|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
3-545 |
0e+00 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 1018.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 3 MHPRAGQKAQQEDLHNIPALVANYFLQQPDATNPDHKVLFGTSGHRGTADKSTFNENHILAIAQAVAEVRAEQGTTGPLF 82
Cdd:PRK07564 1 IHPRAGQPAQPSDLINVPRLVSAYYTLKPDPTNPFQDVKFGTSGHRGSSLQPSFNENHILAIFQAICEYRGKQGITGPLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 83 LGKDTHALSEPAFSTVIEVLVANGVEVIIQENNGFTPTPGISHAILTHNLVNDKKADGIVITPSHNPPQDGGIKYNPTHG 162
Cdd:PRK07564 81 VGGDTHALSEPAIQSALEVLAANGVGVVIVGRGGYTPTPAVSHAILKYNGRGGGLADGIVITPSHNPPEDGGIKYNPPNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 163 GPAEAELTQAIEDRANVIIAEQMQGVKRTPIAQAKQSELVKEVDLVAPYVADLVNVVDMEAIQKANIKIGVDPLGGSGID 242
Cdd:PRK07564 161 GPADTDVTDAIEARANELLAYGLKGVKRIPLDRALASMTVEVIDPVADYVEDLENVFDFDAIRKAGLRLGVDPLGGATGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 243 YWRQIGKAYNLDLTLVSEAVDPSFQFMSLDKDGVVRMDCSSPYAMAGLLALKDEYALAFGNDPDYDRHGIVTPKGLMNPN 322
Cdd:PRK07564 241 YWKAIAERYGLDLTVVNAPVDPTFNFMPLDDDGKIRMDCSSPYAMAGLLALKDAFDLAFANDPDGDRHGIVTPGGLMNPN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 323 HFLAVCIDYLYRNREGWGKDVAVGKTLVSSALIDRVVADLGRELCEVPVGFKWFVDGLYKGQFGFGGEESAGASFLRKDG 402
Cdd:PRK07564 321 HYLAVAIAYLFHHRPGWRAGAGVGKTLVSSAMIDRVAAKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESAGASFLRRDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 403 TPWSTDKDGLILCLLAAEITAVTGKNPQEYYEELAAKHGESKYNRIQAVANGAQKDVLKKLSPEMVSAETLAGDAITARL 482
Cdd:PRK07564 401 SVWTTDKDGLIAVLLAAEILAVTGKSPSEIYRELWARFGRPYYSRHDAPATPEQKAALRKLSPELVGATELAGDPIDASL 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330560947 483 THAPGNGAAIGGLKVTTENGWFAARPSGTEDIYKIYCESFKGEEHLKAIEAEAQEIVNQVFAA 545
Cdd:PRK07564 481 TEAPGNGAAIGGLKVVTENGWFAARPSGTETTYKIYAESFEGDEHLHQIQKEAQEIVADLIAA 543
|
|
| pgm |
TIGR01132 |
phosphoglucomutase, alpha-D-glucose phosphate-specific; This enzyme interconverts ... |
2-543 |
0e+00 |
|
phosphoglucomutase, alpha-D-glucose phosphate-specific; This enzyme interconverts alpha-D-glucose-1-P and alpha-D-glucose-6-P. [Energy metabolism, Sugars]
Pssm-ID: 273459 Cd Length: 543 Bit Score: 1017.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 2 AMHPRAGQKAQQEDLHNIPALVANYFLQQPDATNPDHKVLFGTSGHRGTADKSTFNENHILAIAQAVAEVRAEQGTTGPL 81
Cdd:TIGR01132 1 AIHPRAGQPAQQEDLINVAQLVAQYYVLQPEAGNAAHAVKFGTSGHRGSALRGTFNEPHILAIAQAIAEYRAAQGITGPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 82 FLGKDTHALSEPAFSTVIEVLVANGVEVIIQENNGFTPTPGISHAILTHNLVNDKKADGIVITPSHNPPQDGGIKYNPTH 161
Cdd:TIGR01132 81 YIGKDTHALSEPAFISVLEVLAANGVEVIVQENNGFTPTPAVSHAILTHNKKGEPLADGIVITPSHNPPEDGGIKYNPPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 162 GGPAEAELTQAIEDRANVIIAEQMQGVKRTPIAQAKQSELVKEVDLVAPYVADLVNVVDMEAIQKANIKIGVDPLGGSGI 241
Cdd:TIGR01132 161 GGPADTEATQAIEDRANALLANGLKGVKRLPLAQALASGTVKAHDLVQPYVDGLADIVDMAAIQKAGLRLGVDPLGGSGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 242 DYWRQIGKAYNLDLTLVSEAVDPSFQFMSLDKDGVVRMDCSSPYAMAGLLALKDEYALAFGNDPDYDRHGIVTPKGLMNP 321
Cdd:TIGR01132 241 DYWKRIAEKYNLNLTLVNPQVDPTFRFMTLDKDGKIRMDCSSPYAMAGLLALRDKYDLAFGNDPDYDRHGIVTPAGLMNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 322 NHFLAVCIDYLYRNREGWGKDVAVGKTLVSSALIDRVVADLGRELCEVPVGFKWFVDGLYKGQFGFGGEESAGASFLRKD 401
Cdd:TIGR01132 321 NHYLAVAINYLFQHRPQWGGDVAVGKTLVSSAMIDRVVADLGRQLVEVPVGFKWFVDGLFDGSFGFGGEESAGASFLRFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 402 GTPWSTDKDGLILCLLAAEITAVTGKNPQEYYEELAAKHGESKYNRIQAVANGAQKDVLKKLSPEMVSAETLAGDAITAR 481
Cdd:TIGR01132 401 GTPWSTDKDGIIMCLLAAEITAVTGKNPQQHYNELAAKFGAPSYNRIQAPATSAQKARLKKLSPEMVSATTLAGDPITAR 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330560947 482 LTHAPGNGAAIGGLKVTTENGWFAARPSGTEDIYKIYCESFKGEEHLKAIEAEAQEIVNQVF 543
