|
Name |
Accession |
Description |
Interval |
E-value |
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
40-566 |
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: 690.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 40 DLSFGTGGIRGVAGLGTNRINKYTIAKATEGLSNYLIHNFKE-KGISVAIAYDCRNDSLDFAKKASEVLCSHGIRVYIFS 118
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDaKNRGVVIGYDSRHNSREFAELTAAVLAANGIKVYLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 119 DIMCTPILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEYIKEVEDLGCIKymdINNAKGKNLY 198
Cdd:cd05799 81 DLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIK---FEEALDSGLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 199 EFVPIEILNKYFYNVKNLTLRKDIVKnyEKNFKILYTPLHGTGNVPVRRALCEIGYNNVFVVKDQEKPNGNFPTVKYPNP 278
Cdd:cd05799 158 KYIGEEIDDAYLEAVKKLLVNPELNE--GKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKFPNP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 279 EDNKAFYASLKEAENINPDVIIATDPDCDRVGIMVRDHSTRYVALNGNELGVILTNYILSSLEEEKKIPENSVLLKTIVT 358
Cdd:cd05799 236 EEPGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGKLPKNPVIVKTIVS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 359 TDMVKNICKDYGVKVEEVLTGFKYIGEKIEEFKKNGqNKFIFGFEESYGYLFGDFVREKDGIISSALICEMALYYKSQNK 438
Cdd:cd05799 316 SELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGG-KKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAYLKAQGK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 439 NLFDVLTELYDKYGYYREKLISMEFKGEEGKNKIENIINNLRIDDsktifneeillkedyktglkinmnkkkeyinklpk 518
Cdd:cd05799 395 TLLDRLDELYEKYGYYKEKTISITFEGKEGPEKIKAIMDRLRNNP----------------------------------- 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 152935006 519 sNVLKFHLNNGTNFVIRPSGTEPKIKIYLSSV-HTTAEGAEMKINKLEK 566
Cdd:cd05799 440 -NVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVgKKTLEEAEKKLDALKK 487
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
43-572 |
1.67e-126 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 379.16 E-value: 1.67e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 43 FGTGGIRGVAGlgTNrINKYTIAKATEGLSNYLIhnfKEKGISVAIAYDCRNDSLDFAKKASEVLCSHGIRVYIFsDIMC 122
Cdd:COG1109 7 FGTDGIRGIVG--EE-LTPEFVLKLGRAFGTYLK---EKGGPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDL-GLVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 123 TPILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEYIKEVEdlgcIKYMDinnAKGKNLYEFVP 202
Cdd:COG1109 80 TPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKED----FRRAE---AEEIGKVTRIE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 203 iEILNKYFYNVKNlTLRKDIVKnyeKNFKILYTPLHGTGNVPVRRALCEIGYnNVFVVKDQekPNGNFPTVkYPNPEdNK 282
Cdd:COG1109 153 -DVLEAYIEALKS-LVDEALRL---RGLKVVVDCGNGAAGGVAPRLLRELGA-EVIVLNAE--PDGNFPNH-NPNPE-PE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 283 AFYASLKEAENINPDVIIATDPDCDRVGIMVRDHstryVALNGNELGVILTNYILSSleeekkiPENSVLLKTIVTTDMV 362
Cdd:COG1109 223 NLEDLIEAVKETGADLGIAFDGDADRLGVVDEKG----RFLDGDQLLALLARYLLEK-------GPGGTVVVTVMSSLAL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 363 KNICKDYGVKVEEVLTGFKYIGEKIEEfkkngqNKFIFGFEESYGYLFGDFVREKDGIISSALICEMAlyyKSQNKNlfd 442
Cdd:COG1109 292 EDIAEKHGGEVVRTKVGFKYIKEKMRE------TGAVLGGEESGGIIFPDFVPTDDGILAALLLLELL---AKQGKS--- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 443 vLTELYDKYGYYREKLISMEFKGEEgknKIENIINNLRiddsktifneeillkedyktglkinmnKKKEYINKLPKSNVL 522
Cdd:COG1109 360 -LSELLAELPRYPQPEINVRVPDEE---KIGAVMEKLR---------------------------EAVEDKEELDTIDGV 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 152935006 523 KFHLNNGTNFVIRPSGTEPKIKIYLSSvhTTAEGAEMKINKLEKNIKNMI 572
Cdd:COG1109 409 KVDLEDGGWVLVRPSGTEPLLRVYAEA--KDEEEAEELLAELAELVEEAL 456
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
20-564 |
1.14e-125 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 381.34 E-value: 1.14e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 20 EKEQLKNIDDEQEIKDRFYKDLSFGTGGIRGVAGLGTNRINKYTIAKATEGLSNYLIHNF----KEKGIsvAIAYDCRND 95
Cdd:PTZ00150 24 EIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIETFgqalKSRGV--VIGYDGRYH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 96 SLDFAKKASEVLCSHGIRVYIFSDIMCTPILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEYI 175
Cdd:PTZ00150 102 SRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 176 KEVEDLGCIKYMDINNAKGKNLYEfvpiEILNKYFynvKNLTLRKDIVKNYEKNFKILYTPLHGTGNVPVRRALCEIGYN 255
Cdd:PTZ00150 182 LSNLEPWSSSWEYLTETLVEDPLA----EVSDAYF---ATLKSEYNPACCDRSKVKIVYTAMHGVGTRFVQKALHTVGLP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 256 NVFVVKDQEKPNGNFPTVKYPNPEDNK-AFYASLKEAENINPDVIIATDPDCDRVGIMVRdHSTRYVALNGNELGVILTN 334
Cdd:PTZ00150 255 NLLSVAQQAEPDPEFPTVTFPNPEEGKgALKLSMETAEAHGSTVVLANDPDADRLAVAEK-LNNGWKIFTGNELGALLAW 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 335 YiLSSLEEEKKIP-ENSVLLKTIVTTDMVKNICKDYGVKVEEVLTGFKYIGEKIEEFKKNGQNKFIFGFEESYGYLFGDF 413
Cdd:PTZ00150 334 W-AMKRYRRQGIDkSKCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIELNAENGLTTLFAYEEAIGFMLGTR 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 414 VREKDGIISSALICEMALYYKSQNKNLFDVLTELYDKYGYYREK---LISMEfkgeegKNKIENIINNLRIDDS--KTIF 488
