNSYYICYDPS----RIVSI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 477 MEDIRNNP--PKEIGKYKVLKLRDYSNGKIKDCITGETYNEDLPKSNVIYFELENDFWGCIRPSGTEPKIKLYMGVKGEN 554
Cdd:PTZ00150 472 FNDIRNNGsyPTKLGGYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLKWYAELSGTK 551
|
....*
gi 524608991 555 LEEAD 559
Cdd:PTZ00150 552 DEAVE 556
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
44-573 |
3.38e-135 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 401.12 E-value: 3.38e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 44 FGTAGLRGIVGVGtnrMNKYTVGKATQGLANYIVKNNGqdKGVAIAYDSRNMSQEFSKLAALILNANGIKTYRFEsLRPT 123
Cdd:COG1109 7 FGTDGIRGIVGEE---LTPEFVLKLGRAFGTYLKEKGG--PKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLG-LVPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 124 PELSYTVRELGCISGIVITASHNPPKYNGYKVYWEDGAQISAPVDAGITEEVNAiknysdiKEITEEEATEKGLYNTIgE 203
Cdd:COG1109 81 PALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEK-------EDFRRAEAEEIGKVTRI-E 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 204 EIDNKYIEYLKSiALNKEIDKeygKDIKIVYTPLHGTGKKLALRILNELGFtNVHIVKEQaePDGRFPTVSyPNPEdPAA 283
Cdd:COG1109 153 DVLEAYIEALKS-LVDEALRL---RGLKVVVDCGNGAAGGVAPRLLRELGA-EVIVLNAE--PDGNFPNHN-PNPE-PEN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 284 FELALKFAKEIQADIVVANDPDADRIGLHVRDsktGDYIlfNGNMIGLTVADYLInQKREKGlldknvALIKTIVSSNMT 363
Cdd:COG1109 224 LEDLIEAVKETGADLGIAFDGDADRLGVVDEK---GRFL--DGDQLLALLARYLL-EKGPGG------TVVVTVMSSLAL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 364 DKICEENGVKLFEVLTGFKNVAAKIREfekensYKCIMGYEESYGCLVGDRVRDKDGIAALMLLSEAAAlykKQGLTLWD 443
Cdd:COG1109 292 EDIAEKHGGEVVRTKVGFKYIKEKMRE------TGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLA---KQGKSLSE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 444 nmqnMYKKYGYYKESQIAIVLEGAEgaqKIKDMMEDIRNNPPKEigkykvlklrdysngkikdcitgetynEDLPKSNVI 523
Cdd:COG1109 363 ----LLAELPRYPQPEINVRVPDEE---KIGAVMEKLREAVEDK---------------------------EELDTIDGV 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 524608991 524 YFELENDFWGCIRPSGTEPKIKLYMGVKGEnlEEADILVEDLRNGMREIL 573
Cdd:COG1109 409 KVDLEDGGWVLVRPSGTEPLLRVYAEAKDE--EEAEELLAELAELVEEAL 456
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
43-547 |
3.66e-84 |
|
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: 269.81 E-value: 3.66e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 43 EFGTAGLRGIVGVGTNRMNkytVGKATQGLANYIVKNNGQDKGVAIAYDSRNMSQEFSKLAALILNANGIKTYRFESLRP 122
Cdd:cd05800 2 KFGTDGWRGIIAEDFTFEN---VRRVAQAIADYLKEEGGGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSDRPVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 123 TPELSYTVRELGCISGIVITASHNPPKYNGYKVYWEDGAQISAPVDAGITEEVNAIknysdikEITEEEATEKGLYNTIg 202
Cdd:cd05800 79 TPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASG-------EPPGLEARAEGLIETI- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 203 eEIDNKYIEYLKSIalnkeIDKEY--GKDIKIVYTPLHGTGKKLALRILNELGFTNVHIvkeQAEPDGRFPTVSyPNPED 280
Cdd:cd05800 151 -DPKPDYLEALRSL-----VDLEAirEAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEI---RAERDPLFGGIP-PEPIE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 281 PAAFELAlKFAKEIQADIVVANDPDADRIGlhVRDSKtGDYIlfNGNMIGLTVADYLINQKREKGlldknvALIKTIVSS 360
Cdd:cd05800 221 KNLGELA-EAVKEGGADLGLATDGDADRIG--AVDEK-GNFL--DPNQILALLLDYLLENKGLRG------PVVKTVSTT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 361 NMTDKICEENGVKLFEVLTGFKNVAAKIREfekensYKCIMGYEESYGCLVGDRVRDKDGIAALMLLSEAAALYKKqglT 440
Cdd:cd05800 289 HLIDRIAEKHGLPVYETPVGFKYIAEKMLE------EDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGK---P 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 441 LWDNMQNMYKKYG--YYKEsqIAIVLEgaegAQKIKDMMEDIRNNPPKEIGKYKVLKLRDYSNGKikdcitgetynedlp 518
Cdd:cd05800 360 LSELVAELEEEYGpsYYDR--IDLRLT----PAQKEAILEKLKNEPPLSIAGGKVDEVNTIDGVK--------------- 418
|
490 500
....*....|....*....|....*....