Cdd:TIGR01132 481 LTAAPGNGAAIGGLKVTTDNGWFAARPSGTEDVYKIYCESFKGEEHLKQIEKEAVEIVSEVL 542
|
|
| Pgm |
COG0033 |
Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism]; |
3-545 |
0e+00 |
|
Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 439803 Cd Length: 544 Bit Score: 990.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 3 MHPRAGQKAQQEDLHNIPALVANYFLQQPDATNPDHKVLFGTSGHRGTADKSTFNENHILAIAQAVAEVRAEQGTTGPLF 82
Cdd:COG0033 1 LHPRAGQPAPPSDLIDVPRLVSAYYTIKPDPTTPFQDVKFGTSGHRGSSLKGSFNEPHILAITQAIFDYRKAQGITGPLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 83 LGKDTHALSEPAFSTVIEVLVANGVEVIIQENNGFTPTPGISHAILTHNLVNDKKADGIVITPSHNPPQDGGIKYNPTHG 162
Cdd:COG0033 81 LGGDTHALSEPAIQTALEVLAANGVGVVIVGQGGYTPTPAVSHAILKYNRGTSGAADGIVLTPSHNPPEDGGIKYNPPNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 163 GPAEAELTQAIEDRANVIIAEQMQGVKRTPIAQAKQSELVKEVDLVAPYVADLVNVVDMEAIQKANIKIGVDPLGGSGID 242
Cdd:COG0033 161 GPADEDVTDAIEARANEILEYGLADVKRVPLDRAGTAMTVEVIDPVADYVELLESVFDFDAIRAAGFRIGFDPLGGATGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 243 YWRQIGKAYNLDLTLVSEAVDPSFQFMSLDKDGVVRMDCSSPYAMAGLLALKDEYALAFGNDPDYDRHGIVTPK-GLMNP 321
Cdd:COG0033 241 YWKAIAERYGLDLTVVNGVPDPDFRFMTLDWDGGIRMDPSSPYAMASLIAGKDAPDFAAANDGDGDRHGIVTPRgGLMNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 322 NHFLAVCIDYLYRNREGWGKDVAVGKTLVSSALIDRVVADLGRELCEVPVGFKWFVDGLYKGQFGFGGEESAGASFLRKD 401
Cdd:COG0033 321 NHYLAVAIAYLFTHRPGWAALAGVGKTMVTSSAIDRVAAALGRPLYEVPVGFKWFVNGLDAGSLGFGGEESAGASFLRRD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 402 GTPWSTDKDGLILCLLAAEITAVTGKNPQEYYEELAAKHGESKYNRIQAVANGAQKDVLKKLSPEMVSAETLAGDAITAR 481
Cdd:COG0033 401 GSVWTTDKDGLWAVLLAAEILAVTGKSPAEIYRELWARFGRPYYSRHDAEATDEQKARLAKLSGEQVGATTLAGEDIFAY 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330560947 482 LTHAPGNGAAIGGLKVTTENGWFAARPSGTEDIYKIYCESFKGEEHLKAIEAEAQEIVNQVFAA 545
Cdd:COG0033 481 LDPAPGNGAAIGGLKVVTENGWFAARPSGTETTYKIYAESFEGDEHLHQIDAEAADLVDAALAL 544
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
20-539 |
0e+00 |
|
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100094 [Multi-domain] Cd Length: 522 Bit Score: 978.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 20 PALVANYFLQQPDATNPDHKVLFGTSGHRGTADKSTFNENHILAIAQAVAEVRAEQGTTGPLFLGKDTHALSEPAFSTVI 99
Cdd:cd05801 1 PRLITAYYTLKPDPSNPAQRVAFGTSGHRGSSLKGSFNEAHILAISQAICDYRKSQGITGPLFLGKDTHALSEPAFISAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 100 EVLVANGVEVIIQENNGFTPTPGISHAILTHNLVNDK-KADGIVITPSHNPPQDGGIKYNPTHGGPAEAELTQAIEDRAN 178
Cdd:cd05801 81 EVLAANGVEVIIQQNDGYTPTPVISHAILTYNRGRTEgLADGIVITPSHNPPEDGGFKYNPPHGGPADTDITRWIEKRAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 179 VIIAEQMQGVKRTPIAQAKQSELVKEVDLVAPYVADLVNVVDMEAIQKANIKIGVDPLGGSGIDYWRQIGKAYNLDLTLV 258
Cdd:cd05801 161 ALLANGLKGVKRIPLEAALASGYTHRHDFVTPYVADLGNVIDMDAIRKSGLRLGVDPLGGASVPYWQPIAEKYGLNLTVV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 259 SEAVDPSFQFMSLDKDGVVRMDCSSPYAMAGLLALKDEYALAFGNDPDYDRHGIVTPK-GLMNPNHFLAVCIDYLYRNRE 337
Cdd:cd05801 241 NPKVDPTFRFMTLDHDGKIRMDCSSPYAMAGLLKLKDKFDLAFANDPDADRHGIVTPSaGLMNPNHYLSVAIDYLFTHRP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 338 GWGKDVAVGKTLVSSALIDRVVADLGRELCEVPVGFKWFVDGLYKGQFGFGGEESAGASFLRKDGTPWSTDKDGLILCLL 417
Cdd:cd05801 321 LWNKSAGVGKTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDGLLDGSLGFGGEESAGASFLRRDGTVWTTDKDGIIMCLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 418 AAEITAVTGKNPQEYYEELAAKHGESKYNRIQAVANGAQKDVLKKLSPEMVSAETLAGDAITARLTHAPGNGAAIGGLKV 497