Cdd:PTZ00150 413 VRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYHFTNnsyYICYD------PSRIVSIFNDIRNNGSypTKLG 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152935006 489 NEEILLKEDYKTGLKINMNKKKEYINKLPKSNVLKFHLNNGTNFVIRPSGTEPKIKIYLSSVHTTAEGAEMKINKL 564
Cdd:PTZ00150 487 GYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLKWYAELSGTKDEAVEKELAAL 562
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
43-558 |
5.09e-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: 159.60 E-value: 5.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 43 FGTGGIRGVAGLGTNRINKYTIAKAtegLSNYLihnfkeKGISVAIAYDCRNDSLDFAKKASEVLCSHGIRVyIFSDIMC 122
Cdd:TIGR03990 4 FGTSGIRGIVGEELTPELALKVGKA---FGTYL------RGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDV-VDLGIAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 123 TPILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEYI-------KEVEDLGCIKYMDinnakgk 195
Cdd:TIGR03990 74 TPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAesgdferADWDEIGTVTSDE------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 196 nlyefvpiEILNKYFYNVKNLTlrkDIVKNYEKNFKILYTPLHGTGNVPVRRALCEIGyNNVFVVKDQekPNGNFPtvkY 275
Cdd:TIGR03990 147 --------DAIDDYIEAILDKV---DVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELG-CKVITLNCQ--PDGTFP---G 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 276 PNPEDNKAFYASLKEA-ENINPDVIIATDPDCDRvgIMVRDHSTRYValNGNELGVILTNYILssleEEKKipensvllK 354
Cdd:TIGR03990 210 RNPEPTPENLKDLSALvKATGADLGIAHDGDADR--LVFIDEKGRFI--GGDYTLALFAKYLL----EHGG--------G 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 355 TIVTT----DMVKNICKDYGVKVEEVLTGFKYIGEKIEEfkkngqNKFIFGFEESYGYLFGDFVREKDGIISSALICEMA 430
Cdd:TIGR03990 274 KVVTNvsssRAVEDVAERHGGEVIRTKVGEVNVAEKMKE------EGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 431 LYYksqNKNLFDVLTElYDKYGYYREKLismEFKGEEGKNKIENIINNLRIDDSKTIfneeillkeDyktGLKINMnkkk 510
Cdd:TIGR03990 348 AEE---GKPLSELLAE-LPKYPMSKEKV---ELPDEDKEEVMEAVEEEFADAEIDTI---------D---GVRIDF---- 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 152935006 511 eyinklPKSNVLkfhlnngtnfvIRPSGTEPKIKIYLSSvhTTAEGAE 558
Cdd:TIGR03990 405 ------EDGWVL-----------VRPSGTEPIVRIYAEA--KTEERAE 433
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
40-179 |
1.15e-40 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 143.90 E-value: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 40 DLSFGTGGIRGVAGLGTNriNKYTIAKATEGLSNYLIHnfKEKGISVAIAYDCRNDSLDFAKKASEVLCSHGIRVYIFsD 119
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGEL--TPEFALKLGQAIASYLRA--QGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILL-G 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 120 IMCTPILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEYIKEVE 179
Cdd:pfam02878 76 LLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKED 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
40-566 |
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: 690.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 40 DLSFGTGGIRGVAGLGTNRINKYTIAKATEGLSNYLIHNFKE-KGISVAIAYDCRNDSLDFAKKASEVLCSHGIRVYIFS 118
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDaKNRGVVIGYDSRHNSREFAELTAAVLAANGIKVYLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 119 DIMCTPILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEYIKEVEDLGCIKymdINNAKGKNLY 198
Cdd:cd05799 81 DLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIK---FEEALDSGLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 199 EFVPIEILNKYFYNVKNLTLRKDIVKnyEKNFKILYTPLHGTGNVPVRRALCEIGYNNVFVVKDQEKPNGNFPTVKYPNP 278
Cdd:cd05799 158 KYIGEEIDDAYLEAVKKLLVNPELNE--GKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKFPNP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 279 EDNKAFYASLKEAENINPDVIIATDPDCDRVGIMVRDHSTRYVALNGNELGVILTNYILSSLEEEKKIPENSVLLKTIVT 358
Cdd:cd05799 236 EEPGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGKLPKNPVIVKTIVS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 359 TDMVKNICKDYGVKVEEVLTGFKYIGEKIEEFKKNGqNKFIFGFEESYGYLFGDFVREKDGIISSALICEMALYYKSQNK 438
Cdd:cd05799 316 SELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGG-KKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAYLKAQGK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 439 NLFDVLTELYDKYGYYREKLISMEFKGEEGKNKIENIINNLRIDDsktifneeillkedyktglkinmnkkkeyinklpk 518
Cdd:cd05799 395 TLLDRLDELYEKYGYYKEKTISITFEGKEGPEKIKAIMDRLRNNP----------------------------------- 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 152935006 519 sNVLKFHLNNGTNFVIRPSGTEPKIKIYLSSV-HTTAEGAEMKINKLEK 566
Cdd:cd05799 440 -NVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVgKKTLEEAEKKLDALKK 487
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
43-572 |
1.67e-126 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 379.16 E-value: 1.67e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 43 FGTGGIRGVAGlgTNrINKYTIAKATEGLSNYLIhnfKEKGISVAIAYDCRNDSLDFAKKASEVLCSHGIRVYIFsDIMC 122