gi 524608991 519 ksnviyFELENDFWGCIRPSGTEPKIKLY 547
Cdd:cd05800 419 ------LVLEDGSWLLIRPSGTEPLLRIY 441
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
41-181 |
2.90e-49 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 167.02 E-value: 2.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 41 DLEFGTAGLRGIVGVGTNrmNKYTVGKATQGLANYIvKNNGQDKGVAIAYDSRNMSQEFSKLAALILNANGIKTYRFEsL 120
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGEL--TPEFALKLGQAIASYL-RAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLG-L 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524608991 121 RPTPELSYTVRELGCISGIVITASHNPPKYNGYKVYWEDGAQISAPVDAGITEEVNAIKNY 181
Cdd:pfam02878 77 LPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDFY 137
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
137-566 |
5.81e-48 |
|
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: 171.00 E-value: 5.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 137 SGIVITASHNPPKYNGYKVYWEDGAQISAPVDAGITEEVNAIKNYSDikeITEEEATEKGlyntiGEEIDNKYIEYLKSI 216
Cdd:cd03084 31 GGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSA---VAYELGGSVK-----AVDILQRYFEALKKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 217 ALNKEIDKeygKDIKIVYTPLHGTGKKLALRILNELGftnVHIVKEQAEPDGRFPTVsYPNPEDPAAFELALKFAKEIQA 296
Cdd:cd03084 103 FDVAALSN---KKFKVVVDSVNGVGGPIAPQLLEKLG---AEVIPLNCEPDGNFGNI-NPDPGSETNLKQLLAVVKAEKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 297 DIVVANDPDADRIGLHVRDSKtgdyiLFNGNMIGLTVADYLINQKrekgllDKNVALIKTIVSSNMTDKICEENGVKLFE 376
Cdd:cd03084 176 DFGVAFDGDADRLIVVDENGG-----FLDGDELLALLAVELFLTF------NPRGGVVKTVVSSGALDKVAKKLGIKVIR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 377 VLTGFKNVAAKIREFEkensykCIMGYEESYGCLVGDRVRDKDGIAALMLLSEAAAlykKQGLTLwdnmqnmykkygyyk 456
Cdd:cd03084 245 TKTGFKWVGEAMQEGD------VVLGGEESGGVIFPEFHPGRDGISAALLLLEILA---NLGKSL--------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 457 esqiaivlegaegaqkikdmmEDIRNNPPKEIgkYKVLKLRDysngkikdcitgetynedlpksnviyfelendfWGCIR 536
Cdd:cd03084 301 ---------------------SELFSELPRYY--YIRLKVRG---------------------------------WVLVR 324
|
410 420 430
....*....|....*....|....*....|.
gi 524608991 537 PSGTEPKIKLYMGVK-GENLEEADILVEDLR 566
Cdd:cd03084 325 ASGTEPAIRIYAEADtQEDVEQIKKEARELV 355
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
44-567 |
1.06e-43 |
|
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: 161.53 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 44 FGTAGLRGIVGVGTNRMNKYTVGKAtqgLANYIVKNNgqdkgVAIAYDSRNMSQEFSKLAALILNANGIKTYRFESLrPT 123
Cdd:TIGR03990 4 FGTSGIRGIVGEELTPELALKVGKA---FGTYLRGGK-----VVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIA-PT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 124 PELSYTVRELGCISGIVITASHNPPKYNGYKVYWEDGAQISAPVDAgiteevnaiknysDIKEITEEEATEKGLYNTIGE 203
Cdd:TIGR03990 75 PTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEE-------------EIEEIAESGDFERADWDEIGT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 204 EIDNKYI--EYLKSIALNKEIDKEYGKDIKIVYTPLHGTGKKLALRILNELGftnVHIVKEQAEPDGRFPtvsYPNPE-D 280
Cdd:TIGR03990 142 VTSDEDAidDYIEAILDKVDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELG---CKVITLNCQPDGTFP---GRNPEpT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 281 PAAFELALKFAKEIQADIVVANDPDADRIGLhVRDskTGDYIlfNGNMIGLTVADYLInqKREKGLLDKNVAliktivSS 360
Cdd:TIGR03990 216 PENLKDLSALVKATGADLGIAHDGDADRLVF-IDE--KGRFI--GGDYTLALFAKYLL--EHGGGKVVTNVS------SS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 361 NMTDKICEENGVKLFEVLTGFKNVAAKIREfekensYKCIMGYEESYGCLVGDRVRDKDGI--AALML---------LSE 429
Cdd:TIGR03990 283 RAVEDVAERHGGEVIRTKVGEVNVAEKMKE------EGAVFGGEGNGGWIFPDHHYCRDGLmaAALFLellaeegkpLSE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 430 AAAlykkqgltlwdnmqnMYKKYGYYKESqiaIVLEGaegaQKIKDMMEDIRnnppKEIGKYKVLKLrdysngkikDCIT 509
Cdd:TIGR03990 357 LLA---------------ELPKYPMSKEK---VELPD----EDKEEVMEAVE----EEFADAEIDTI---------DGVR 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 524608991 510 getynedlpksnvIYFElenDFWGCIRPSGTEPKIKLYmgVKGENLEEADILVEDLRN 567