Cdd:cd05801 401 AAEILAVTGKDPGQLYQELTERFGEPYYARIDAPATPEQKARLKKLSPEQVTATELAGDPILAKLTRAPGNGASIGGLKV 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1330560947 498 TTENGWFAARPSGTEDIYKIYCESFKGEEHLKAIEAEAQEIV 539
Cdd:cd05801 481 TTANGWFAARPSGTEDVYKIYAESFLSEEHLKKIQKEAQEIV 522
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
42-539 |
4.81e-99 |
|
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: 307.56 E-value: 4.81e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 42 FGTSGHRGT-ADKSTFnENhILAIAQAVAEV-RAEQGTTGPLFLGKDTHALSEPAFSTVIEVLVANGVEVIIQEnnGFTP 119
Cdd:cd05800 3 FGTDGWRGIiAEDFTF-EN-VRRVAQAIADYlKEEGGGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSD--RPVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 120 TPGISHAILTHNLvndkkADGIVITPSHNPPQDGGIKYNPTHGGPAEAELTQAIEDRANVIIAEQMQGVKRTpiaqakqs 199
Cdd:cd05800 79 TPAVSWAVKKLGA-----AGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAEG-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 200 eLVKEVDLVAPYVADLVNVVDMEAIQKANIKIGVDPLGGSGIDYWRQIGKAYNLDLTLVSEAVDPSFqfmsldkdGVVRM 279
Cdd:cd05800 146 -LIETIDPKPDYLEALRSLVDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLF--------GGIPP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 280 DCSSPYAMAGLLALKDE-YALAFGNDPDYDRHGIVTPKG-LMNPNHFLAVCIDYLYRNReGWGKDVAvgKTLVSSALIDR 357
Cdd:cd05800 217 EPIEKNLGELAEAVKEGgADLGLATDGDADRIGAVDEKGnFLDPNQILALLLDYLLENK-GLRGPVV--KTVSTTHLIDR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 358 VVADLGRELCEVPVGFKWFVDGLYKGQFGFGGEESAGASFlrKDGTPwstDKDGLILCLLAAEITAVTGKNPQEYYEELA 437
Cdd:cd05800 294 IAEKHGLPVYETPVGFKYIAEKMLEEDVLIGGEESGGLGI--RGHIP---ERDGILAGLLLLEAVAKTGKPLSELVAELE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 438 AKHGESKYNRIQAVANGAQK-DVLKKLSPEmvSAETLAGDAITARLThapgngaaIGGLKVTTENG-WFAARPSGTEDIY 515
Cdd:cd05800 369 EEYGPSYYDRIDLRLTPAQKeAILEKLKNE--PPLSIAGGKVDEVNT--------IDGVKLVLEDGsWLLIRPSGTEPLL 438
|
490 500
....*....|....*....|....
gi 1330560947 516 KIYCESfKGEEHLKAIEAEAQEIV 539
Cdd:cd05800 439 RIYAEA-PSPEKVEALLDAGKKLA 461
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
41-539 |
9.36e-78 |
|
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: 248.81 E-value: 9.36e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 41 LFGTSGHRGTADKsTFNENHILAIAQAVAEVraeqgttgplflgkdthalsepafstvievlvangveviiqenngftpt 120
Cdd:cd03084 1 IFGTSGVRGVVGD-DITPETAVALGQAIGST------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 121 pgishailthnlvndkkaDGIVITPSHNPPQDGGIKYNPTHGGPAEAELTQAIEDRANVIIAEQMQGVKRTPIaqakqse 200
Cdd:cd03084 31 ------------------GGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYELGGS------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 201 lVKEVDLVAPYVADLVNVVDMEAIQKANIKIGVDPLGGSGIDYWRQIGKAYNLDLTLVSEAVDPSFqfmsldkdGVVRMD 280
Cdd:cd03084 86 -VKAVDILQRYFEALKKLFDVAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNF--------GNINPD 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 281 CSSPYAMAGLLALKDEYALAFG--NDPDYDRHGIVTPKG-LMNPNHFLAVCIDYLYRnreGWGKDVAVGKTLVSSALIDR 357
Cdd:cd03084 157 PGSETNLKQLLAVVKAEKADFGvaFDGDADRLIVVDENGgFLDGDELLALLAVELFL---TFNPRGGVVKTVVSSGALDK 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 358 VVADLGRELCEVPVGFKWFVDGLYKGQFGFGGEESAGASFLRKdgtpwSTDKDGLILCLLAAEITAVTGKNPQEYYEELa 437
Cdd:cd03084 234 VAKKLGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGVIFPEF-----HPGRDGISAALLLLEILANLGKSLSELFSEL- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 438 akhgeskynriqavangaqkdvlkklspemvsaETLAGDAITARlthapgngaaigglkvttenGWFAARPSGTEDIYKI 517
Cdd:cd03084 308 ---------------------------------PRYYYIRLKVR--------------------GWVLVRASGTEPAIRI 334
|
490 500
....*....|....*....|..