Cdd:COG1109 7 FGTDGIRGIVG--EE-LTPEFVLKLGRAFGTYLK---EKGGPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDL-GLVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 123 TPILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEYIKEVEdlgcIKYMDinnAKGKNLYEFVP 202
Cdd:COG1109 80 TPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKED----FRRAE---AEEIGKVTRIE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 203 iEILNKYFYNVKNlTLRKDIVKnyeKNFKILYTPLHGTGNVPVRRALCEIGYnNVFVVKDQekPNGNFPTVkYPNPEdNK 282
Cdd:COG1109 153 -DVLEAYIEALKS-LVDEALRL---RGLKVVVDCGNGAAGGVAPRLLRELGA-EVIVLNAE--PDGNFPNH-NPNPE-PE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 283 AFYASLKEAENINPDVIIATDPDCDRVGIMVRDHstryVALNGNELGVILTNYILSSleeekkiPENSVLLKTIVTTDMV 362
Cdd:COG1109 223 NLEDLIEAVKETGADLGIAFDGDADRLGVVDEKG----RFLDGDQLLALLARYLLEK-------GPGGTVVVTVMSSLAL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 363 KNICKDYGVKVEEVLTGFKYIGEKIEEfkkngqNKFIFGFEESYGYLFGDFVREKDGIISSALICEMAlyyKSQNKNlfd 442
Cdd:COG1109 292 EDIAEKHGGEVVRTKVGFKYIKEKMRE------TGAVLGGEESGGIIFPDFVPTDDGILAALLLLELL---AKQGKS--- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 443 vLTELYDKYGYYREKLISMEFKGEEgknKIENIINNLRiddsktifneeillkedyktglkinmnKKKEYINKLPKSNVL 522
Cdd:COG1109 360 -LSELLAELPRYPQPEINVRVPDEE---KIGAVMEKLR---------------------------EAVEDKEELDTIDGV 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 152935006 523 KFHLNNGTNFVIRPSGTEPKIKIYLSSvhTTAEGAEMKINKLEKNIKNMI 572
Cdd:COG1109 409 KVDLEDGGWVLVRPSGTEPLLRVYAEA--KDEEEAEELLAELAELVEEAL 456
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
20-564 |
1.14e-125 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 381.34 E-value: 1.14e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 20 EKEQLKNIDDEQEIKDRFYKDLSFGTGGIRGVAGLGTNRINKYTIAKATEGLSNYLIHNF----KEKGIsvAIAYDCRND 95
Cdd:PTZ00150 24 EIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIETFgqalKSRGV--VIGYDGRYH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 96 SLDFAKKASEVLCSHGIRVYIFSDIMCTPILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEYI 175
Cdd:PTZ00150 102 SRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 176 KEVEDLGCIKYMDINNAKGKNLYEfvpiEILNKYFynvKNLTLRKDIVKNYEKNFKILYTPLHGTGNVPVRRALCEIGYN 255
Cdd:PTZ00150 182 LSNLEPWSSSWEYLTETLVEDPLA----EVSDAYF---ATLKSEYNPACCDRSKVKIVYTAMHGVGTRFVQKALHTVGLP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 256 NVFVVKDQEKPNGNFPTVKYPNPEDNK-AFYASLKEAENINPDVIIATDPDCDRVGIMVRdHSTRYVALNGNELGVILTN 334
Cdd:PTZ00150 255 NLLSVAQQAEPDPEFPTVTFPNPEEGKgALKLSMETAEAHGSTVVLANDPDADRLAVAEK-LNNGWKIFTGNELGALLAW 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 335 YiLSSLEEEKKIP-ENSVLLKTIVTTDMVKNICKDYGVKVEEVLTGFKYIGEKIEEFKKNGQNKFIFGFEESYGYLFGDF 413
Cdd:PTZ00150 334 W-AMKRYRRQGIDkSKCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIELNAENGLTTLFAYEEAIGFMLGTR 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 414 VREKDGIISSALICEMALYYKSQNKNLFDVLTELYDKYGYYREK---LISMEfkgeegKNKIENIINNLRIDDS--KTIF 488
Cdd:PTZ00150 413 VRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYHFTNnsyYICYD------PSRIVSIFNDIRNNGSypTKLG 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152935006 489 NEEILLKEDYKTGLKINMNKKKEYINKLPKSNVLKFHLNNGTNFVIRPSGTEPKIKIYLSSVHTTAEGAEMKINKL 564
Cdd:PTZ00150 487 GYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLKWYAELSGTKDEAVEKELAAL 562
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
43-546 |
7.12e-81 |
|
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: 261.33 E-value: 7.12e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 43 FGTGGIRGVAGLGTNRINkytIAKATEGLSNYLIHNFKEKGiSVAIAYDCRNDSLDFAKKASEVLCSHGIRVYIFSDIMC 122
Cdd:cd05800 3 FGTDGWRGIIAEDFTFEN---VRRVAQAIADYLKEEGGGGR-GVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSDRPVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 123 TPILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEYIKEVEDLGCIkymdinnAKGKNLYEFvp 202
Cdd:cd05800 79 TPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLE-------ARAEGLIET-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 203 IEILNKYFYNVKNLTlrkDIVKNYEKNFKILYTPLHGTGNVPVRRALCEIGYNNVFVVKDQEkpngnfPTVKYPNPEDNK 282
Cdd:cd05800 150 IDPKPDYLEALRSLV---DLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERD------PLFGGIPPEPIE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 283 AFYASLKEA-ENINPDVIIATDPDCDRVGIMvrDHSTRYValNGNELGVILTNYILssleeEKKIPENSVlLKTIVTTDM 361
Cdd:cd05800 221 KNLGELAEAvKEGGADLGLATDGDADRIGAV--DEKGNFL--DPNQILALLLDYLL-----ENKGLRGPV-VKTVSTTHL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 362 VKNICKDYGVKVEEVLTGFKYIGEKIEEfkkngqNKFIFGFEESYGYLFGDFVREKDGIISSALICEMALYYKsqnKNLF 441
Cdd:cd05800 291 IDRIAEKHGLPVYETPVGFKYIAEKMLE------EDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTG---KPLS 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 442 DVLTELYDKYG--YYREklismefkgeegknkieniiNNLRIDDSKtifneeillKEDYKTGLKinmNKKKEYINKLPKS 519
Cdd:cd05800 362 ELVAELEEEYGpsYYDR--------------------IDLRLTPAQ---------KEAILEKLK---NEPPLSIAGGKVD 409
|
490 500 510
....*....|....*....|....*....|..