Cdd:TIGR03990 402 -------------IDFE---DGWVLVRPSGTEPIVRIY--AEAKTEERAEELLEEGRS 441
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
44-567 |
5.46e-43 |
|
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: 159.27 E-value: 5.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 44 FGTAGLRGIVGVGTNRMNKYTVGKAtqgLANYivknnGQDKGVAIAYDSRNMSQEFSKLAALILNANGIKTYRFESLrPT 123
Cdd:cd03087 2 FGTSGIRGVVGEELTPELALKVGKA---LGTY-----LGGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIV-PT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 124 PELSYTVRELGcISGIVITASHNPPKYNGYKVYWEDGAQISAPVDAGITeevnaiknysdikEITEEEATEKGLYNTIGE 203
Cdd:cd03087 73 PALQYAVRKLG-DAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIE-------------EIIFSERFRRVAWDEVGS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 204 EIDNKYI--EYLKSIAlnKEIDKEYGKDIKIVYTPLHGTGKKLALRILNELGftnVHIVKEQAEPDGRFPTvsyPNPE-D 280
Cdd:cd03087 139 VRREDSAidEYIEAIL--DKVDIDGGKGLKVVVDCGNGAGSLTTPYLLRELG---CKVITLNANPDGFFPG---RPPEpT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 281 PAAFELALKFAKEIQADIVVANDPDADRIGlhVRDSKtGDYIlfNGNMIGLTVADYlinqkrekgLLDKNVALIKTIVSS 360
Cdd:cd03087 211 PENLSELMELVRATGADLGIAHDGDADRAV--FVDEK-GRFI--DGDKLLALLAKY---------LLEEGGGKVVTPVDA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 361 NMT-DKICEENGVKLFEVLTGFKNVAAKIREfekensYKCIMGYEESYGCLVGDRVRDKDGIAALMLLSEAAALYKKQGl 439
Cdd:cd03087 277 SMLvEDVVEEAGGEVIRTPVGDVHVAEEMIE------NGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLAEEKPLS- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 440 TLWDNMqnmyKKYGYYKESqiaIVLEGAEGAqkikDMMEDIRnnppkeigkykvlklrdysngkikdcitgETYNEDLPK 519
Cdd:cd03087 350 ELLDEL----PKYPLLREK---VECPDEKKE----EVMEAVE-----------------------------EELSDADED 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 524608991 520 SNVIY---FELEnDFWGCIRPSGTEPKIKLYmgVKGENLEEADILVEDLRN 567
Cdd:cd03087 390 VDTIDgvrIEYE-DGWVLIRPSGTEPKIRIT--AEAKTEERAKELLEEGRS 437
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
50-546 |
1.92e-37 |
|
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: 143.81 E-value: 1.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 50 RGIVGVGTNRMNKYTVGKAtqgLANYIVKNNGQDkgVAIAYDSRNMSQEFSklAALI--LNANGIKTYRFEsLRPTPELS 127
Cdd:cd03089 8 RGIAGEELTEEIAYAIGRA---FGSWLLEKGAKK--VVVGRDGRLSSPELA--AALIegLLAAGCDVIDIG-LVPTPVLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 128 YTVRELGCISGIVITASHNPPKYNGYKVywedgaqisapVDAGITEEVNAIKnysDIKEITEEEATEKGLYNTIGEEID- 206
Cdd:cd03089 80 FATFHLDADGGVMITASHNPPEYNGFKI-----------VIGGGPLSGEDIQ---ALRERAEKGDFAAATGRGSVEKVDi 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 207 -NKYIEYLKS-IALNKeidkeygKDIKIVYTPLHGTGKKLALRILNELGFTnvhiVKEQ-AEPDGRFPTvSYPNPEDPAA 283
Cdd:cd03089 146 lPDYIDRLLSdIKLGK-------RPLKVVVDAGNGAAGPIAPQLLEALGCE----VIPLfCEPDGTFPN-HHPDPTDPEN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 284 FElALKFA-KEIQADIVVANDPDADRIGLhVrdSKTGDYIlfNGNMI-GLTVADYLinqKREKGlldknvaliKTIV--- 358
Cdd:cd03089 214 LE-DLIAAvKENGADLGIAFDGDGDRLGV-V--DEKGEII--WGDRLlALFARDIL---KRNPG---------ATIVydv 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 359 --SSNMTDKIcEENGVKLFEVLTGFKNVAAKIREFEkensykCIMGYEES---------YGClvgDrvrdkDGI-AALML 426
Cdd:cd03089 276 kcSRNLYDFI-EEAGGKPIMWKTGHSFIKAKMKETG------ALLAGEMSghiffkdrwYGF---D-----DGIyAALRL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 427 LSEAAalykKQGLTLWDNMQNMYKkygYYKESQIAIVLEGAEGAQKIKDMMEDIRnNPPKEIgkykvlklrdysngkikD 506
Cdd:cd03089 341 LELLS----KSGKTLSELLADLPK---YFSTPEIRIPVTEEDKFAVIERLKEHFE-FPGAEI-----------------I 395
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 524608991 507 CITGETynedlpksnvIYFElenDFWGCIRPSGTEPKIKL 546
Cdd:cd03089 396 DIDGVR----------VDFE---DGWGLVRASNTEPVLVL 422
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
44-565 |
5.18e-36 |
|