gi 1330560947 518 YCESFKgEEHLKAIEAEAQEIV 539
Cdd:cd03084 335 YAEADT-QEDVEQIKKEARELV 355
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
37-543 |
4.55e-71 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 234.71 E-value: 4.55e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 37 DHKVLFGTSGHRGTADKsTFNENHILAIAQAVAEVRAEQGTtGPLFLGKDTHALSEPAFSTVIEVLVANGVEVIiqeNNG 116
Cdd:COG1109 2 TYKKLFGTDGIRGIVGE-ELTPEFVLKLGRAFGTYLKEKGG-PKVVVGRDTRLSSPMLARALAAGLASAGIDVY---DLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 117 FTPTPGISHAILTHNlvndkkAD-GIVITPSHNPPQDGGIKYNPTHGGPAEAELTQAIEDRanviiaeqMQGVKRTPIAQ 195
Cdd:COG1109 77 LVPTPALAFAVRHLG------ADgGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEAL--------IEKEDFRRAEA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 196 AKQSELVKEVDLVAPYVADLVNVVDmEAIQKANIKIGVDPLGGSGIDYWRQIGKAYNLDLTLVSEAVDPSFQFMSLDKDg 275
Cdd:COG1109 143 EEIGKVTRIEDVLEAYIEALKSLVD-EALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNPE- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 276 vvrmdcssPYAMAGL--LALKDEYALAFGNDPDYDRHGIVTPKG-LMNPNHFLAVCIDYLYRnrEGWGKDVAvgKTLVSS 352
Cdd:COG1109 221 --------PENLEDLieAVKETGADLGIAFDGDADRLGVVDEKGrFLDGDQLLALLARYLLE--KGPGGTVV--VTVMSS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 353 ALIDRVVADLGRELCEVPVGFKWFVDGLYKGQFGFGGEESAGASFLrkdgtPWSTDKDGLILCLLAAEITAVTGKNPQEY 432
Cdd:COG1109 289 LALEDIAEKHGGEVVRTKVGFKYIKEKMRETGAVLGGEESGGIIFP-----DFVPTDDGILAALLLLELLAKQGKSLSEL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 433 YEELaakhGESKYNRIQAVANGAQKdvLKKLSPEMVSAETLAGDAITarlthapgngaaIGGLKVTTENG-WFAARPSGT 511
Cdd:COG1109 364 LAEL----PRYPQPEINVRVPDEEK--IGAVMEKLREAVEDKEELDT------------IDGVKVDLEDGgWVLVRPSGT 425
|
490 500 510
....*....|....*....|....*....|..
gi 1330560947 512 EDIYKIYCESfKGEEHLKAIEAEAQEIVNQVF 543
Cdd:COG1109 426 EPLLRVYAEA-KDEEEAEELLAELAELVEEAL 456
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
42-540 |
1.35e-51 |
|
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: 183.48 E-value: 1.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 42 FGTSGHRGT--ADKSTFNENHILAIAQAVAEVRAEQGTTGPLF---LGKDTHALSEpAFS-TVIEVLVANGVEVIIqeNN 115
Cdd:cd05799 4 FGTAGLRGKmgAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRgvvIGYDSRHNSR-EFAeLTAAVLAANGIKVYL--FD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 116 GFTPTPGISHAilthnlVNDKKAD-GIVITPSHNPPQDGGIK-YNPThGGpaeaeltQAIEDRANVIIAEqMQGV---KR 190
Cdd:cd05799 81 DLRPTPLLSFA------VRHLGADaGIMITASHNPKEYNGYKvYWED-GA-------QIIPPHDAEIAEE-IEAVlepLD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 191 TPIAQAKQSELVKEVD--LVAPYVADLVN-VVDMEAIQKANIKIGVDPLGGSGIDYWRQIGKAYNL-DLTLVSE--AVDP 264
Cdd:cd05799 146 IKFEEALDSGLIKYIGeeIDDAYLEAVKKlLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFtNVIVVEEqaEPDP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 265 SFQfmsldkdgvvrmDCSSP-------YAMAGLLALKDEYALAFGNDPDYDRHGIVTPKG-----LMNPNHFLAVCIDYL 332
Cdd:cd05799 226 DFP------------TVKFPnpeepgaLDLAIELAKKVGADLILATDPDADRLGVAVKDKdgewrLLTGNEIGALLADYL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 333 YRNREGWG---KDVAVGKTLVSSALIDRVVADLGRELCEVPVGFKW-------FVDGlyKGQFGFGGEESAGasFLRKDG 402
Cdd:cd05799 294 LEQRKEKGklpKNPVIVKTIVSSELLRKIAKKYGVKVEETLTGFKWignkieeLESG--GKKFLFGFEESIG--YLVGPF 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 403 TPwstDKDGLILCLLAAEITAV---TGKNPQEYYEELAAKHG---ESKYNRIQAVANGAQKdvlkklspemvsaetlaGD 476
Cdd:cd05799 370 VR---DKDGISAAALLAEMAAYlkaQGKTLLDRLDELYEKYGyykEKTISITFEGKEGPEK-----------------IK 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330560947 477 AITARLTHAPGNgaaiggLKVTTENG-WFAARPSGTEDIYKIYCESfKGEEHLKAIEAEAQEIVN 540
Cdd:cd05799 430 AIMDRLRNNPNV------LTFYLEDGsRVTVRPSGTEPKIKFYIEV-VGKKTLEEAEKKLDALKK 487
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
39-178 |
8.93e-43 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 149.30 E-value: 8.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 39 KVLFGTSGHRGTADKSTFNENHILAIAQAVAEVRAEQGTTGPLFLGKDTHALSEPAFSTVIEVLVANGVEVIiqeNNGFT 118
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGELTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVI---LLGLL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 119 PTPGISHAILTHNLvndkkADGIVITPSHNPPQDGGIKYNPTHGGPAEAELTQAIEDRAN 178
Cdd:pfam02878 78 PTPAVSFATRKLKA-----DGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIE 132