gi 152935006 520 NV-----LKFHLNNGTNFVIRPSGTEPKIKIY 546
Cdd:cd05800 410 EVntidgVKLVLEDGSWLLIRPSGTEPLLRIY 441
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
43-558 |
1.33e-46 |
|
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: 169.29 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 43 FGTGGIRGVAGLGTNRINKYTIAKAtegLSNYLihnfkeKGISVAIAYDCRNDSLDFAKKASEVLCSHGIRVYIFsDIMC 122
Cdd:cd03087 2 FGTSGIRGVVGEELTPELALKVGKA---LGTYL------GGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDI-GIVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 123 TPILSYAVRELKcKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAE-YIKEVEDLgcikymdinnAKGKNLYEFV 201
Cdd:cd03087 72 TPALQYAVRKLG-DAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEiIFSERFRR----------VAWDEVGSVR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 202 PIEILNKYFynvknltlRKDIVKN----YEKNFKILYTPLHGTGNVPVRRALCEIGyNNVFVVKDQekPNGNFPTvkyPN 277
Cdd:cd03087 141 REDSAIDEY--------IEAILDKvdidGGKGLKVVVDCGNGAGSLTTPYLLRELG-CKVITLNAN--PDGFFPG---RP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 278 PEDNKAFYASLKEA-ENINPDVIIATDPDCDRvgIMVRDHSTRYValNGNELGVILTNYILssleEEKKipensvllKTI 356
Cdd:cd03087 207 PEPTPENLSELMELvRATGADLGIAHDGDADR--AVFVDEKGRFI--DGDKLLALLAKYLL----EEGG--------GKV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 357 VTT----DMVKNICKDYGVKVEEVLTGFKYIGEKIEEfkkngqNKFIFGFEESYGYLFGDFVREKDGIISSALICEMAly 432
Cdd:cd03087 271 VTPvdasMLVEDVVEEAGGEVIRTPVGDVHVAEEMIE------NGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELL-- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 433 ykSQNKNLFDVLTELyDKYGYYREKlisMEFKGEEGKNKIENIINNL--RIDDSKTIfneeillkeDyktGLKINmnkkk 510
Cdd:cd03087 343 --AEEKPLSELLDEL-PKYPLLREK---VECPDEKKEEVMEAVEEELsdADEDVDTI---------D---GVRIE----- 399
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 152935006 511 eyinklpksnvlkfhLNNGTnFVIRPSGTEPKIKIYLSSvhTTAEGAE 558
Cdd:cd03087 400 ---------------YEDGW-VLIRPSGTEPKIRITAEA--KTEERAK 429
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
43-558 |
5.09e-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: 159.60 E-value: 5.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 43 FGTGGIRGVAGLGTNRINKYTIAKAtegLSNYLihnfkeKGISVAIAYDCRNDSLDFAKKASEVLCSHGIRVyIFSDIMC 122
Cdd:TIGR03990 4 FGTSGIRGIVGEELTPELALKVGKA---FGTYL------RGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDV-VDLGIAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 123 TPILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEYI-------KEVEDLGCIKYMDinnakgk 195
Cdd:TIGR03990 74 TPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAesgdferADWDEIGTVTSDE------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 196 nlyefvpiEILNKYFYNVKNLTlrkDIVKNYEKNFKILYTPLHGTGNVPVRRALCEIGyNNVFVVKDQekPNGNFPtvkY 275
Cdd:TIGR03990 147 --------DAIDDYIEAILDKV---DVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELG-CKVITLNCQ--PDGTFP---G 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 276 PNPEDNKAFYASLKEA-ENINPDVIIATDPDCDRvgIMVRDHSTRYValNGNELGVILTNYILssleEEKKipensvllK 354
Cdd:TIGR03990 210 RNPEPTPENLKDLSALvKATGADLGIAHDGDADR--LVFIDEKGRFI--GGDYTLALFAKYLL----EHGG--------G 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 355 TIVTT----DMVKNICKDYGVKVEEVLTGFKYIGEKIEEfkkngqNKFIFGFEESYGYLFGDFVREKDGIISSALICEMA 430
Cdd:TIGR03990 274 KVVTNvsssRAVEDVAERHGGEVIRTKVGEVNVAEKMKE------EGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 431 LYYksqNKNLFDVLTElYDKYGYYREKLismEFKGEEGKNKIENIINNLRIDDSKTIfneeillkeDyktGLKINMnkkk 510
Cdd:TIGR03990 348 AEE---GKPLSELLAE-LPKYPMSKEKV---ELPDEDKEEVMEAVEEEFADAEIDTI---------D---GVRIDF---- 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 152935006 511 eyinklPKSNVLkfhlnngtnfvIRPSGTEPKIKIYLSSvhTTAEGAE 558
Cdd:TIGR03990 405 ------EDGWVL-----------VRPSGTEPIVRIYAEA--KTEERAE 433
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
137-460 |
4.03e-42 |
|
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: 154.82 E-value: 4.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 137 AGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEI-AEYIKEVEDLGciKYMDINNAKGknlyefvPIEILNKYFYNVKN 215
Cdd:cd03084 31 GGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIeDLAEKEDEPSA--VAYELGGSVK-------AVDILQRYFEALKK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 216 LtLRKDIVKNyeKNFKILYTPLHGTGNVPVRRALCEIGYNnvfVVKDQEKPNGNFPtVKYPNPEDNKAFYASLKEAENIN 295