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: 139.93 E-value: 5.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 44 FGTAGLRGIVGVGTNRMNKYTVGKAtqgLANYIVKNNGQDKgVAIAYDSRNMSQEFSklAALI--LNANGIKTYRFESLr 121
Cdd:cd05802 2 FGTDGIRGVANEPLTPELALKLGRA---AGKVLGKGGGRPK-VLIGKDTRISGYMLE--SALAagLTSAGVDVLLLGVI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 122 PTPELSYTVRELGCISGIVITASHNPPKYNGYKVYWEDGAQISapvDAgiTEEvnAIKNYSDIKEITEEEATEKGLYNTI 201
Cdd:cd05802 75 PTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLP---DE--VEE--EIEALIDKELELPPTGEKIGRVYRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 202 GEEIDnKYIEYLKSIalnkeIDKEYGKDIKIVYTPLHGTGKKLALRILNELGftnVHIVKEQAEPDGRfptvsypN---- 277
Cdd:cd05802 148 DDARG-RYIEFLKST-----FPKDLLSGLKIVLDCANGAAYKVAPEVFRELG---AEVIVINNAPDGL-------Ninvn 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 278 -----PEdpaafELAlKFAKEIQADIVVANDPDADRIgLHVrDSK----TGDYILFngnMIGLtvadYLinqkREKGLLD 348
Cdd:cd05802 212 cgsthPE-----SLQ-KAVLENGADLGIAFDGDADRV-IAV-DEKgnivDGDQILA---ICAR----DL----KERGRLK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 349 KNvalikTIVS---SNMT-DKICEENGVKLFEVLTGFKNVAAKIREfekensYKCIMGYEESYGCLVGDRVRDKDGI-AA 423
Cdd:cd05802 273 GN-----TVVGtvmSNLGlEKALKELGIKLVRTKVGDRYVLEEMLK------HGANLGGEQSGHIIFLDHSTTGDGLlTA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 424 LMLLSEAaalyKKQGLTLwDNMQNMYKKYgyykesqiaivlegaegAQKikdmMEDIRNNPPKEIGKYKvlklrdysngK 503
Cdd:cd05802 342 LQLLAIM----KRSGKSL-SELASDMKLY-----------------PQV----LVNVRVKDKKALLENP----------R 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 524608991 504 IKDCItgETYNEDLPKSNVIYfelendfwgcIRPSGTEPKIKLyMgVKGENLEEADILVEDL 565
Cdd:cd05802 386 VQAAI--AEAEKELGGEGRVL----------VRPSGTEPLIRV-M-VEGEDEELVEKLAEEL 433
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
48-563 |
1.05e-29 |
|
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: 122.03 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 48 GLRGIVGVGTN--RMNKYTVGKATqglanyIVKNNGQDKGVAIAYDSRNMSQEFSKLAALILNANGIKTYRFEsLRPTPE 125
Cdd:cd05803 6 GIRGIVGEGLTpeVITRYVAAFAT------WQPERTKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLG-IAPTPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 126 LSYTVRELGCISGIVITASHNPPKYNGYKVYWEDGAQISApvdagiteevnaiKNYSDIKEITEEEATEKGLYNTIGE-- 203
Cdd:cd05803 79 VQVLVRQSQASGGIIITASHNPPQWNGLKFIGPDGEFLTP-------------DEGEEVLSCAEAGSAQKAGYDQLGEvt 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 204 EIDNKYIEYLKSIALNKEID--KEYGKDIKIVYTPLHGTGKKLALRILNELGftnVHIVKEQAEPDGRFPTVSYPNPEDP 281
Cdd:cd05803 146 FSEDAIAEHIDKVLALVDVDviKIRERNFKVAVDSVNGAGGLLIPRLLEKLG---CEVIVLNCEPTGLFPHTPEPLPENL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 282 AAFELALKFAKeiqADIVVANDPDADRIGLhvrdsktgdyILFNGNMIG--LTVA---DYLINQKREKGLLDKNVAlikt 356
Cdd:cd05803 223 TQLCAAVKESG---ADVGFAVDPDADRLAL----------VDEDGRPIGeeYTLAlavDYVLKYGGRKGPVVVNLS---- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 357 ivSSNMTDKICEENGVKLFEVLTGFKNVAAKIREfekensYKCIMGYEESYGCLVGDRVRDKDGIAAlmllseaaalykk 436
Cdd:cd05803 286 --TSRALEDIARKHGVPVFRSAVGEANVVEKMKE------VDAVIGGEGNGGVILPDVHYGRDSLVG------------- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 437 qgltlwdnmqnmykkygyykesqIAIVLEG-AEGAQKIKDMMEDIrnnPPKEIGKYKVlKLRDYSNGKIKDCITGETYNE 515
Cdd:cd05803 345 -----------------------IALVLQLlAASGKPLSEIVDEL---PQYYISKTKV-TIAGEALERLLKKLEAYFKDA 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 524608991 516 DLPKSNVIYFELEnDFWGCIRPSGTEPKIKLYmgVKGENLEEADILVE 563
Cdd:cd05803 398 EASTLDGLRLDSE-DSWVHVRPSNTEPIVRII--AEAPTQDEAEALAD 442
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
44-547 |
2.05e-29 |
|
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: 121.97 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 44 FGTAGLRGIVGVGTnrMNKYTVGKATQGLANYiVKNNGQDKGVAIAYDSRNMSqEFSKLAAL-ILNANGIKTYRFESLR- 121
Cdd:cd05801 23 FGTSGHRGSSLKGS--FNEAHILAISQAICDY-RKSQGITGPLFLGKDTHALS-EPAFISALeVLAANGVEVIIQQNDGy 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 122 -PTPELSYTV------RELGCISGIVITASHNPPKYNGYKVYWEDGAqisaPVDAGITEEV----NAI--KNYSDIKEIT 188