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
320-440 |
2.59e-37 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 133.73 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 320 NPNHFLAVCIDYLYRNREgWGKDVAVGKTLVSSALIDRVVADLGRELCEVPVGFKWFVDGLYKGQFGFGGEESAGASFLR 399
Cdd:pfam02880 1 DGDQILALLAKYLLEQGK-LPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1330560947 400 KDgtpwsTDKDGLILCLLAAEITAVTGKNPQEYYEELAAKH 440
Cdd:pfam02880 80 HA-----TTKDGILAALLVLEILARTGKSLSELLEELPEKY 115
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
41-539 |
8.90e-34 |
|
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: 133.41 E-value: 8.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 41 LFGTSGHRGTADKsTFNENHILAIAQAVAEvRAEQGTtgpLFLGKDTHALSEPAFSTVIEVLVANGVEVIiqeNNGFTPT 120
Cdd:TIGR03990 3 LFGTSGIRGIVGE-ELTPELALKVGKAFGT-YLRGGK---VVVGRDTRTSGPMLENAVIAGLLSTGCDVV---DLGIAPT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 121 PGISHAILTHNlvndkkAD-GIVITPSHNPPQDGGIK-YNPThGGPAEAELTQAIEDranviIAEQmqgvKRTPIAQ-AK 197
Cdd:TIGR03990 75 PTLQYAVRELG------ADgGIMITASHNPPEYNGIKlLNSD-GTELSREQEEEIEE-----IAES----GDFERADwDE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 198 QSELVKEVDLVAPYVADLVNVVDMEAIQKANIKIGVDPLGGSG----IDYWRQIGKAYnldLTLVSEaVDPSFqfmsldk 273
Cdd:TIGR03990 139 IGTVTSDEDAIDDYIEAILDKVDVEAIRKKGFKVVVDCGNGAGslttPYLLRELGCKV---ITLNCQ-PDGTF------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 274 dgVVRMDCSSPYAMAGLLAL--KDEYALAFGNDPDYDRHGIVTPKG-LMNPNHFLAVCIDYLYRNRegwGKDVAVgkTLV 350
Cdd:TIGR03990 208 --PGRNPEPTPENLKDLSALvkATGADLGIAHDGDADRLVFIDEKGrFIGGDYTLALFAKYLLEHG---GGKVVT--NVS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 351 SSALIDRVVADLGRELCEVPVGFKWFVDGLYKGQFGFGGEESAGASFlrkdgTPWSTDKDGLILCLLAAEITAVTGKNPQ 430
Cdd:TIGR03990 281 SSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGAVFGGEGNGGWIF-----PDHHYCRDGLMAAALFLELLAEEGKPLS 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 431 EYYEELaakhgeSKYNRIQA---VANGAQKDVLKKLspemvsAETLAGDAITArlthapgngaaIGGLKVTTENGWFAAR 507
Cdd:TIGR03990 356 ELLAEL------PKYPMSKEkveLPDEDKEEVMEAV------EEEFADAEIDT-----------IDGVRIDFEDGWVLVR 412
|
490 500 510
....*....|....*....|....*....|..
gi 1330560947 508 PSGTEDIYKIYCESfKGEEHLKAIEAEAQEIV 539
Cdd:TIGR03990 413 PSGTEPIVRIYAEA-KTEERAEELLEEGRSLV 443
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
41-539 |
1.63e-28 |
|
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100089 Cd Length: 439 Bit Score: 118.06 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 41 LFGTSGHRGTadkstFNENH----ILAIAQAVAEVRAEqgttGPLFLGKDTHALSEPAFSTVIEVLVANGVEVIiqeNNG 116
Cdd:cd03087 1 LFGTSGIRGV-----VGEELtpelALKVGKALGTYLGG----GTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVI---DIG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 117 FTPTPGISHAILTHNLVndkkadGIVITPSHNPPQDGGIK-YNPThGGPAEAELTQAIEDRanvIIAEQMQGVKRTPIAQ 195
Cdd:cd03087 69 IVPTPALQYAVRKLGDA------GVMITASHNPPEYNGIKlVNPD-GTEFSREQEEEIEEI---IFSERFRRVAWDEVGS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 196 AKQSELVKEvdlvaPYVADLVNVVDMEAiqKANIKIGVDPLGGSGIDYWRQIGKAYNLDLTLVSEAVDPSFqfmsldkdg 275
Cdd:cd03087 139 VRREDSAID-----EYIEAILDKVDIDG--GKGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFF--------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 276 VVRMDCSSPYAMAGLLALKDEYALAFG--NDPDYDRHGIVTPKG-LMNPNHFLAVCIDYLYRNRegwGKDVAVgkTLVSS 352
Cdd:cd03087 203 PGRPPEPTPENLSELMELVRATGADLGiaHDGDADRAVFVDEKGrFIDGDKLLALLAKYLLEEG---GGKVVT--PVDAS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 353 ALIDRVVADLGRELCEVPVGFKWFVDGLYKGQFGFGGEESAGasFLRKDGTPWstdKDGLILCLLAAEITAVTGKnpqeY 432
Cdd:cd03087 278 MLVEDVVEEAGGEVIRTPVGDVHVAEEMIENGAVFGGEPNGG--WIFPDHQLC---RDGIMTAALLLELLAEEKP----L 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 433 YEELAAkhgESKYNRIQA---VANGAQKDVLKKLSPEmvsAETLAGDAITarlthapgngaaIGGLKVTTENGWFAARPS 509
Cdd:cd03087 349 SELLDE---LPKYPLLREkveCPDEKKEEVMEAVEEE---LSDADEDVDT------------IDGVRIEYEDGWVLIRPS 410
|
490 500 510
....*....|....*....|....*....|
gi 1330560947 510 GTEDIYKIYCESfKGEEHLKAIEAEAQEIV 539
Cdd:cd03087 411 GTEPKIRITAEA-KTEERAKELLEEGRSKV 439
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
43-447 |
3.70e-23 |
|
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: 103.07 E-value: 3.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 43 GTSGHR---GTADKSTFNENHILAIAQAVAEVRAEQGTtgpLFLGKDTHALSEPAFSTVIEVLVANGVEVIIQENNGFTP 119