Cdd:cd03084 102 L-FDVAALSN--KKFKVVVDSVNGVGGPIAPQLLEKLGAE---VIPLNCEPDGNFG-NINPDPGSETNLKQLLAVVKAEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 296 PDVIIATDPDCDRVGIMvrDHSTRYValNGNELGVILTNYILSSLEeekkipENSVLLKTIVTTDMVKNICKDYGVKVEE 375
Cdd:cd03084 175 ADFGVAFDGDADRLIVV--DENGGFL--DGDELLALLAVELFLTFN------PRGGVVKTVVSSGALDKVAKKLGIKVIR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 376 VLTGFKYIGEKIEEFkkngqnKFIFGFEESYGYLFGDFVREKDGIISSALICEMALYyksQNKNLFDVLTELYDKYgYYR 455
Cdd:cd03084 245 TKTGFKWVGEAMQEG------DVVLGGEESGGVIFPEFHPGRDGISAALLLLEILAN---LGKSLSELFSELPRYY-YIR 314
|
....*
gi 152935006 456 EKLIS 460
Cdd:cd03084 315 LKVRG 319
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
40-179 |
1.15e-40 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 143.90 E-value: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 40 DLSFGTGGIRGVAGLGTNriNKYTIAKATEGLSNYLIHnfKEKGISVAIAYDCRNDSLDFAKKASEVLCSHGIRVYIFsD 119
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGEL--TPEFALKLGQAIASYLRA--QGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILL-G 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 120 IMCTPILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEYIKEVE 179
Cdd:pfam02878 76 LLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKED 135
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
48-480 |
5.91e-31 |
|
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: 125.32 E-value: 5.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 48 IRGVAG--LGTNRInkYTIAKAteglsnyLIHNFKEKGI-SVAIAYDCRNDSLDFAKKASEVLCSHGIRVYifsDI-MC- 122
Cdd:cd03089 7 IRGIAGeeLTEEIA--YAIGRA-------FGSWLLEKGAkKVVVGRDGRLSSPELAAALIEGLLAAGCDVI---DIgLVp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 123 TPILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNqITDKEAQEIAEYIKEVEDLGCikymdinNAKGknlyEFVP 202
Cdd:cd03089 75 TPVLYFATFHLDADGGVMITASHNPPEYNGFKIVIGGGP-LSGEDIQALRERAEKGDFAAA-------TGRG----SVEK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 203 IEILNKYfynVKNLTlrkDIVKNYEKNFKILYTPLHGTGNVPVRRALCEIGYNNVFVVKDqekPNGNFPTvKYPNPEDNK 282
Cdd:cd03089 143 VDILPDY---IDRLL---SDIKLGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCE---PDGTFPN-HHPDPTDPE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 283 AFyASLKEA--ENiNPDVIIATDPDCDRVGIMvrDHSTRYValNGNELGVILTNYILssleeeKKIPENSVLLKtIVTTD 360
Cdd:cd03089 213 NL-EDLIAAvkEN-GADLGIAFDGDGDRLGVV--DEKGEII--WGDRLLALFARDIL------KRNPGATIVYD-VKCSR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 361 MVKNICKDYGVKVEEVLTGFKYIGEKIEEfkkngqNKFIFGFEESyGYLFgdFvREK-----DGIISSALICEMALYyks 435
Cdd:cd03089 280 NLYDFIEEAGGKPIMWKTGHSFIKAKMKE------TGALLAGEMS-GHIF--F-KDRwygfdDGIYAALRLLELLSK--- 346
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 152935006 436 QNKNLFDVLTELYDkygYYREKLISMEFKGEEGKNKIENIINNLR 480
Cdd:cd03089 347 SGKTLSELLADLPK---YFSTPEIRIPVTEEDKFAVIERLKEHFE 388
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
324-451 |
1.35e-30 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 115.62 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 324 NGNELGVILTNYILssleEEKKIPENSVLLKTIVTTDMVKNICKDYGVKVEEVLTGFKYIGEKIEEfkkngqNKFIFGFE 403
Cdd:pfam02880 1 DGDQILALLAKYLL----EQGKLPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMRE------EGALFGGE 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 152935006 404 ESYGYLFGDFVREKDGIISSALICEMALYYKsqnKNLFDVLTELYDKY 451
Cdd:pfam02880 71 ESGHIIFLDHATTKDGILAALLVLEILARTG---KSLSELLEELPEKY 115
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
43-568 |
9.64e-28 |
|
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: 116.04 E-value: 9.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 43 FGTGGIRGVAGLGTNRINKYTIAKAtegLSNYLIHNFKEKgiSVAIAYDCRN--DSLDFAKKASevLCSHGIRVYiFSDI 120
Cdd:cd05802 2 FGTDGIRGVANEPLTPELALKLGRA---AGKVLGKGGGRP--KVLIGKDTRIsgYMLESALAAG--LTSAGVDVL-LLGV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 121 MCTPILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEYI-------KEVEDLGCIKYMDinnak 193
Cdd:cd05802 74 IPTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIdkelelpPTGEKIGRVYRID----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 194 gknlyefvpiEILNKYFYNVKNlTLRKDIVknyeKNFKILYTPLHGTGNVPVRRALCEIGyNNVFVVKDQekPNGNfptv 273