Cdd:cd05801 99 tPTPVISHAIltynrgRTEGLADGIVITPSHNPPEDGGFKYNPPHGG----PADTDITRWIekraNALlaNGLKGVKRIP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 189 EEEATEKGlyNTIGEEIDNKYIEYLKSIaLNKEIDKEYGkdIKIVYTPLHGTGKKLALRILNELGFtNVHIVKEQAEPDG 268
Cdd:cd05801 175 LEAALASG--YTHRHDFVTPYVADLGNV-IDMDAIRKSG--LRLGVDPLGGASVPYWQPIAEKYGL-NLTVVNPKVDPTF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 269 RFPTVSYP-----NPEDPAAFE--LALKFakeiQADIVVANDPDADRIGLHVRDSKtgdyiLFNGNMIgLTVA-DYLINQ 340
Cdd:cd05801 249 RFMTLDHDgkirmDCSSPYAMAglLKLKD----KFDLAFANDPDADRHGIVTPSAG-----LMNPNHY-LSVAiDYLFTH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 341 kREkgLLDKNVALIKTIVSSNMTDKICEENGVKLFEVLTGFKNVAAKIreFEKENSYkcimGYEESYGCLVGDR-----V 415
Cdd:cd05801 319 -RP--LWNKSAGVGKTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDGL--LDGSLGF----GGEESAGASFLRRdgtvwT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 416 RDKDGIAALMLLSEAAAlykKQGLTLWDNMQNMYKKYG--YYKESQIAIVLEGAE-----GAQKIK------DMMEDIRN 482
Cdd:cd05801 390 TDKDGIIMCLLAAEILA---VTGKDPGQLYQELTERFGepYYARIDAPATPEQKArlkklSPEQVTatelagDPILAKLT 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524608991 483 NPP---KEIGKYKVLKlrdySNGkikdcitgetynedlpksnviyfelendfWGCIRPSGTEPKIKLY 547
Cdd:cd05801 467 RAPgngASIGGLKVTT----ANG-----------------------------WFAARPSGTEDVYKIY 501
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
44-565 |
6.41e-27 |
|
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also designated in MrsA and YhbF E. coli, UreC in Helicobacter pylori, and femR315 or FemD in Staphlococcus aureus. It converts glucosamine-6-phosphate to glucosamine-1-phosphate as part of the pathway toward UDP-N-acetylglucosamine for peptidoglycan and lipopolysaccharides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 130522 Cd Length: 443 Bit Score: 113.62 E-value: 6.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 44 FGTAGLRGIVGVG-TNRMNKYTVGKAtqglANYIVKNNGQDKG-VAIAYDSRNMSQEFSklAALI--LNANGIKTYRFES 119
Cdd:TIGR01455 1 FGTDGVRGRAGQEpLTAELALLLGAA----AGRVLRQGRDTAPrVVIGKDTRLSGYMLE--NALAagLNSAGVDVLLLGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 120 LrPTPELSYTVRELGCISGIVITASHNPPKYNGYKVYWEDGAQISAPVDAGITEEVNaiknysdiKEITEEEATEKGLYN 199
Cdd:TIGR01455 75 L-PTPAVAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLD--------EADPLPRPESEGLGR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 200 TIG-EEIDNKYIEYLKSiALNKEIDKeygKDIKIVYTPLHGTGKKLALRILNELGftnVHIVKEQAEPDGRfptvsypNP 278
Cdd:TIGR01455 146 VKRyPDAVGRYIEFLKS-TLPRGLTL---SGLKVVLDCANGAAYKVAPHVFRELG---AEVIAIGVEPDGL-------NI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 279 ED------PAAFELALkfaKEIQADIVVANDPDADRIgLHVrDSK----TGDYILFngnMIGLTVadylinqkREKGLLD 348
Cdd:TIGR01455 212 NDgcgsthLDALQKAV---REHGADLGIAFDGDADRV-LAV-DANgrivDGDQILY---IIARAL--------KESGELA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 349 KNvalikTIVSSNMTD----KICEENGVKLFEVLTGFKNVAAKIREFEkensYKciMGYEESYGCLVGDRVRDKDGI-AA 423
Cdd:TIGR01455 276 GN-----TVVATVMSNlgleRALEKLGLTLIRTAVGDRYVLEEMRESG----YN--LGGEQSGHIILLDYSTTGDGIvSA 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 424 LMLLseaaALYKKQGLTLWDnmqnMYKKYGYYKESQIAIVLEG----AEGAQKIKDMMEDIRnnppKEIGKykvlklrdy 499
Cdd:TIGR01455 345 LQVL----TIMKKSGSTLSE----LAAEFVPYPQTLVNVRVADrklaAAEAPAVKAAIEDAE----AELGG--------- 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 524608991 500 sNGKIkdcitgetynedlpksnviyfelendfwgCIRPSGTEPKIKLyMgVKGENLEEADILVEDL 565
Cdd:TIGR01455 404 -TGRI-----------------------------LLRPSGTEPLIRV-M-VEAADEELVQQLADTL 437
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
209-311 |
2.47e-26 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 103.14 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 209 YIEYLKSIaLNKEIDKeyGKDIKIVYTPLHGTGKKLALRILNELGFtnvHIVKEQAEPDGRFPTvSYPNPEDPAAFELAL 288
Cdd:pfam02879 2 YIDHLLEL-VDSEALK--KRGLKVVYDPLHGVGGGYLPELLKRLGC---DVVEENCEPDPDFPT-RAPNPEEPEALALLI 74
|
90 100
....*....|....*....|...