Cdd:cd03085 14 GTSGLRkkvKVFQQPNYLENFVQSIFNALPPEKLKGAT---LVVGGDGRYYNKEAIQIIIKIAAANGVGKVVVGQNGLLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 120 TPGISHAILTHNLVNdkkadGIVITPSHNP--P-QDGGIKYNPTHGGPAEAELTQAIEDRANVIIAEQMQGVKRTPIAQA 196
Cdd:cd03085 91 TPAVSAVIRKRKATG-----GIILTASHNPggPeGDFGIKYNTSNGGPAPESVTDKIYEITKKITEYKIADDPDVDLSKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 197 KQSEL------VKEVDLVAPYVADLVNVVDMEAIQKA----NIKIGVDPLGGSGIDYWRQIgkaYNLDLTLVSEAV---D 263
Cdd:cd03085 166 GVTKFggkpftVEVIDSVEDYVELMKEIFDFDAIKKLlsrkGFKVRFDAMHGVTGPYAKKI---FVEELGAPESSVvncT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 264 PSFQF--------MSLDKDGVVRMDcsspyamagllalKDEYALAFGNDPDYDRHGIVTPKGLMNPNHFLAV------CI 329
Cdd:cd03085 243 PLPDFggghpdpnLTYAKDLVELMK-------------SGEPDFGAASDGDGDRNMILGKGFFVTPSDSVAViaanakLI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 330 DYLYRNregwgKDVAVGKTLVSSALIDRVVADLGRELCEVPVGFKWFVDGLYKGQFGFGGEESAGAsflrkdGTPWSTDK 409
Cdd:cd03085 310 PYFYKG-----GLKGVARSMPTSGALDRVAKKLGIPLFETPTGWKFFGNLMDAGKLSLCGEESFGT------GSDHIREK 378
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1330560947 410 DGL--ILCLLAaeITAVTGKNPQEYYEELAAKHGESKYNR 447
Cdd:cd03085 379 DGLwaVLAWLS--ILAHRNVSVEDIVKEHWQKYGRNFYTR 416
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
43-405 |
6.16e-22 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 99.34 E-value: 6.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 43 GTSGHRGTAdkSTFNENHILA--IAQAVAEVRAEQGTTGPLFLGKDTHALSEPAFSTVIEVLVANGVEVIIQENNGFTPT 120
Cdd:PLN02307 26 GTSGLRKKV--KVFMQENYLAnfVQALFNALPAEKVKGATLVLGGDGRYFNKEAIQIIIKIAAANGVRRVWVGQNGLLST 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 121 PGISHAIltHNLVNDKKADGIVITPSHNP--P-QDGGIKYNPTHGGPAEAELTQAIEDRANVI----IAEQMQGVKRTPI 193
Cdd:PLN02307 104 PAVSAVI--RERDGSKANGGFILTASHNPggPeEDFGIKYNYESGQPAPESITDKIYGNTLTIkeykMAEDIPDVDLSAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 194 AQAKQSEL----VKEVDLVAPYVADLVNVVDMEAIQK----ANIKIGVDPLGGSGIDYWRQIgkaynldltLVSE-AVDP 264
Cdd:PLN02307 182 GVTKFGGPedfdVEVIDPVEDYVKLMKSIFDFELIKKllsrPDFTFCFDAMHGVTGAYAKRI---------FVEElGAPE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 265 SFQFMSLDKD--GVVRMDCSSPYA------MAGLLALKDEYALAFG--NDPDYDRHGIVTPKGLMNPNHFLAV------- 327
Cdd:PLN02307 253 SSLLNCVPKEdfGGGHPDPNLTYAkelvkrMGLGKTSYGDEPPEFGaaSDGDGDRNMILGKRFFVTPSDSVAIiaanaqe 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 328 CIDYLyrnrEGWGKDVAvgKTLVSSALIDRVVADLGRELCEVPVGFKWFVDGLYKGQFGFGGEES--AGASFLR-KDGtP 404
Cdd:PLN02307 333 AIPYF----SGGLKGVA--RSMPTSAALDVVAKKLNLPFFEVPTGWKFFGNLMDAGKLSICGEESfgTGSDHIReKDG-I 405
|
.
gi 1330560947 405 W 405
Cdd:PLN02307 406 W 406
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
45-542 |
9.08e-19 |
|
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: 88.90 E-value: 9.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 45 SGHRGTADKStFNENHILAIAQAVAEVRAEQGTTGPLFLGKDTHALSEPAFSTVIEVLVANGVEVIiqeNNGFTPTPGIS 124
Cdd:cd05803 5 SGIRGIVGEG-LTPEVITRYVAAFATWQPERTKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVI---DLGIAPTPTVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 125 HailthnLVNDKKADG-IVITPSHNPPQDGGIKYNPTHG---GPAEAE--LTQAIEDRANVIIAEQMQGVKRTPIAQAKQ 198
Cdd:cd05803 81 V------LVRQSQASGgIIITASHNPPQWNGLKFIGPDGeflTPDEGEevLSCAEAGSAQKAGYDQLGEVTFSEDAIAEH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 199 SELV-KEVDlvapyvadlvnvVDMEAIQKANIKIGVDPLGGSGIDYWRQIGKAynLDLTLVSEAVDPSFQFmsldkdgvV 277
Cdd:cd05803 155 IDKVlALVD------------VDVIKIRERNFKVAVDSVNGAGGLLIPRLLEK--LGCEVIVLNCEPTGLF--------P 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 278 RMDCSSPYAMAGLL-ALKDEYA-LAFGNDPDYDRHGIVTPKG-LMNPNHFLAVCIDYL--YRNREGwgkdvAVGKTLVSS 352
Cdd:cd05803 213 HTPEPLPENLTQLCaAVKESGAdVGFAVDPDADRLALVDEDGrPIGEEYTLALAVDYVlkYGGRKG-----PVVVNLSTS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 353 ALIDRVVADLGRELCEVPVGFKWFVDGLYKGQFGFGGEESAG-----ASFLRkDGTPWSTdkdgLILCLLAAE---ITAV 424
Cdd:cd05803 288 RALEDIARKHGVPVFRSAVGEANVVEKMKEVDAVIGGEGNGGvilpdVHYGR-DSLVGIA----LVLQLLAASgkpLSEI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 425 TGKNPQEYYEELAAKhgeskynriqaVANGAQKDVLKKLSPEMVSAETLAGDaitarlthapgngaaigGLKVTTENGWF 504
Cdd:cd05803 363 VDELPQYYISKTKVT-----------IAGEALERLLKKLEAYFKDAEASTLD-----------------GLRLDSEDSWV 414
|
490 500 510
....*....|....*....|....*....|....*...