Cdd:cd05802 149 ----------DARGRYIEFLKS-TFPKDLL----SGLKIVLDCANGAAYKVAPEVFRELG-AEVIVINNA--PDGL---- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 274 kypN---------PEdnkafyaSLKEA--ENiNPDVIIATDPDCDRVgIMVrDHstryvalNGNEL-G-VILtnYIL-SS 339
Cdd:cd05802 207 ---NinvncgsthPE-------SLQKAvlEN-GADLGIAFDGDADRV-IAV-DE-------KGNIVdGdQIL--AICaRD 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 340 LEEEKKIPENsvllkTIVTTDM----VKNICKDYGVKVEEVLTGFKYIGEKIEEfkkngqNKFIFGFEESYGYLFGDFVR 415
Cdd:cd05802 265 LKERGRLKGN-----TVVGTVMsnlgLEKALKELGIKLVRTKVGDRYVLEEMLK------HGANLGGEQSGHIIFLDHST 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 416 EKDGIISSALICEMALyyKSQNKnlfdvLTELYDKYGYYREKLIsmefkgeegknkieniinNLRIDDSKTIFNEEILLK 495
Cdd:cd05802 334 TGDGLLTALQLLAIMK--RSGKS-----LSELASDMKLYPQVLV------------------NVRVKDKKALLENPRVQA 388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152935006 496 EdyktglkinmnkKKEYINKLpksnvlkfhlnnGTNF--VIRPSGTEPKIKIylssvhtTAEGA-EMKINKLEKNI 568
Cdd:cd05802 389 A------------IAEAEKEL------------GGEGrvLVRPSGTEPLIRV-------MVEGEdEELVEKLAEEL 433
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
47-546 |
9.36e-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: 113.17 E-value: 9.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 47 GIRGVAGLGTN--RINKYTIAKATeglsnylIHNFKEKGISVAIAYDCRNDSLDFAKKASEVLCSHGIRVyIFSDIMCTP 124
Cdd:cd05803 6 GIRGIVGEGLTpeVITRYVAAFAT-------WQPERTKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDV-IDLGIAPTP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 125 ILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEyIKEVEDLGCIKYmdinnaKGKNLYEFVPiE 204
Cdd:cd05803 78 TVQVLVRQSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEGEEVLS-CAEAGSAQKAGY------DQLGEVTFSE-D 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 205 ILNKYFYNVKNLTLRkDIVKNYEKNFKILYTPLHGTGNVPVRRALCEIGynnVFVVKDQEKPNGNFPTVKYPNPEDNKAF 284
Cdd:cd05803 150 AIAEHIDKVLALVDV-DVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLG---CEVIVLNCEPTGLFPHTPEPLPENLTQL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 285 YASLKEAeniNPDVIIATDPDCDRVGIMvrDHSTRYValnGNELGVILT-NYILSSLEEEKKIPENsvllktIVTTDMVK 363
Cdd:cd05803 226 CAAVKES---GADVGFAVDPDADRLALV--DEDGRPI---GEEYTLALAvDYVLKYGGRKGPVVVN------LSTSRALE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 364 NICKDYGVKVEEvltgfKYIGEkIEEFKKNGQNKFIFGFEESYGYLFGD--FVRekDGIISSALIceMALYYKSQNKnlf 441
Cdd:cd05803 292 DIARKHGVPVFR-----SAVGE-ANVVEKMKEVDAVIGGEGNGGVILPDvhYGR--DSLVGIALV--LQLLAASGKP--- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 442 dvLTELYDKYGYYReklISmefkgeegKNKIENIINNL-RIDDskTIFNEEILLKEDYKTGLKINmnkkkeyinkLPKSN 520
Cdd:cd05803 359 --LSEIVDELPQYY---IS--------KTKVTIAGEALeRLLK--KLEAYFKDAEASTLDGLRLD----------SEDSW 413
|
490 500
....*....|....*....|....*.
gi 152935006 521 VLkfhlnngtnfvIRPSGTEPKIKIY 546
Cdd:cd05803 414 VH-----------VRPSNTEPIVRII 428
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
105-549 |
6.97e-22 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 99.44 E-value: 6.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 105 EVLCSHGIRVYIFSD--IMCTPILSYAVRELKCKA-----GIVITASHNSKEYNGYKvYN--HNG---NQITD---KEAQ 169
Cdd:PRK07564 98 EVLAANGVGVVIVGRggYTPTPAVSHAILKYNGRGggladGIVITPSHNPPEDGGIK-YNppNGGpadTDVTDaieARAN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 170 EIAEY-IKEVedlgciKYMDINNAKGKNLYEfvpieilnkyfynvknltlRKDIVKNY--------------EKNFKILY 234
Cdd:PRK07564 177 ELLAYgLKGV------KRIPLDRALASMTVE-------------------VIDPVADYvedlenvfdfdairKAGLRLGV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 235 TPLHGTGnVPVRRALCEIGYNNVFVVKDQEKPNGNFPTVKY-------PNPEdnkafYA--SLKEAENiNPDVIIATDPD 305
Cdd:PRK07564 232 DPLGGAT-GPYWKAIAERYGLDLTVVNAPVDPTFNFMPLDDdgkirmdCSSP-----YAmaGLLALKD-AFDLAFANDPD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 306 CDRVGIMvrdhsTRYVALNGNELGVILTNYILssleeeKKIP---ENSVLLKTIVTTDMVKNICKDYGVKVEEVLTGFKY 382
Cdd:PRK07564 305 GDRHGIV-----TPGGLMNPNHYLAVAIAYLF------HHRPgwrAGAGVGKTLVSSAMIDRVAAKLGRKLYEVPVGFKW 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 383 IGekieefkkNG--QNKFIFGFEESYGYLFGDF-----VREKDGIISSALICEMAlyyKSQNKNLFDVLTELYDKYG--Y 453
Cdd:PRK07564 374 FV--------NGldDGSLGFGGEESAGASFLRRdgsvwTTDKDGLIAVLLAAEIL---AVTGKSPSEIYRELWARFGrpY 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 454 Y-----------REKLISM--------EFKGEegknKIENII-----NNLRIDdsktifneeillkedyktGLKInmnkk 509