gi 524608991 289 KFAKEIQADIVVANDPDADRIGL 311
Cdd:pfam02879 75 ELVKSVGADLGIATDGDADRLGV 97
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
325-452 |
1.24e-24 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 98.68 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 325 NGNMIGLTVADYLInqkrEKGLLDKNVALIKTIVSSNMTDKICEENGVKLFEVLTGFKNVAAKIREFekensyKCIMGYE 404
Cdd:pfam02880 1 DGDQILALLAKYLL----EQGKLPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREE------GALFGGE 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 524608991 405 ESYGCLVGDRVRDKDGIAALMLLSEAAALYKKqglTLWDNMQNMYKKY 452
Cdd:pfam02880 71 ESGHIIFLDHATTKDGILAALLVLEILARTGK---SLSELLEELPEKY 115
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
122-547 |
2.08e-23 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 104.06 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 122 PTPELS-----YTVRELGCISGIVITASHNPP-----KYN----GykvywedgaqisaPVDAGITEEV----NAIKNY-- 181
Cdd:PRK07564 117 PTPAVShailkYNGRGGGLADGIVITPSHNPPedggiKYNppngG-------------PADTDVTDAIearaNELLAYgl 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 182 SDIKEITEEEATEKGlynTIgEEID--NKYIEYLKSIalnkeIDKE--YGKDIKIVYTPLHGTGKKLALRILNELGFtNV 257
Cdd:PRK07564 184 KGVKRIPLDRALASM---TV-EVIDpvADYVEDLENV-----FDFDaiRKAGLRLGVDPLGGATGPYWKAIAERYGL-DL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 258 HIVKEQAEPDGRFPTVSY-------PNPEDPAAFELALKFAkeiqADIVVANDPDADRiglhvrdsktgdyilfngNMI- 329
Cdd:PRK07564 254 TVVNAPVDPTFNFMPLDDdgkirmdCSSPYAMAGLLALKDA----FDLAFANDPDGDR------------------HGIv 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 330 ---GL--------TVADYLINQKREKGlldKNVALIKTIVSSNMTDKICEENGVKLFEVLTGFK---N--VAAKIRefek 393
Cdd:PRK07564 312 tpgGLmnpnhylaVAIAYLFHHRPGWR---AGAGVGKTLVSSAMIDRVAAKLGRKLYEVPVGFKwfvNglDDGSLG---- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 394 ensykciMGYEESYGCLVGDR-----VRDKDGIAALMLLSEAAAlykKQGLTLWDNMQNMYKKYG--YYKESQIAIVLEg 466
Cdd:PRK07564 385 -------FGGEESAGASFLRRdgsvwTTDKDGLIAVLLAAEILA---VTGKSPSEIYRELWARFGrpYYSRHDAPATPE- 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 467 aegaQKikdmmEDIRNNPPKEIGKykvlklRDYSNGKIKDCITGETYNeDLPKSNV-IYFElenDFWGCIRPSGTEPKIK 545
Cdd:PRK07564 454 ----QK-----AALRKLSPELVGA------TELAGDPIDASLTEAPGN-GAAIGGLkVVTE---NGWFAARPSGTETTYK 514
|
..
gi 524608991 546 LY 547
Cdd:PRK07564 515 IY 516
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
45-500 |
1.09e-13 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 73.92 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 45 GTAGLRGIVGVgtnRMNKYTVGKATQGLANYIVKNNGQDKGVAIAYDSRNMSQEFSKLAALILNANGIKtyRF----ESL 120
Cdd:PLN02307 26 GTSGLRKKVKV---FMQENYLANFVQALFNALPAEKVKGATLVLGGDGRYFNKEAIQIIIKIAAANGVR--RVwvgqNGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 121 RPTPELSYTVRE---LGCISGIVITASHNP--PKYN-GYKVYWEDGAqiSAP---VDA--GITEEVNAIKNYSDIKEI-- 187
Cdd:PLN02307 101 LSTPAVSAVIRErdgSKANGGFILTASHNPggPEEDfGIKYNYESGQ--PAPesiTDKiyGNTLTIKEYKMAEDIPDVdl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 188 -----TEEEATEkglyNTIGEEID--NKYIEYLKSI----ALNKEIDKEygkDIKIVYTPLHGTGKKLALRIL-NELGFT 255
Cdd:PLN02307 179 savgvTKFGGPE----DFDVEVIDpvEDYVKLMKSIfdfeLIKKLLSRP---DFTFCFDAMHGVTGAYAKRIFvEELGAP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 256 NVHIVKEQAEPD--GRFPTvsyPNpedpaafelaLKFAKEIQA--------------DIVVANDPDADRiglhvrdsktg 319
Cdd:PLN02307 252 ESSLLNCVPKEDfgGGHPD---PN----------LTYAKELVKrmglgktsygdeppEFGAASDGDGDR----------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 320 dyilfngNMI---------GLTVADYLINQKR-----EKGLldKNVAliKTIVSSNMTDKICEENGVKLFEVLTGFK--- 382
Cdd:PLN02307 308 -------NMIlgkrffvtpSDSVAIIAANAQEaipyfSGGL--KGVA--RSMPTSAALDVVAKKLNLPFFEVPTGWKffg 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 383 NVAakirefekeNSYKCIMGYEESYGClVGDRVRDKDGI-AALMLLSEAAALYK--KQG---LTLWDNMQNMYKKYG--Y 454
Cdd:PLN02307 377 NLM---------DAGKLSICGEESFGT-GSDHIREKDGIwAVLAWLSILAHKNKdvLPGgklVTVEDIVREHWATYGrnF 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 524608991 455 YKESQiaivLEG--AEGAQKIKDMMEDIRN--NPPKEIGKYKVLKLRDYS 500
Cdd:PLN02307 447 YSRYD----YENvdSEAANKMMDHLRDLVNksKKGIKYGVYTLAFADDFE 492
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