gi 1330560947 505 AARPSGTEDIYKIYCESfkgeehlkAIEAEAQEIVNQV 542
Cdd:cd05803 415 HVRPSNTEPIVRIIAEA--------PTQDEAEALADRF 444
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
48-539 |
4.73e-17 |
|
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100091 Cd Length: 443 Bit Score: 83.72 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 48 RGTADKsTFNENHILAIAQAVAEVRAEQGTtGPLFLGKDTHaLSEPAFST-VIEVLVANGVEVIiqeNNGFTPTPGISHA 126
Cdd:cd03089 8 RGIAGE-ELTEEIAYAIGRAFGSWLLEKGA-KKVVVGRDGR-LSSPELAAaLIEGLLAAGCDVI---DIGLVPTPVLYFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 127 ilTHNLvndkKAD-GIVITPSHNPPQDGGIKYNpTHGGPAEAELTQAIEDRAnviiaeqmqgvKRTPIAQAKQSELVKEV 205
Cdd:cd03089 82 --TFHL----DADgGVMITASHNPPEYNGFKIV-IGGGPLSGEDIQALRERA-----------EKGDFAAATGRGSVEKV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 206 DLVAPYVADLVNVVDmeaIQKANIKIGVDPLGGSGIDYWRQIGKAYNLDLTLVSEAVDPSFqfmsldkdgvvrmDCSSPY 285
Cdd:cd03089 144 DILPDYIDRLLSDIK---LGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFpnh--------hpDPTDPE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 286 AMAGLL-ALKDEYA---LAFgnDPDYDRHGIVTPKG-LMNPNHFLAV-CIDYLYRNRegwGKDVaVGKTLVSSALIDrVV 359
Cdd:cd03089 213 NLEDLIaAVKENGAdlgIAF--DGDGDRLGVVDEKGeIIWGDRLLALfARDILKRNP---GATI-VYDVKCSRNLYD-FI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 360 ADLGRELCEVPVGFKWFVDGLYKGQFGFGGEESAGASFlrKDgtPWSTDKDGLILCLLAAEITAVTGKNPQEYYEELaAK 439
Cdd:cd03089 286 EEAGGKPIMWKTGHSFIKAKMKETGALLAGEMSGHIFF--KD--RWYGFDDGIYAALRLLELLSKSGKTLSELLADL-PK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 440 HGESKYNRIqAVANGAQKDVLKKLspemvsaetlagdaitarLTHAPGNGAAIG---GLKVTTENGWFAARPSGTEDIYK 516
Cdd:cd03089 361 YFSTPEIRI-PVTEEDKFAVIERL------------------KEHFEFPGAEIIdidGVRVDFEDGWGLVRASNTEPVLV 421
|
490 500
....*....|....*....|...
gi 1330560947 517 IYCESfKGEEHLKAIEAEAQEIV 539
Cdd:cd03089 422 LRFEA-DTEEGLEEIKAELRKLL 443
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
41-427 |
5.78e-16 |
|
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: 80.22 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 41 LFGTSGHRGTADKsTFNENHILAIAQAVAEVRAEQGTTGPLFLGKDTHaLSEPAF-STVIEVLVANGVEVIIQennGFTP 119
Cdd:cd05802 1 LFGTDGIRGVANE-PLTPELALKLGRAAGKVLGKGGGRPKVLIGKDTR-ISGYMLeSALAAGLTSAGVDVLLL---GVIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 120 TPGISHailthnLVNDKKAD-GIVITPSHNPPQDGGIK-YNptHGG---PAEAELtqAIEDRANVIIAEQMQGVKrtpIA 194
Cdd:cd05802 76 TPAVAY------LTRKLRADaGVVISASHNPFEDNGIKfFS--SDGyklPDEVEE--EIEALIDKELELPPTGEK---IG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 195 QAKQSElvkevDLVAPYVADLVNVVDMEAIQkaNIKIGVDPLGGSGidYwrQIGKA--YNLDLTLVSEAVDPsfqfmsld 272
Cdd:cd05802 143 RVYRID-----DARGRYIEFLKSTFPKDLLS--GLKIVLDCANGAA--Y--KVAPEvfRELGAEVIVINNAP-------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 273 kDGV-VRMDCSSPYAMAGLLALKDEYA---LAFgnDPDYDRHGIVTPKG-LMNPNHFLAVCIDYLyrNREGWGK-DVAVG 346
Cdd:cd05802 204 -DGLnINVNCGSTHPESLQKAVLENGAdlgIAF--DGDADRVIAVDEKGnIVDGDQILAICARDL--KERGRLKgNTVVG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 347 kTLVSSALIDRVVADLGRELCEVPVGFKWFVDGLYKGQFGFGGEESAGASFLRKdgtpwSTDKDGLILCLLAAEITAVTG 426
Cdd:cd05802 279 -TVMSNLGLEKALKELGIKLVRTKVGDRYVLEEMLKHGANLGGEQSGHIIFLDH-----STTGDGLLTALQLLAIMKRSG 352
|
.