Cdd:PRK07564 443 YsrhdapatpeqKAALRKLspelvgatELAGD----PIDASLteapgNGAAIG------------------GLKV----- 495
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 152935006 510 keyinklpksnVLKfhlnNGTnFVIRPSGTEPKIKIYLSS 549
Cdd:PRK07564 496 -----------VTE----NGW-FAARPSGTETTYKIYAES 519
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
42-549 |
2.19e-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: 94.62 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 42 SFGTGGIRGVAGLGT-NRINKYTIAKAteglsnylIHNF-KEKGIS--VAIAYDCRNDSLDFAKKASEVLCSHGIRVYIF 117
Cdd:cd05801 22 AFGTSGHRGSSLKGSfNEAHILAISQA--------ICDYrKSQGITgpLFLGKDTHALSEPAFISALEVLAANGVEVIIQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 118 SD--IMCTPILSYAV-----RELKCKA-GIVITASHNSKEYNGYKvYN--HNGNQITD--KEAQEIAEYIKEvEDLGCIK 185
Cdd:cd05801 94 QNdgYTPTPVISHAIltynrGRTEGLAdGIVITPSHNPPEDGGFK-YNppHGGPADTDitRWIEKRANALLA-NGLKGVK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 186 YMDINNAKGKNLYEfvPIEILNKY---FYNVKNLtlrkDIVKNyeKNFKILYTPLHGTGnVPVRRALCEIgYN-NVFVVK 261
Cdd:cd05801 172 RIPLEAALASGYTH--RHDFVTPYvadLGNVIDM----DAIRK--SGLRLGVDPLGGAS-VPYWQPIAEK-YGlNLTVVN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 262 DQEKPNGNFPTVKYpnpeDNK---------AFYASLKEAENInpDVIIATDPDCDRVGIMVRDHSTryvaLNGNELGVIL 332
Cdd:cd05801 242 PKVDPTFRFMTLDH----DGKirmdcsspyAMAGLLKLKDKF--DLAFANDPDADRHGIVTPSAGL----MNPNHYLSVA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 333 TNYILSSLEEEKKipeNSVLLKTIVTTDMVKNICKDYGVKVEEVLTGFKYIGEKIEEfkkngqNKFIFGFEESYGYLFGD 412
Cdd:cd05801 312 IDYLFTHRPLWNK---SAGVGKTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDGLLD------GSLGFGGEESAGASFLR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 413 F-----VREKDGIISSALICEMALYYKSQNKNLFDVLTELYDKYGYYREKL-ISMEFKGeegknkienIINNLRIDD--S 484
Cdd:cd05801 383 RdgtvwTTDKDGIIMCLLAAEILAVTGKDPGQLYQELTERFGEPYYARIDApATPEQKA---------RLKKLSPEQvtA 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 152935006 485 KTIFNEEILLKEDYKTGLKINMNKkkeyinklpksnvLKFHLNNGTnFVIRPSGTEPKIKIYLSS 549
Cdd:cd05801 454 TELAGDPILAKLTRAPGNGASIGG-------------LKVTTANGW-FAARPSGTEDVYKIYAES 504
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
221-312 |
2.39e-20 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 86.19 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 221 DIVKNYEKNFKILYTPLHGTGNVPVRRALCEIGYNnvfVVKDQEKPNGNFPTvKYPNPEDNKAFYASLKEAENINPDVII 300
Cdd:pfam02879 11 DSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCD---VVEENCEPDPDFPT-RAPNPEEPEALALLIELVKSVGADLGI 86
|
90
....*....|..
gi 152935006 301 ATDPDCDRVGIM 312
Cdd:pfam02879 87 ATDGDADRLGVV 98
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
120-549 |
2.52e-09 |
|
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: 59.93 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 120 IMCTPILSYAVRELKCKAGIVITASHNS---KEYNGYKvYN-HNG----NQITDK---EAQEIAEYikevedlgciKYMD 188
Cdd:cd03085 88 LLSTPAVSAVIRKRKATGGIILTASHNPggpEGDFGIK-YNtSNGgpapESVTDKiyeITKKITEY----------KIAD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 189 INNakgknlyefVPIEILNKYFYNVKNLTLR-KDIVKNY------------------EKNFKILYTPLHGTGNVPVRRAL 249
Cdd:cd03085 157 DPD---------VDLSKIGVTKFGGKPFTVEvIDSVEDYvelmkeifdfdaikkllsRKGFKVRFDAMHGVTGPYAKKIF 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 250 C-EIGYNNVFVVKDQEKP--NGNFPTvkyPNPEDNKAFYASLKEAEninPDVIIATDPDCDRVGIMVRdhstRYVALNGN 326
Cdd:cd03085 228 VeELGAPESSVVNCTPLPdfGGGHPD---PNLTYAKDLVELMKSGE---PDFGAASDGDGDRNMILGK----GFFVTPSD 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 327 ELGVILTNYilssleeeKKIP---ENSV--LLKTIVTTDMVKNICKDYGVKVEEVLTGFKYIGEKIEEFKKNgqnkfIFG 401
Cdd:cd03085 298 SVAVIAANA--------KLIPyfyKGGLkgVARSMPTSGALDRVAKKLGIPLFETPTGWKFFGNLMDAGKLS-----LCG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 402 fEESYGyLFGDFVREKDGIIssALICEMA-LYYKsqNKNLFDVLTELYDKYG---YYR---EKLISmefkgeEGKNKien 474
Cdd:cd03085 365 -EESFG-TGSDHIREKDGLW--AVLAWLSiLAHR--NVSVEDIVKEHWQKYGrnfYTRydyEEVDS------EAANK--- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 475 IINNLRiddsKTIFNEEILLKEDYKtGLKINMNKKKEYINKLPKS----NVLKFHLNNGTNFVIRPSGTEPK---IKIYL 547
Cdd:cd03085 430 MMDHLR----ALVSDLPGVGKSGDK-GYKVAKADDFSYTDPVDGSvskkQGLRIIFEDGSRIIFRLSGTGSSgatIRLYI 504
|
..