32-500 |
5.61e-13 |
|
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: 71.48 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 32 TEIKDSFYKDLEFGTAGLRgivgvgtnrmNKYTVGKATQGLANYI--VKNNGQDKGVAIA---------YDSRNMSQEFS 100
Cdd:cd03085 1 QTVPTKPYEGQKPGTSGLR----------KKVKVFQQPNYLENFVqsIFNALPPEKLKGAtlvvggdgrYYNKEAIQIII 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 101 KLAAlilnANGIKtyRF----ESLRPTPELSYTVRELGCISGIVITASHNP--P------KYNgykvyWEDGaqisAPVD 168
Cdd:cd03085 71 KIAA----ANGVG--KVvvgqNGLLSTPAVSAVIRKRKATGGIILTASHNPggPegdfgiKYN-----TSNG----GPAP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 169 AGITEEVNAI-KNYSDIKEITEEEA-------TEKGLYNTIGEEID--NKYIEYLKSI----ALNKEIDKeygKDIKIVY 234
Cdd:cd03085 136 ESVTDKIYEItKKITEYKIADDPDVdlskigvTKFGGKPFTVEVIDsvEDYVELMKEIfdfdAIKKLLSR---KGFKVRF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 235 TPLHGTGKKLALRIL-NELGFTNVHIVKEQAEPD--GRFPTvsyPNpedpaafelaLKFAKEIQA-------DIVVANDP 304
Cdd:cd03085 213 DAMHGVTGPYAKKIFvEELGAPESSVVNCTPLPDfgGGHPD---PN----------LTYAKDLVElmksgepDFGAASDG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 305 DADRiglhvrdsktgdyilfngNMI---GLTV---------ADY--LINQKREKGLldKNVAliKTIVSSNMTDKICEEN 370
Cdd:cd03085 280 DGDR------------------NMIlgkGFFVtpsdsvaviAANakLIPYFYKGGL--KGVA--RSMPTSGALDRVAKKL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 371 GVKLFEVLTGFK---NV--AAKIrefekensykCIMGyEESYGclVG-DRVRDKDGI-AALMLLSEAAalYKKQglTLWD 443
Cdd:cd03085 338 GIPLFETPTGWKffgNLmdAGKL----------SLCG-EESFG--TGsDHIREKDGLwAVLAWLSILA--HRNV--SVED 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524608991 444 NMQNMYKKYG------Y-YKESQiaivlegAEGAQKI----KDMMEDIRNNPPKEIGKYKVLKLRDYS 500
Cdd:cd03085 401 IVKEHWQKYGrnfytrYdYEEVD-------SEAANKMmdhlRALVSDLPGVGKSGDKGYKVAKADDFS 461
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
44-441 |
4.29e-12 |
|
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: 68.38 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 44 FGTAGLRGIVGvgtnRMNKYTVGKATQGLANYIvKNNGQDKGVAIAYDSRNMSQEFSKLAALILNANGIKTYRFESLrPT 123
Cdd:cd03088 2 FGTSGLRGLVT----DLTDEVCYAYTRAFLQHL-ESKFPGDTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAV-PT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 124 PELSYTVRELGCISgIVITASHNPPKYNGYKVYWEDGaQISAPVDAGITEEVNAIKNYSDIKEITEEEATEKGLYNTIge 203
Cdd:cd03088 76 PALALYAMKRGAPA-IMVTGSHIPADRNGLKFYRPDG-EITKADEAAILAALVELPEALFDPAGALLPPDTDAADAYI-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 204 eidNKYIEYLKSIALNkeidkeyGKDIKiVYTplH-GTGKKLALRILNELGftnvhivkeqAE--PDGR---FPTVsypN 277
Cdd:cd03088 152 ---ARYTDFFGAGALK-------GLRIG-VYQ--HsSVGRDLLVRILEALG----------AEvvPLGRsdtFIPV---D 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 278 PE--DPAAFELALKFAKEIQADIVVANDPDADRiGLhVRDsKTGDYIlfNGNMIGLTVADYLinqkrekglldkNVALIK 355
Cdd:cd03088 206 TEavRPEDRALAAAWAAEHGLDAIVSTDGDGDR-PL-VAD-ETGEWL--RGDILGLLTARFL------------GADTVV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 356 TIVSSNMTdkiCEENGVKLFEVLT--GFKNVAAKIREFEKENsYKCIMGYEESYGCLVGDRVRDKDG-IAALM----LLS 428
Cdd:cd03088 269 TPVSSNSA---IELSGFFKRVVRTriGSPYVIAAMAEAAAAG-AGRVVGYEANGGFLLGSDIERNGRtLKALPtrdaVLP 344
|
410
....*....|....*
gi 524608991 429 EAAALY--KKQGLTL 441
Cdd:cd03088 345 ILAVLAaaKEAGIPL 359
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
44-308 |
1.68e-10 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 63.43 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 44 FGTAGLRGIVGVGTNRMNKYTVGKAtqgLANYIvknngQDKGVAIAYDSRNMSQEFSKLAALILNANGIKTYRFeSLRPT 123
Cdd:PRK15414 7 FKAYDIRGKLGEELNEDIAWRIGRA---YGEFL-----KPKTIVLGGDVRLTSETLKLALAKGLQDAGVDVLDI-GMSGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 124 PELSYTVRELGCISGIVITASHNPPKYNGYKVYWEDGAQISApvDAGItEEVNAIKNYSDIKEITEeeaTEKGLYNTIge 203
Cdd:PRK15414 78 EEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVREGARPISG--DTGL-RDVQRLAEANDFPPVDE---TKRGRYQQI-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 204 EIDNKYIEYLKSIalnkeIDKEYGKDIKIVYTPLHGTGKKLALRI---LNELGfTNVHIVKEQAEPDGRFPTvSYPNPED 280
Cdd:PRK15414 150 NLRDAYVDHLFGY-----INVKNLTPLKLVINSGNGAAGPVVDAIearFKALG-APVELIKVHNTPDGNFPN-GIPNPLL 222
|
250 260
....*....|....*....|....*...