gi 1330560947 427 K 427
Cdd:cd05802 353 K 353
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
210-317 |
3.69e-15 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 71.17 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 210 PYVADLVNVVDMEAIQKANIKIGVDPLGGSGIDYWRQIGKAYNLDLTLVSEAVDPSFQFmsldkdGVVRMDCSSPYAMAG 289
Cdd:pfam02879 1 AYIDHLLELVDSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPT------RAPNPEEPEALALLI 74
|
90 100
....*....|....*....|....*...
gi 1330560947 290 LLALKDEYALAFGNDPDYDRHGIVTPKG 317
Cdd:pfam02879 75 ELVKSVGADLGIATDGDADRLGVVDERG 102
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
42-441 |
1.53e-10 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 63.55 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 42 FGTSGHRGT--ADKSTFNENHILAIAQ----AVAEVRAEQGTTGPLFLGKDTHALSEPAFSTVIEVLVANGVEVIIqenn 115
Cdd:PTZ00150 47 FGTAGLRGKmgAGFNCMNDLTVQQTAQglcaYVIETFGQALKSRGVVIGYDGRYHSRRFAEITASVFLSKGFKVYL---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 116 gFT---PTPGISHAIlthnlVNDKKADGIVITPSHNPPQDGGIKYNPTHGG----PAEAELTQAIEDranviiaeqmqgv 188
Cdd:PTZ00150 123 -FGqtvPTPFVPYAV-----RKLKCLAGVMVTASHNPKEDNGYKVYWSNGAqiipPHDKNISAKILS------------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 189 KRTPIAQAkqSELVKEVDLVAP-------YVADLVNVVDMEAIQKANIKIGVDPLGGSGIDYWRQIGKAYNL-DLTLVSE 260
Cdd:PTZ00150 184 NLEPWSSS--WEYLTETLVEDPlaevsdaYFATLKSEYNPACCDRSKVKIVYTAMHGVGTRFVQKALHTVGLpNLLSVAQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 261 AVDPSFQFMSldkdgvVRMdcSSPYAMAGLLALKDEYALAFG------NDPDYDRHGIVTPKG----LMNPNHFLAVCID 330
Cdd:PTZ00150 262 QAEPDPEFPT------VTF--PNPEEGKGALKLSMETAEAHGstvvlaNDPDADRLAVAEKLNngwkIFTGNELGALLAW 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 331 YLYRNREGWGKD---VAVGKTLVSSALIDRVVADLGRELCEVPVGFKWFVDGLYK------GQFGFGGEESAGASFlrkd 401
Cdd:PTZ00150 334 WAMKRYRRQGIDkskCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIElnaengLTTLFAYEEAIGFML---- 409
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1330560947 402 gTPWSTDKDGLILCLLAAEIT---AVTGKNPQEYYEELAAKHG 441
Cdd:PTZ00150 410 -GTRVRDKDGVTAAAVVAEMAlylYERGKTLVEHLESLYKQYG 451
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
42-174 |
1.47e-06 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 50.90 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 42 FGTSGHRGTADKSTFNENHILAIAQAVAEVRAEQGTtgPLFL-GKDTHaLSEPAFSTVIEV-LVANGVEViiqennGFT- 118
Cdd:PRK10887 4 FGTDGIRGKVGQAPITPDFVLKLGWAAGKVLARQGR--PKVLiGKDTR-ISGYMLESALEAgLAAAGVDV------LLTg 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330560947 119 --PTPGIshAILTHNLvndkKAD-GIVITPSHNPPQDGGIKYNPTHGG--PAEAELtqAIE 174
Cdd:PRK10887 75 pmPTPAV--AYLTRTL----RAEaGIVISASHNPYYDNGIKFFSADGTklPDEVEL--AIE 127
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
140-234 |
9.08e-05 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 45.41 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 140 GIVITPSHNPPQDGGIKYNPTHGGPAEAELTQAIEDRANviiaeqmqgvkrTPIAQAKQSELVKEVDLVAPYVADLVNVV 219
Cdd:PTZ00302 78 GVMITASHNPIQDNGVKIIDPDGGMLEESWEKICTDFAN------------ARTGEDLVSVLMDCLTEHGIKLSNLKLDL 145
|
90
....*....|....*
gi 1330560947 220 DMEAIQKANIKIGVD 234
Cdd:PTZ00302 146 NKSNCSKAKVHVGRD 160
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
63-240 |
1.44e-03 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 41.20 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 63 AIAQAVAE-VRAEQGTTGP----LFLGKDTHaLSEPAFSTVIEV-LVANGVEVIiqeNNGFTPTPGISHAILTHNLVNDK 136
Cdd:PLN02371 95 AIGAAFAEwLLEKKKADGSgelrVSVGRDPR-ISGPRLADAVFAgLASAGLDVV---DMGLATTPAMFMSTLTEREDYDA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330560947 137 kadGIVITPSHNPPQDGGIKYNPTHGGPAEAELTQaIEDRANVIIAEqmQGVKRTPIAQAKQSELVKEVDLVAPYVADLV 216
Cdd:PLN02371 171 ---PIMITASHLPYNRNGLKFFTKDGGLGKPDIKD-ILERAARIYKE--WSDEGLLKSSSGASSVVCRVDFMSTYAKHLR 244
|
170 180 190
....*....|....*....|....*....|.
gi 1330560947 217 NVVDMEAIQKANI-------KIGVDPLGGSG 240
Cdd:PLN02371 245 DAIKEGVGHPTNYetplegfKIVVDAGNGAG 275
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
489-539 |
1.56e-03 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 37.25 E-value: 1.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1330560947 489 GAAIGGLKVTTENGW-FAARPSGTEDIYKIYCESfKGEEHLKAIEAEAQEIV 539
Cdd:pfam00408 20 KVFADAEKILGEDGRrLDVRPSGTEPVLRVMVEG-DSDEELARLADEIADLL 70
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
136-156 |
7.57e-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: 39.11 E-value: 7.57e-03
|
| |