gi 152935006 548 SS 549
Cdd:cd03085 505 ES 506
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
128-429 |
6.23e-06 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 48.79 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 128 YAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEYIKEVEDL--------GCIKYMDINNAKGKNLYE 199
Cdd:PRK15414 82 FATFHLGVDGGIEVTASHNPMDYNGMKLVREGARPISGDTGLRDVQRLAEANDFppvdetkrGRYQQINLRDAYVDHLFG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 200 FVpieilnkyfyNVKNLTLRK-----------DIVKNYEKNFKILytplhgtgNVPVRralceigynnvfVVKDQEKPNG 268
Cdd:PRK15414 162 YI----------NVKNLTPLKlvinsgngaagPVVDAIEARFKAL--------GAPVE------------LIKVHNTPDG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 269 NFPTvKYPNPEDNKAFYASLKEAENINPDVIIATDPDCDRVGIMvrdhstryvalngNELGVILTNYILSSLEEE---KK 345
Cdd:PRK15414 212 NFPN-GIPNPLLPECRDDTRNAVIKHGADMGIAFDGDFDRCFLF-------------DEKGQFIEGYYIVGLLAEaflEK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 346 IPENSVLLKTIVTTDMVKNICKDYGVKVEEVlTGFKYIGEKIEefkkngQNKFIFGFEESYGYLFGDFVREKDGIISSAL 425
Cdd:PRK15414 278 NPGAKIIHDPRLSWNTVDVVTAAGGTPVMSK-TGHAFIKERMR------KEDAIYGGEMSAHHYFRDFAYCDSGMIPWLL 350
|
....
gi 152935006 426 ICEM 429
Cdd:PRK15414 351 VAEL 354
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
43-545 |
7.34e-06 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 48.59 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 43 FGTGGIRGVAG-------------------LGTNRINKYTIAKATEgLSNYLIHNFKEKGISVAiaydcrndsldfakka 103
Cdd:PRK10887 4 FGTDGIRGKVGqapitpdfvlklgwaagkvLARQGRPKVLIGKDTR-ISGYMLESALEAGLAAA---------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 104 sevlcshGIRVYiFSDIMCTPILSYAVRELKCKAGIVITASHNSKEYNGYKVYNHNGNQITDKEAQEIAEYIK------E 177
Cdd:PRK10887 67 -------GVDVL-LTGPMPTPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELDkpltcvE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 178 VEDLGciKYMDINNAKGKnlYefvpIEILNKYFYNvkNLTLRkdivknyekNFKILYTPLHG-TGNV-PvrRALCEIGyN 255
Cdd:PRK10887 139 SAELG--KASRINDAAGR--Y----IEFCKSTFPN--ELSLR---------GLKIVVDCANGaTYHIaP--NVFRELG-A 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 256 NVFVVKDQekPNG-NFptvkypnpedNKAFYA----SLKEA--ENiNPDVIIATDPDCDRVgIMVrDHSTRYValNGNEl 328
Cdd:PRK10887 197 EVIAIGCE--PNGlNI----------NDECGAtdpeALQAAvlAE-KADLGIAFDGDGDRV-IMV-DHLGNLV--DGDQ- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 329 gvILtnYILSsleEEKKipENSVLLKTIVTTDM----VKNICKDYGVKVEEVLTGFKYIGEKIEEfkkngqNKFIFGFEE 404
Cdd:PRK10887 259 --LL--YIIA---RDRL--RRGQLRGGVVGTLMsnmgLELALKQLGIPFVRAKVGDRYVLEKLQE------KGWRLGGEN 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 405 SYGYLFGDFVREKDGIIsSALICEMALyyKSQNKNLFDVLTELYdkygYYREKLISMEFKGeEGKNKIENiinnlriDDS 484
Cdd:PRK10887 324 SGHILCLDKTTTGDGIV-AALQVLAAM--VRSGMSLADLCSGMK----LFPQVLINVRFKP-GADDPLES-------EAV 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 152935006 485 KTIFNE-EILLKEdyktglkinmnkkkeyinklpKSNVLkfhlnngtnfvIRPSGTEPKIKI 545
Cdd:PRK10887 389 KAALAEvEAELGG---------------------RGRVL-----------LRKSGTEPLIRV 418
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
135-328 |
1.26e-05 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 48.13 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 135 CKAGIVITASHNSKEYNGYKVYNHNGNqiTDKEAqeiaeyIKEVEDLGCIKYMDINNAKGKNLYEFVPIEILNKYFYNVK 214
Cdd:PLN02371 168 YDAPIMITASHLPYNRNGLKFFTKDGG--LGKPD------IKDILERAARIYKEWSDEGLLKSSSGASSVVCRVDFMSTY 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152935006 215 NLTLRKDIVK------NYEK---NFKILYTPLHGTGNVPVRRALCEIG---YNNVFVvkdqeKPNGNFPTvKYPNPEDNK 282
Cdd:PLN02371 240 AKHLRDAIKEgvghptNYETpleGFKIVVDAGNGAGGFFAEKVLEPLGadtSGSLFL-----EPDGMFPN-HIPNPEDKA 313
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 152935006 283 AFYASLKEAENINPDVIIATDPDCDRVGIMvrDHSTRyvALNGNEL 328
Cdd:PLN02371 314 AMSATTQAVLANKADLGIIFDTDVDRSAVV--DSSGR--EINRNRL 355
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
81-154 |
8.16e-04 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 42.28 E-value: 8.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 152935006 81 EKGISVAIAYDCRNDSLDFAKKASEVLCSHGIRVyIFSDIMCTPILSYAVRELKCkAGIVITASHNSKEYNGYK 154
Cdd:PRK09542 33 EGATTVVIGHDMRDSSPELAAAFAEGVTAQGLDV-VRIGLASTDQLYFASGLLDC-PGAMFTASHNPAAYNGIK 104
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
519-547 |
1.17e-03 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 37.63 E-value: 1.17e-03
10 20
....*....|....*....|....*....
gi 152935006 519 SNVLKFHLNNGTNFVIRPSGTEPKIKIYL 547
Cdd:pfam00408 23 ADAEKILGEDGRRLDVRPSGTEPVLRVMV 51
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
131-163 |
1.92e-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: 41.04 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|....
gi 152935006 131 RELKCKA-GIVITASHNSKEYNGYKVYNHNGNQI 163
Cdd:cd03086 30 KKLGGKTiGVMITASHNPVEDNGVKIVDPDGEML 63
|
|
| |