gi 524608991 281 PAAFELALKFAKEIQADIVVANDPDADR 308
Cdd:PRK15414 223 PECRDDTRNAVIKHGADMGIAFDGDFDR 250
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
123-390 |
2.28e-10 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 63.15 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 123 TPELSYTVRELGCI--SGIVITASHNPPKYNGYKVYWEDGaqisapvdaGITEevnaiknySDIKEITEEEATE-KGLYN 199
Cdd:PLN02371 154 TPAMFMSTLTEREDydAPIMITASHLPYNRNGLKFFTKDG---------GLGK--------PDIKDILERAARIyKEWSD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 200 TIGEEIDNKYIEYLKSI--------ALNKEIDKEYG---------KDIKIVYTPLHGTGKKLALRILNELG---FTNVHI 259
Cdd:PLN02371 217 EGLLKSSSGASSVVCRVdfmstyakHLRDAIKEGVGhptnyetplEGFKIVVDAGNGAGGFFAEKVLEPLGadtSGSLFL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 260 vkeqaEPDGRFPTVSyPNPEDPAAFELALKFAKEIQADIVVANDPDADRIGlhVRDSkTGDYIlfNGN-MIGLTVAdylI 338
Cdd:PLN02371 297 -----EPDGMFPNHI-PNPEDKAAMSATTQAVLANKADLGIIFDTDVDRSA--VVDS-SGREI--NRNrLIALMSA---I 362
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 524608991 339 NQKREKGlldknvaliKTIV-----SSNMTDKIcEENGVKLFEVLTGFKNVAAKIRE 390
Cdd:PLN02371 363 VLEEHPG---------TTIVtdsvtSDGLTTFI-EKKGGKHHRFKRGYKNVIDKGVR 409
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
86-308 |
1.80e-09 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 59.99 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 86 VAIAYDSRNMSQEFSKLAALILNANGIKTYRFeSLRPTPELSYTVRELGCiSGIVITASHNPPKYNGYKVyWEDGAQisa 165
Cdd:PRK09542 38 VVIGHDMRDSSPELAAAFAEGVTAQGLDVVRI-GLASTDQLYFASGLLDC-PGAMFTASHNPAAYNGIKL-CRAGAK--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 166 PV--DAGITEevnaiknysdIKEITEEEATE-KGLYNTIGE-EIDNKYIEYLKSIalnkeIDKEYGKDIKIVYTPLHGTG 241
Cdd:PRK09542 112 PVgqDTGLAA----------IRDDLIAGVPAyDGPPGTVTErDVLADYAAFLRSL-----VDLSGIRPLKVAVDAGNGMG 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524608991 242 KKLALRILNELGFTnvhIVKEQAEPDGRFPTvSYPNPEDPAAFELALKFAKEIQADIVVANDPDADR 308
Cdd:PRK09542 177 GHTVPAVLGGLPIT---LLPLYFELDGTFPN-HEANPLDPANLVDLQAFVRETGADIGLAFDGDADR 239
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
122-309 |
2.62e-06 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 50.13 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 122 PTPELSYTVRELGCISGIVITASHNPPKYNGYKVYWEDGAQISAPVDAGITEEVNaiknysdiKEITEEEATEKGLYNTI 201
Cdd:PRK10887 77 PTPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELD--------KPLTCVESAELGKASRI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 202 GEEIDnKYIEYLKS-----IALNKeidkeygkdIKIVYTPLHGTGKKLALRILNELGfTNVHIVkeQAEPDGRfptvsyp 276
Cdd:PRK10887 149 NDAAG-RYIEFCKStfpneLSLRG---------LKIVVDCANGATYHIAPNVFRELG-AEVIAI--GCEPNGL------- 208
|
170 180 190
....*....|....*....|....*....|....*....
gi 524608991 277 N------PEDPAAFELALkfaKEIQADIVVANDPDADRI 309
Cdd:PRK10887 209 NindecgATDPEALQAAV---LAEKADLGIAFDGDGDRV 244
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
120-208 |
3.79e-05 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 46.57 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 120 LRPTPELSYTVRELGCISGIVITASHNPPKYNGYKVYWEDGAQISAPVDAGITEEVNAIKNySDIKEITEEEATEKGLYN 199
Cdd:PTZ00302 60 LRSFLYGGKRAKRGNKSVGVMITASHNPIQDNGVKIIDPDGGMLEESWEKICTDFANARTG-EDLVSVLMDCLTEHGIKL 138
|
....*....
gi 524608991 200 TIGEEIDNK 208
Cdd:PTZ00302 139 SNLKLDLNK 147
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
86-441 |
4.06e-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: 46.09 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 86 VAIAYDSRNMSQEFSKlaALI--LNANGIKTYRFESLrPTPELSYTVRELGCISGIVITASHNPPKYNGYKVYWEDGAQI 163
Cdd:cd05805 37 VTVSRDASRASRMLKR--ALIsgLLSTGVNVRDLGAL-PLPVARYAIRFLGASGGIHVRTSPDDPDKVEIEFFDSRGLNI 113
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 164 SAPVDAGItEEVNAIKNYSdikeitEEEATEKGLYNTIGEEIDNkYIEYLKSiALNKEIDKEYGKDIKIVYtpLHGTGKK 243
Cdd:cd05805 114 SRAMERKI-ENAFFREDFR------RAHVDEIGDITEPPDFVEY-YIRGLLR-ALDTSGLKKSGLKVVIDY--AYGVAGI 182
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 244 LALRILNELGFTNVhIVKEQAEPDgrfptVSYPNPEDPAAFELALKFAKEIQADIVVANDPDADRIGLhVRDSktGDYIL 323
Cdd:cd05805 183 VLPGLLSRLGCDVV-ILNARLDED-----APRTDTERQRSLDRLGRIVKALGADFGVIIDPNGERLIL-VDEA--GRVIS 253
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524608991 324 fngnMIGLTVADYLINQKREKGlldKNVALikTIVSSNMTDKICEENGVKLFEVLTGFKNVAAKIREfekensyKCIMGY 403
Cdd:cd05805 254 ----DDLLTALVSLLVLKSEPG---GTVVV--PVTAPSVIEQLAERYGGRVIRTKTSPQALMEAALE-------NVVLAG 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 524608991 404 EESYGCLVGDRVRDKDGIAALMLLSEAAAlykKQGLTL 441
Cdd:cd05805 318 DGDGGFIFPEFHPGFDAIAALVKILEMLA---RTNISL 352
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| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
138-177 |
1.59e-03 |
|
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: 41.43 E-value: 1.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 524608991 138 GIVITASHNPPKYNGYKVYWEDGAQISAPVDAGITEEVNA 177
Cdd:cd03086 38 GVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANA 77
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